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High Blood Sugar — Are We Missing Half the Story? The Role of Reductive Stress
Reproduced from original article:
https://articles.mercola.com/sites/articles/archive/2025/03/15/high-blood-sugar-reductive-stress.aspx
Analysis by Dr. Joseph Mercola March 15, 2025
STORY AT-A-GLANCE
- High blood sugar in Type 2 diabetes overwhelms cellular machinery like a chaotic factory, creating not just oxidative stress as previously thought, but also a more fundamental problem called reductive stress. Reductive stress occurs when there’s an oversupply of electron-carrying molecules in cells, creating a “traffic jam” of electrons that can’t be processed efficiently by the mitochondria’s electron transport chain
- While traditional views focused on oxidative stress alone, scientists now understand that reductive stress actually triggers oxidative stress. It’s the initial spark that sets off a chain reaction of cellular damage in diabetic conditions
- When the main pathway for processing glucose becomes blocked due to reductive stress, sugar molecules get diverted into harmful alternative pathways, creating additional toxic byproducts and inflammation
- The combination of reductive and oxidative stress explains many serious complications of diabetes including neuropathy, retinopathy, nephropathy and cardiovascular problems — all stemming from this initial electron overload
- Understanding reductive stress offers new therapeutic possibilities. Instead of just focusing on lowering blood sugar or fighting oxidative damage after it occurs, effective treatments target the electron transport chain efficiency and/or help cells recycle NADH more effectively
Visualize a huge workshop in your body that never stops working. Every second of the day, this workshop — your cells — transforms the food you eat into the energy and building blocks you need to survive. Picture endless supplies of raw materials being delivered to this workshop. When the workshop receives exactly what it needs, it hums along smoothly, producing vital components and discarding waste at a comfortable pace.
But when it is flooded with more resources than it can handle, chaos develops that reminds you of an old “I Love Lucy” episode. Conveyor belts clog, half-finished products pile up and machines begin malfunctioning. That chaos mirrors what happens inside your cells when you have chronically high blood sugar or otherwise known as Type 2 diabetes.
Scientists once focused on how too much sugar in your bloodstream creates damage through something called oxidative stress — an onslaught of destructive, oxygen-containing molecules. While that is important, a more serious stealth problem — reductive stress — turns out to be the main problem.1 For an easy-to-understand overview of what reductive stress is, and how it’s caused, see “Redox Simplified, Part 1.”
Reductive stress was first reported in the literature just before 1990 and is only relatively recently appreciated.2 It is at least as significant as oxidative stress for explaining why your cells lose their balance under conditions of prolonged high blood sugar. Reductive stress is the hidden spark that sets off a harmful chain reaction, eventually leading to severe problems for cells, tissues and organs.
Type 2 diabetes is frequently described as a disease of “overnutrition.” People consume more caloric energy than their bodies know what to do with, so cells try to cope with that oversupply. Insulin is the hormone that helps move sugar from the bloodstream into cells for use or storage.
This sugar is primarily glucose — a simple sugar that is chemically identical to what’s sometimes called dextrose, especially when you find it as a commercially available product in a store or used in IVs. In the early stages of Type 2 diabetes, cells grow resistant to insulin’s signal, making them slow to remove excess sugar from circulation.
However, in the late 1980s, scientists began to understand that there was another, more significant explanation beyond overnutrition. They couldn’t fully explain the observed pathologies solely based on excessive nutrient intake.
While overnutrition can contribute to health problems, more commonly, we see a disruption in the cellular machinery responsible for metabolizing fuel. Essentially, the “furnaces” within cells, the mitochondria, become less efficient at burning fuel. This diminished capacity to use fuel effectively leads to a buildup of harmful byproducts and, ultimately, cellular damage.
Why Overly High Sugar Leads to Reductive Stress
Many researchers once blamed only oxidative stress for the damage caused by chronic elevated blood sugars, but the story is far more complex. A less publicized culprit called reductive stress occurs when there is an oversupply of special electron-carrying molecules in your cells.
• Too much electron-carrying molecules in your cells — One of the key carriers is NADH, which picks up electrons when sugar is broken down for energy. Ordinarily, NADH unloads its electrons in the electron transport chain (ETC) of your mitochondria. When you have too much sugar around, your metabolic pathways generate more NADH than your cells can handle. This oversupply forms a traffic jam of electrons stuck in your mitochondrial ETC.
• The impact of excess NADH — During normal metabolism, oxygen in your mitochondria eventually accepts electrons from carriers like NADH, letting ATP and water form. However, if NADH is piling up too fast or is not being recycled quickly enough, your mitochondria reach a bottleneck and start leaking electrons onto oxygen in erratic ways. That partial reaction creates a reactive oxygen species called superoxide.
• Having excess NADH causes reductive stress — This sets off a cascade that leads to excessive oxidative stress. The two stresses work hand in hand — they both push the system toward an oxidative meltdown. Realizing that they are connected helps explain many of the complications tied to long-term high blood sugar.
Cells also have backup carriers like NADPH and glutathione, which help defend against or fix routine oxidative damage. But when you have high blood sugar, these carriers are also thrown off balance, sometimes contributing further to reductive stress. So, what should be a finely tuned assembly line of electrons becomes a crowded, poorly managed factory.
How Mitochondria and Enzymes Suffer Under Excess Sugar
Under healthy conditions, most sugar flows through glycolysis and then the Krebs cycle in your mitochondria, leading to a steady generation of NADH for ATP production. In a state of chronically high blood sugar, a steady flood of sugar pours in, leading to overly high rates of NADH production.
• Influx of sugar creates electron pressure — Pancreatic beta cells and liver cells are particularly vulnerable because they possess an enzyme called glucokinase, which does not slow down as sugar accumulates. It just keeps stuffing sugar into the mill, generating more pyruvate and acetyl-CoA, and eventually too much NADH.
This leads to what some researchers call electron pressure. Think of it as building water pressure in a dam. The more NADH, the more “water” is pushing against the gates of the electron transport chain. If the gates can’t relieve that pressure quickly enough, water (electrons) spills out in harmful ways, forming superoxide and other reactive oxygen species (ROS).
• Rethinking the accepted causes of oxidative stress — Though we typically consider fat metabolism or the lack of antioxidants to be reasons for oxidative stress, it is actually an overabundance of these electron carriers, like NADH, that triggers these chains of events.
• Low oxygen consumption occurs — Low oxygen usage in cells, sometimes referred to as pseudohypoxia, can also happen under these conditions. Even though oxygen might be physically present, the cell’s ability to use that oxygen effectively stalls when electron carriers accumulate. It’s the same effect as having enough workers on an assembly line but not being able to move products forward because the packaging stations are jammed.
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When Reductive Stress Morphs Into Oxidative Damage
Too much NADH sets the stage for oxidative stress, but how does that transition really happen?
• The process behind excess NADH creation — The mitochondria’s Complex I tries to oxidize NADH — basically convert it back to NAD+ — but an overwhelming influx of NADH leads to partial electron leaks onto oxygen, generating superoxide.
• Superoxide transforms into more harmful substances — The superoxide easily transforms into other even more hazardous molecules, such as hydrogen peroxide or hydroxyl radicals, intensifying the cell’s damage. Hence, reductive stress is the fuse that ignites oxidative stress.
Researchers used to think of oxidative stress and reductive stress as opposites, but in fact, you can’t get a huge wave of oxidative molecules without first bottling up too many electrons somewhere upstream. The meltdown occurs when all these unwanted oxygen-based molecules assault proteins, lipids and genetic material within cells, blocking regular functions and straining the system further.
How Key Enzymes Become Blocked, Triggering Toxic Side Routes
Glyceraldehyde 3-phosphate dehydrogenase, or GAPDH, is an important enzyme in glycolysis. You can think of it as a traffic cop, directing the flow of carbon units down the main route for energy production.
• Reductive stress roadblocks GAPDH — In reductive stress conditions, superoxide and other reactive molecules can chemically inactivate GAPDH, jamming the normal route. That means partially digested sugar fragments accumulate, searching for an escape route. If the main road of glycolysis is blocked, these fragments slip into alternative pathways — often called branching pathways.
• Examples of branching pathways — One of the branches is the polyol pathway, where sugar is first turned into sorbitol and then into fructose. This route increases NADH and drains NADPH, leaving the cell less capable of defending against oxidative threats. Another branch is the hexosamine pathway, which decorates proteins with sugar-like attachments and can promote even more harmful byproducts.
A third branch leads to the creation of advanced glycation end products, lumps of sugar stuck onto proteins that distort them and spark inflammation.
Each of these side roads ends up producing or amplifying reactive oxygen species, so the cell quickly finds itself in an escalating cycle — high sugar leads to reductive stress, which leads to oxidative stress, which damages enzymes, forcing leftover sugar into toxic detours, fueling even more oxidative stress.
• Diabetes is the result — The cyclical meltdown causes the hallmark problems of diabetes — nerves lose function (neuropathy), eyes develop vision problems (retinopathy), kidneys fail (nephropathy) and blood vessels clog or weaken (leading to strokes, heart attacks and amputations). It’s a chain reaction that starts from too much sugar and too many electrons in the wrong place at the wrong time.
The following graph, Figure 4 from Liang-Jun Yan’s paper, “Pathogenesis of chronic hyperglycemia: from reductive stress to oxidative stress,”3 published in the Journal of Diabetes Research in 2014, illustrates this process.
Consequences for People with Diabetes and Recommended Solutions
As chronic hyperglycemia persists, cells get battered by waves of destructive molecules. This environment disrupts insulin secretion, lowers insulin sensitivity and robs tissues of normal functioning. Measuring such damage often shows high levels of oxidative stress in people with poor sugar control, reinforcing that the end result of reductive stress — excess electron carriers — translates into extensive oxidative harm.
• There is a glimmer of hope — If the fundamental problem is that NADH builds up too fast, then reducing or balancing that electron overload might prevent later catastrophes.
• Addressing the root problem of diabetes — While many diabetes treatments focus on lowering blood sugar in general, or on cleaning up ROS after they form, what we really need are strategies to either curb the production of extra NADH or help cells recycle NADH back to NAD+ more efficiently.
• Other strategies that help manage diabetes — Some researchers suggest that strengthening the electron transport chain, or using dietary or pharmaceutical interventions that enhance NAD+ regeneration, can short-circuit the entire cascade before oxidative stress goes wild.
In simpler language, controlling reductive stress means improving the traffic flow of electrons in the cell, ensuring they don’t stack up to dangerous levels. If you manage the electron flow at the front end, you reduce the chance of harmful chain reactions downstream.
Putting It All Together — Why Reductive Stress Matters So Much
Prolonged high blood sugar is definitely toxic to cells, but we now see that the toxicity operates through a two-phase process — first, reductive stress (an electron overload), then oxidative stress (excess oxygen-based radicals) finalizes the damage.
• Oxidative stress is just one piece of the puzzle — The statement above modifies the classic narrative that only oxidative stress is to blame. Recognizing how reductive stress kindles oxidative stress helps us see that lowering sugar might not be enough; we also need to keep watch on the entire electron-handling machinery within cells.
• Reductive stress must be detected earlier — One of the big questions is why reductive stress has been overlooked for so long if it’s so central. Part of the answer is that oxidative stress is easier to detect with standard lab tests and known chemical markers, whereas reductive stress is more subtle, only revealing itself in how the electron carriers build up.
Also, reductive stress was first documented decades ago and then largely forgotten, overshadowed by the simpler story of oxygen-based radicals. Only with improved technologies and a deeper dive into electron transport chain dynamics did researchers rediscover how an oversupply of NADH or NADPH can disrupt everything.
In everyday life, the main message remains consistent — keep blood sugar under control to protect your cells from a damaging cascade.
• Strategies to address reductive stress — Good nutrition, exercise and regular medical check-ups all form part of the frontline in preventing reductive stress from flaring into full-blown oxidative chaos.
• The importance of studying reductive stress — Long term, the real advantage in understanding reductive stress is that it offers a new angle — one that goes beyond the usual talk of high sugar and ROS. By targeting the earliest link in the chain, you can knock out multiple problems at once, safeguarding insulin production, reducing inflammation and preserving healthy organ function.
Supplements That May Help Address Reductive Stress
Several nutritional supplements can be helpful in this regard, including the following:
• Coenzyme Q10 (CoQ10) / Ubiquinol:
◦ Mechanism — CoQ10 is a vital component of the ETC in mitochondria. It acts as an electron shuttle, helping to move electrons along the ETC and facilitate ATP production. In its reduced form, ubiquinol, it can also act as an antioxidant.
◦ Relevance to reductive stress — By improving the efficiency of the ETC, CoQ10 may help to prevent the buildup of NADH and the subsequent leakage of electrons that leads to reductive stress.
• Alpha-lipoic acid (ALA):
◦ Mechanism — ALA is a potent antioxidant that can also regenerate other antioxidants, such as vitamin C and glutathione. It also plays a role in mitochondrial energy metabolism.
◦ Relevance to reductive stress — ALA’s antioxidant properties can help to mitigate the oxidative damage that results from reductive stress. It may also indirectly support the ETC by regenerating other antioxidants involved in the process.
◦ Note — ALA exists in two forms (R-lipoic acid and S-lipoic acid), and the R form is generally considered more biologically active.
• Methylene blue:
◦ Mechanism — Methylene blue acts as an alternative electron acceptor in the ETC, effectively bypassing Complex I and III. It can cycle between its oxidized and reduced forms, shuttling electrons directly to cytochrome c and oxygen, improving mitochondrial function even when the standard electron transport chain is impaired.
Methylene blue’s ability to accept electrons makes it particularly useful in conditions where the standard ETC is overwhelmed or dysfunctional.
◦ Relevance to reductive stress — By providing an alternative route for electron flow, methylene blue helps relieve the electron congestion that characterizes reductive stress. It effectively acts as an “electron pressure release valve,” helping to prevent the buildup of NADH and reducing the likelihood of electron leakage and subsequent oxidative damage.
• Pyrroloquinoline quinone (PQQ):
◦ Mechanism — PQQ is a potent antioxidant that has been shown to stimulate mitochondrial biogenesis (the creation of new mitochondria).
◦ Relevance to reductive stress — By increasing the number of mitochondria and improving their function, PQQ enhances the cell’s overall capacity to handle electron flow and reduce the likelihood of reductive stress.
• Riboflavin (B2), niacinamide (B3) and thiamine (B1):
◦ Mechanism — B vitamins play essential roles as coenzymes in various metabolic pathways, including those involved in energy production and the ETC. Riboflavin is a precursor to FAD, and niacin is a precursor to NAD. Both are electron carriers.
◦ Relevance to reductive stress — Adequate levels of B vitamins are essential for the proper functioning of the ETC and may help to prevent the buildup of reducing equivalents.
Frequently Asked Questions (FAQs) on Reductive Stress and Type 2 Diabetes
Q: What is reductive stress, and how does it relate to Type 2 diabetes?
A: Reductive stress occurs when cells accumulate too many electron-carrying molecules, such as NADH, due to prolonged high blood sugar levels. This overload creates a bottleneck in the mitochondria, leading to an imbalance that ultimately triggers oxidative stress. In Type 2 diabetes, excessive sugar intake overwhelms the metabolic system, causing a cascade of harmful effects that damage cells, tissues and organs.
Q: How does reductive stress contribute to oxidative stress and cellular damage?
A: When NADH builds up in cells, it overwhelms the electron transport chain (ETC) in mitochondria, leading to electron leakage. These leaked electrons react with oxygen to form harmful reactive oxygen species (ROS) like superoxide and hydrogen peroxide. This oxidative damage disrupts cellular processes, impairs insulin function and contributes to complications like neuropathy, retinopathy and kidney disease.
Q: Why is reductive stress often overlooked in diabetes research?
A: Traditionally, scientists have focused on oxidative stress as the primary cause of cellular damage in diabetes. However, newer research shows that reductive stress precedes oxidative stress and acts as the initial trigger. The difficulty in measuring reductive stress and its more subtle effects led to its underappreciation for decades, but advances in mitochondrial research have revived interest in its role.
Q: What strategies can help manage reductive stress in Type 2 diabetes?
A: Managing blood sugar levels through a healthy diet and exercise supervision is key to preventing reductive stress. Additionally, certain supplements, such as coenzyme Q10 (CoQ10), alpha-lipoic acid (ALA) and methylene blue may help manage reductive stress and prevent oxidative damage.
Q: How do supplements like CoQ10 and alpha-lipoic acid help with reductive stress?
A: CoQ10 improves mitochondrial function by facilitating electron transfer in the ETC, reducing the buildup of NADH. Alpha-lipoic acid (ALA) acts as an antioxidant and helps regenerate other protective molecules like glutathione. Both supplements aid in restoring cellular balance, reducing oxidative stress and improving insulin sensitivity in people with diabetes.
The Hidden Link: How Modern Diets May Be Fueling the Rise in Autism
Reproduced from original article:
https://articles.mercola.com/sites/articles/archive/2024/08/20/modern-diets-autism.aspx
Analysis by Ashley Armstrong August 20, 2024
STORY AT-A-GLANCE
- Autism rates have risen dramatically, from 2 to 4 cases per 10,000 children in the 1960s to ’70s to about 1 in 36 children in the U.S. today
- A groundbreaking study found a link between polyunsaturated fatty acid (PUFA) metabolites in umbilical cord fluid and autism severity in children. The study found that high levels of diHETrE, a metabolite of arachidonic acid (derived from linoleic acid), in cord blood significantly impacted autism spectrum disorder (ASD) symptom severity
- Modern diets have seen a massive shift towards consuming more PUFAs, with linoleic acid intake increasing from less than 2% to over 25% of total daily calories. High-PUFA intake during pregnancy may influence fetal neurodevelopment through increased production of inflammatory molecules called eicosanoids
- Similar studies have linked high maternal omega-6 intake to increased risks of ADHD and cognitive impairments in children
- Experts suggest returning to traditional fat sources lower in PUFAs and reconsidering prenatal nutrition advice that currently promotes vegetable oils over saturated fats
In recent years, the prevalence of autism spectrum disorder (ASD) has risen dramatically, leaving researchers and parents alike searching for answers. While the exact causes remain elusive, emerging evidence points to an unexpected culprit: the fats we eat.
A groundbreaking study has uncovered a potential link between polyunsaturated fatty acids (PUFAs) in our diets and the development of autism. This discovery not only sheds light on the possible origins of ASD but also raises important questions about the long-term effects of our modern dietary habits.
The Changing Face of Autism
To understand the significance of this research, we must first look at how our understanding and recognition of autism have evolved over time. In the 1950s, autism was barely on the medical radar. It wasn’t until the early 1960s that pioneers like Leo Kanner and Hans Asperger brought autism into the spotlight as a distinct condition.
The first prevalence studies, conducted in the 1960s and 1970s, painted a very different picture from what we see today. Back then, autism was estimated to affect just 2 to 4 cases per 10,000 children.1 Fast forward to the present day, and the numbers are staggering. Current estimates suggest that about 1 in 36 children in the U.S. is identified with ASD2 — a dramatic increase that cannot be explained by improved diagnosis alone.
This surge in autism rates has coincided with significant changes in our dietary patterns, particularly in the types of fats we consume. Could there be a connection?
The PUFA Problem
At the heart of this potential link are polyunsaturated fatty acids, or PUFAs. These are a type of fat found in many foods, particularly vegetable (seed) oils, certain seeds and nuts, and even in the meat of animals fed high-PUFA diets. High-PUFA diets can interfere with thyroid hormone utilization and impair gut health, contributing to inflammation and metabolic issues. (As discussed in my previous article, here.)
The study in question made a startling discovery: the presence of metabolic byproducts of PUFA breakdown in the umbilical cord fluid was linked to severity of autism symptoms in children.3 In other words, the waste products created when our bodies process PUFAs may be negatively impacting the neurodevelopment of children, even before they’re born.
This isn’t entirely new information in the scientific community. Similar results have been observed in mice, but this study marks one of the first times these findings have been confirmed in humans. It’s a crucial step in understanding the potential risks associated with our modern diets.
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The Dietary Shift
To fully grasp the implications of this research, we need to look at how our diets have changed over the past century. In the early 1900s, the average person’s fat intake looked very different from what it does today. Animal fats like tallow, lard, butter, and eggs were dietary staples. Vegetable oils, now ubiquitous in processed foods and cooking, simply didn’t exist in the human diet.
Today, we’ve seen a massive shift towards consuming more PUFAs and fewer saturated fats. This change is particularly pronounced in the consumption of linoleic acid (LA), an omega-6 PUFA that’s abundant in vegetable oils. Prior to the 20th century, LA made up less than 2% of total daily caloric intake. Now, it accounts for over 25% of total calories for the average person4 — a more than tenfold increase!
This dietary revolution hasn’t been limited to humans. The animals we eat, particularly chickens and pigs, are now often raised on high-PUFA feed in confinement barns. As a result, chicken has become the highest source of linoleic acid consumption in the United States.5 We’re not just changing our own diets; we’re changing the nutritional profile of our entire food chain.
The Science Behind the Link
In this research paper, levels of diHETrE in umbilical cord fluid significantly impacted ASD symptoms in children and were associated with impaired adaptive functioning. What is diHETrE and how does that relate to PUFA intake? To understand how PUFAs might influence autism development, we need to briefly delve into some biochemistry.
When we consume PUFAs, our bodies break them down through a complex process involving digestion, absorption, and metabolism. To simplify this discussion, let’s focus on Linoleic Acid (LA) intake, which is an omega-6 that is high in vegetable (seed) oils, some seeds and nuts, and the fat of chickens and pigs fed a diet high in LA.
Some of the LA we consume is used directly for energy or as structural components in our bodies. The rest is converted into a compound called Arachidonic Acid (AA) through a series of chemical reactions.
AA can then be further transformed into other bioactive molecules called eicosanoids. Eicosanoids are a broad class of signaling molecules that play crucial roles in inflammation, pain perception, and other physiological processes. They’re formed through two main pathways:
1. The Cyclooxygenase (COX) pathway — Here, AA is converted by COX enzymes into various eicosanoids like prostaglandins and thromboxanes.
2. The Lipoxygenase (LOX) pathway — In this route, AA is transformed by lipoxygenase enzymes into other eicosanoids such as leukotrienes and lipoxins.
Once formed, these eicosanoids act locally on nearby cells, modulating various physiological processes. The key point here is that eicosanoids are primarily derived from PUFAs. The more PUFAs we consume, the more eicosanoids our bodies produce.
COX and LOX enzymes work through oxidation processes. The multiple double bonds in PUFAs create points of unsaturation that are reactive and can be easily oxidized by COX and LOX enzymes. These unsaturated sites are crucial for the enzymes to introduce oxygen and form the bioactive eicosanoids.
Saturated fatty acids lack double bonds in their carbon chains, making them less reactive and unsuitable substrates for the COX and LOX enzymes. The absence of double bonds means that there are no reactive sites for the introduction of oxygen. Thus, COX and LOX enzymes cannot act on saturated fats to produce eicosanoids.
Just another reason why the TYPES of fat we eat matter — they not only serve roles for energy and structure, but they also play a very important role in signaling and physiological functions. Eicosanoids are primarily derived from PUFAs. So, the less PUFA we eat, the less eicosanoids there will be around the body.
The Smoking Gun: diHETrE
The study that uncovered the link between PUFAs and autism severity found elevated levels of a specific eicosanoid called diHETrE in umbilical cord blood. DiHETrE is derived from AA and has known inflammatory properties. Its production involves the action of LOX enzymes, which introduce hydroxyl groups into the fatty acid chain.
While we do consume small amounts of AA directly in our diets, the vast majority comes from the conversion of dietary LA. This means that increased intake of LA can lead to higher levels of AA, as more raw material is available for conversion.
The study’s conclusions were striking: “Specifically, high levels of AA-derived diols in cord blood, including total diHETrE, 11,12-diHETrE, and 14,15-diHETrE, were found to impact ASD symptom severity significantly. At high levels of 11,12-diHETrE, it was associated with SA disability … Based on these findings, AA-derived metabolites in cord blood may influence subsequent neurodevelopment in children.”
These findings suggest that the presence of PUFA metabolites (which rise through higher consumption of dietary PUFAs) during the fetal period may influence the development of ASD symptoms through inflammatory cytokines.
Schematic figure from the paper of arachidonic acid (AA) metabolism in neonatal cord blood and its relation to ASDBeyond Autism: The Broader Impact
While this study focused on autism, it’s important to note that the potential negative effects of high-PUFA intake extend beyond ASD.
Another study investigating umbilical cord fluid found that elevated levels of AA were linked to higher ADHD symptom scores during childhood.6 Further, maternal diets high in omega-6s increases ADHD risk in the child.7,8
High omega-6 diets in mothers have also been associated with increased risk of cognitive impairments in their children.9,10 These findings collectively support the “fetal origins of disease” concept, which suggests that altered nutrition in early life can lead to disease development later on.
This is particularly relevant to central nervous system (CNS) development, as “the developing CNS is particularly vulnerable during intrauterine development to metabolic compromise given the exceptional energy demands of its many cell types that are being generated (including neurons, astroglia, microglia, oligodendroglia, vasculature), their protracted movements (migration), morphogenesis, and assembly into functional circuits.
Thus, disruption of these processes by environmental factors will likely provoke long-lived modifications to brain structure and, ultimately, function”.11
The Generational Impact
Perhaps one of the most concerning aspects of this dietary shift is its potential to affect multiple generations. And this impacts the child’s development after birth as well, as the fatty acid composition of breast milk has drastically changed in parallel with changes in dietary fats.
As Dr. Mercola’s review paper on LA12 notes: “A seminal study conducted in 1959 [27] provided lactating women with a high-LA diet consisting of fats from lard, corn oil, or linseed oil, which approximated the LA content of the standard American diet, with approximately 15% to 30% of total calories coming from LA.
Within 2 to 3 days of changing their usual diet to the high-LA diet, the amounts of LA in their breast milk increased from 8% to 10% to 42%. The study highlights that the LA content of breast milk has significantly increased in human breast milk due primarily to marked changes in the nature of the fats consumed.”
This rapid change in breast milk composition means that infants are now being exposed to significantly higher levels of LA from their very first meals. The dietary shifts we’ve made aren’t just affecting us; they’re changing the nutritional landscape for generations to come.
The Path Forward
Given the mounting evidence of potential harm from excessive PUFA consumption, particularly in the context of fetal and early childhood development, what can be done?
1. Return to traditional fats — One obvious step is to shift back towards more traditional fat sources that are richer in saturated fats and lower in PUFAs. In the 1800s, fats consumed in the diet included animal fats like tallow, lard, eggs and butter.13
Vegetable (seed) oils did not exist at this time for humans or animals! We need to go back to consuming traditional fats which were richer in saturated fat and lower in PUFAs. Limiting consumption of vegetable (seed oils), nuts and seeds, plus fattier cuts of meats from chickens and pigs fed a high-PUFA diet will help lower your total PUFA intake.
2. Educate and raise awareness — Many people are unaware of the dramatic changes in our dietary fat consumption over the past century. Educating the public, friends and family about these changes and their potential impacts is crucial.
3. Reconsider prenatal nutrition advice — Given the potential impact of maternal diet on fetal development, a renewed focus on prenatal nutrition that takes these findings into account is warranted.
In fact, the USDA ‘Tips for Pregnant Moms’ document currently states: “Choose vegetable oils instead of butter.”14
Conclusion
It’s important to note that the link between PUFAs and autism is not without controversy. The dramatic increase in autism rates over the past few decades is likely multifactorial, with potential contributors including improved diagnosis, changes in diagnostic criteria, environmental factors, and genetic influences.
However, in the face of rising rates of neurodevelopmental disorders, every potential contributing factor must be carefully examined. The link between PUFAs and autism development may prove to be a crucial piece of the puzzle, opening up new avenues for prevention and intervention.
Ultimately, this research serves as a reminder of the profound impact our dietary choices can have, not just on our own health, but on the health and development of future generations.
About the Author
Ashley Armstrong is the cofounder of Angel Acres Egg Co., which specializes in low-PUFA (polyunsaturated fat) eggs that are shipped to all 50 states (join waitlist here), and Nourish Cooperative, which ships low-PUFA pork, beef, cheese, A2 dairy and traditional sourdough to all 50 states. Waitlists will reopen shortly.
- 1 J Intellect Disabil Res. 2005 Apr;49(Pt 4):231-8. doi: 10.1111/j.1365-2788.2005.00676.x
- 2 Surveillance Summaries / March 24, 2023 / 72(2);1–14
- 3 Psychiatry and Clinical Neurosciences, doi: 10.1111/pcn.13710
- 4 Am J Clin Nutr. 1999 Sep;70(3 Suppl):560S-569S. doi: 10.1093/ajcn/70.3.560s
- 5 National Cancer Institute, Identification of Top Food Sources of Various Dietary Components
- 6 The Journal of Pediatrics Volume 209, June 2019, Pages 204-211.e4
- 7, 10 J Pediatr. 2019 Jun:209:204-211.e4. doi: 10.1016/j.jpeds.2019.02.022. Epub 2019 Mar 28
- 8 J Child Psychol Psychiatry. 2018 Sep;59(9):1003-1011. doi: 10.1111/jcpp.12898. Epub 2018 Mar 24
- 9 J Nutr. 2013 Sep;143(9):1481-8. doi: 10.3945/jn.113.178640. Epub 2013 Jul 31
- 11 J Neuroendocrinol. 2023 Sep; 35(9): e13320, Introduction
- 12 Nutrients 2023, 15(14), 3129; doi: 10.3390/nu15143129
- 13 The American Journal of Clinical Nutrition Volume 93, Issue 5, May 2011, Pages 950-962
- 14 USDA, Tips for Pregnant Moms
The Importance of Enzymes for Health, Longevity and Chronic Disease Prevention
Reproduced from original article:
https://articles.mercola.com/sites/articles/archive/2023/12/19/importance-of-enzymes.aspx
The original Mercola article may not remain on the original site, but I will endeavor to keep it on this site as long as I deem it to be appropriate.
Analysis by Dr. Joseph Mercola December 19, 2023
STORY AT-A-GLANCE
- Enzymes are catalysts that accelerate biochemical reactions in your body. Digestive enzymes are important for proper digestion and nutrient absorption, but the benefits of enzymes do not end there
- Researchers have discovered enzymes for all sorts of uses, from boosting athletic endurance by optimizing digestion and nutrient uptake to treating cancer
- To optimize enzyme function, eat plenty of fresh, raw and/or fermented foods. Sprouts are a particularly excellent source. Fasting has also been shown to conserve enzymes
As the name implies, digestive enzymes are important for optimal digestion and nutrient absorption. But their functions and benefits do not end there. Enzymes are actually necessary for most cellular functions and biological processes.
Enzymes — proteins composed of amino acids — are secreted by your body to catalyze functions that normally would not occur at body temperature, making them vital to good health and longevity.1,2
Science has identified more than 3,000 different enzymes, yet we’ve likely only scratched the surface. There are at least 75,000 enzymes in our bodies.3 Each organ has its own set of enzymes, and each enzyme has a different function. In essence, they act like specialized keys cut to fit specific locks. In this analogy, the locks are biochemical reactions.
Enzymes Do More Than Aid Digestion
Over the years, researchers have discovered enzymes for all sorts of uses, from boosting athletic endurance by optimizing digestion and nutrient uptake4 to treating cancer. According to some researchers, enzyme preservation is an important aspect of longevity, as younger people have far higher levels than older ones.
For example, young adults have about 30 times more amylase in their saliva than 69-year-olds, and 27-year-olds have twice the amount of lipase as 77-year-olds. Chronically ill people also tend to have much lower levels of enzymes.5
In one recent animal study,6 the nicotinamide mononucleotide (NMN) — an enzyme involved in energy metabolism, found in broccoli, cucumbers and cabbage — helped regenerate aging cells, making them behave as younger cells and preventing certain age-related genetic changes.
As a result, the NMN-treated mice gained less weight than untreated ones (likely a result of increased energy conversion) and experienced improved eyesight. Fortunately, optimizing your enzymes is as easy as eating plenty of fresh, raw and/or fermented foods. Sprouts are a particularly excellent source of live enzymes.
Fasting has also been shown to conserve enzymes. If you do not eat, you will not produce digestive enzymes, allowing metabolic enzyme production and activity to proliferate instead.
Types of Enzymes and Their Functions
Enzymes can be broadly divided into the following categories:7
• Digestive enzymes, involved in digestion; the breaking down of foods into nutrients and elimination of waste products. Digestive enzymes are extra-cellular, meaning they’re found outside your cells.
There are eight primary digestive enzymes, each designed to help break down different types of food:
| Protease — Digesting protein | Maltase — Converting complex sugars from grains into glucose |
| Amylase — Digesting carbohydrates | Lactase — Digesting milk sugar (lactose) in dairy products |
| Lipase — Digesting fats (If you have IBS, cystic fibrosis , celiac disease, no gallbladder or gallbladder dysfunction and/or obesity, you may benefit from higher levels of lipase.
Also beware that fluorinated water may decrease lipase and protease production)8 |
Phytase — Helps with overall digestion, especially in producing the B vitamins |
| Cellulase — Breaking down fiber | Sucrase — Digesting most sugars |
• Metabolic enzymes, involved in energy production and detoxification. Metabolic enzymes are intra-cellular, meaning inside your cells, where they help the cell carry out a variety of functions related to its reproduction and replenishment.
• Food-based enzymes, contained in raw, uncooked/unprocessed foods and/or supplements. Dietary enzyme supplements are derived either from plants or animals.
For example, enzymes can be extracted from certain fungi and bacteria, raw foods, such as the bromelain in pineapple and papain from papaya. Pancreatic enzyme supplements, such as pepsin and trypsin, are obtained from the stomach, small intestine and pancreas of animals.
People who may benefit from eating more raw foods and/or taking a food enzyme supplement include those who:
• Eat cooked, microwaved or processed foods. The more raw foods you eat, the lower the burden on your body to produce the enzymes it needs, not only for digestion, but for practically everything.
Whatever enzymes are not used up in digestion are then available to help with other important physiological processes.
• Are over the age of 30. Studies show your body’s production of enzymes decreases by about 13% every decade. So by age 40, your enzyme production could be 25% lower than it was when you were a child.
By the time you’re 70, you could be producing only one-third of the enzymes you need for good health. Making matters worse, your stomach produces less hydrochloric acid as you age, and hydrochloric acid is crucial in activating your stomach’s digestive enzymes.
When digestion of foods requires such a heavy demand, enzyme supplies run short and your enzyme-producing capacity can become exhausted.
• Struggle with toxicity.
• Are acutely or chronically ill, including those with digestive problems, endocrine gland imbalances, high blood sugar, diabetes, obesity, high cholesterol, stress-related problems, arthritis and other inflammatory conditions.
Supplements containing amylase, lipase and proteases (enzymes that help break down starches, fats and proteins respectively) have been shown to benefit those with food sensitivities.9 For optimal digestion, you need all three. Other less well-known digestive enzymes include ribonuclease and deoxycyribonuclease-I, which digest nucleic acids and DNA/nuclease respectively.
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Enzymes and Coenzymes Play Important Roles in Health
Enzymes are catalysts that cause biochemical reactions to happen. In other words, they assist and accelerate reactions, sometimes to a mind-boggling several million reactions per second. In this way, enzymes significantly lower the amount of energy needed for a reaction to occur. And, without them, some reactions would not even be able to take place at all. Here’s a sampling of activities in your body that require enzymes in order to occur:
| Energy production | Carrying away toxic wastes |
| Absorption of oxygen | Dissolving blood clots |
| Fighting infections and healing wounds | Breaking down carbohydrates, proteins and fats, and regulating cholesterol and triglyceride levels |
| Reducing inflammation | Hormone regulation |
| RNA/DNA functioning | Nerve impulse regulation |
| Getting nutrients into your cells | Slowing the aging process |
As important as they are, enzymes do not work alone. They rely on other elements to accomplish their tasks, such as certain vitamins and minerals. These elements are called coenzymes.10 One of the most well-known coenzymes is coenzyme Q10 (CoQ10), found in the mitochondria (power centers) of your cells where it is involved in making ATP, a principal energy source. Another example is magnesium, which participates in over 300 enzyme reactions.
However, while your body produces its own enzymes, this ability begins to decline as early as your late 20s. The situation is worsened if you eat primarily processed foods, as viable enzymes are only found in fresh foods. This is yet another reason why diet has such a tremendous impact on disease risk, as enzyme imbalance or deficiency can significantly raise your risk of cancer and autoimmune diseases.
Annesse Brockley’s and Kristin Urdiales’ book, “Autoimmune,” explores the link between digestive enzyme deficiency and autoimmune disease. While still controversial, the link between digestive enzymes and immune dysfunction is quite compelling, and helps us understand why and how diet can be such a powerful intervention.
Cancer-Fighting Benefits of Pancreatic Enzymes
A large portion of your digestion occurs in your duodenum, the early part of your small intestine. Your pancreas secretes digestive juices in response to food in your stomach. These digestive juices contain the eight groups of enzymes responsible for breaking down carbs, protein, fats and other nutrients.
When your pancreas is not working well, a deficiency in pancreatic enzymes can lead to malabsorption of nutrients and overgrowth of bacteria in your small intestine, a condition that presents itself as gas and bloating, fatigue and constipation. It may also play a role in irritable bowel syndrome (IBS).11 Pancreatic insufficiency may be treated by taking a pancreatic enzyme supplement.
Interestingly, pancreatic enzymes may also be very useful in the treatment of cancer. When used for this purpose, pancreatic enzymes are taken between meals rather than with them. When taken at a time when they’re not needed for digestion, the enzymes have been shown to go to work systemically, affecting your body organs via your blood.
One of the mechanisms by which enzymes fight cancer is by stripping away the fibrin coating that cancer cells protect themselves with. Fibrin is a fibrous protein that cancer cells wrap themselves with in order to protect themselves against attack by your immune system. Due to its fibrous nature, this coating is 15 times thicker than the outer layer of a normal, healthy cell.
By stripping off this layer, enzymes help your immune system detect the antigens contained within the cancer cell, thereby allowing your immune system to kill the cell and dispose of it naturally. Moreover, certain enzymes trigger macrophage to release tumor necrosis factor (TNF), which plays an important role in downregulating an overactive immune system, thereby helping those with autoimmune conditions.
Enzymes Used in Leukemia Treatment
L-asparaginase, an enzyme isolated from the bacteria Escherichia coli and Erwinia chrysanthemi, has a long history of use in the treatment of acute lymphoblastic leukemia, the most common form of childhood leukemia in the U.S.
It’s also widely used in veterinary medicine to treat certain types of cancers in cats and dogs, specifically cancers involving the immune system.12 L-asparaginase works by “starving” the cancer cell of asparaginase, an enzyme needed in the production of proteins.
Healthy cells need only a small amount of asparaginase, and can produce what it needs internally. Cancer cells not only need hefty amounts; they also cannot produce this enzyme internally and must obtain it from outside sources.
L-asparaginase works by eliminating asparaginase and, by depriving the cancer cell of it, the cell dies since it cannot produce what it needs to thrive. Researchers have now found an L-asparaginase-like enzyme found in baker’s yeast may be a less toxic alternative to the bacteria-derived enzyme. As reported by Medical News Today:13
“First study author Iris Munhoz Costa … explains that unlike bacteria, yeast is eukaryotic. This means that it contains a membrane-covered nucleus consisting of genetic material, as is the case with human cells. As such, it is hypothesized that yeast-derived enzymes are less likely than bacterial enzymes to trigger severe immune responses.”
The Kelley Treatment — Cancer Treatment Using Enzymes
In 2011, I interviewed Dr. Nick Gonzalez, a prominent cancer doctor who specialized in alternative treatment methods. Gonzalez died in 2015 from what appears to have been a heart attack. Prior to his untimely death, he’d had remarkable success treating cancer patients with a three-pronged nutritional approach based on the groundbreaking work of Dr. William Kelley, a dentist who cofounded nutritional typing.
Many of these patients were diagnosed with highly lethal forms of cancer that conventional medicine cannot effectively address, including pancreatic cancer, brain cancer and leukemia. Gonzalez’s program consisted of three basic components:
- Individualized diet based on nutritional (metabolic) typing
- Individualized supplement program, which includes vitamins, minerals, trace elements and pancreatic enzymes
- Detoxification, which included coffee enemas and colon cleanses
In regard to the enzymes, he stressed the importance of taking the correct ratio of active and inactive enzymes. Interestingly, the inactive precursors are particularly active against cancer. They also have a far longer shelf life, and are more stable than the active ones.
According to Gonzalez, pancreatic enzymes not only are useful as treatment for active cancer but are also one of the best preventive measures. Before his death, Gonzalez published two highly rated books, “The Trophoblast and the Origins of Cancer,” and “One Man Alone: An Investigation of Nutrition, Cancer, and William Donald Kelley.”
The Many Benefits of Seaprose-S
Seaprose-S (also known as protease-s) is one proteolytic, meaning systemic, enzyme with powerful health benefits.14 It’s particularly effective for breaking up of mucus15 and reducing inflammation.16 Some studies also suggest it may have antibiotic properties. Its anti-inflammatory and mucus-dissolving activities have been shown to benefit conditions such as:
| Arthritis | Edema |
| Pleurisy (inflammation of your lung lining) | Peritonitis (inflammation of your abdominal lining) |
| Thrombophlebitis (pain and inflammation in your veins following a blood clot) |
Pulmonary tuberculosis |
| Bronchitis | Pulmonary emphysema |
| COPD | Bronchiolitis |
| Bronchial asthma | Wound complications following vaginal birth or C-section17 |
| Venous inflammatory disease18 |
This enzyme is one you would take in-between meals, not with your meals, as it’s not aimed at improving digestion but rather doing its work systemically. By passing unused into your digestive tract, seaprose-S can enter your bloodstream, thereby reaching all the tissues in your body.
How to Boost Your Enzyme Levels Naturally
There are four ways to naturally increase your enzyme levels:
- Increase your intake of raw, living foods
- Fast
- Chew your food thoroughly
- Avoid chewing gum
The very best way to get enzymes into your body is by consuming at least 75% of your foods raw. For many of you, you’ll have to work toward this goal gradually. While all raw foods contain enzymes, the most powerful enzyme-rich foods are those that are sprouted (seeds and legumes). Sprouting increases the enzyme content in these foods tremendously. Besides sprouts, other enzyme-rich foods include:
| Papaya, pineapple, mango, kiwifruit and grapes | Raw honey (the enzymes actually come from the bee’s saliva) |
| Extra virgin olive oil | Raw meat and dairy |
| Avocado | Bee pollen |
| Coconut oil | Fish sauce19,20,21 and other fermented fish products22 |
By eating these types of foods, you supply your body with the amino acids and the enzyme co-factors needed to boost your own natural enzyme production. Another way to lower your body’s demand for enzymes is to reduce your caloric intake. Did you know the average person spends 80% of his available energy simply digesting food?
By reducing overall consumption, as well as introducing more living foods, you reduce your need for digestive enzymes, which allows your body to put more of its energy into producing metabolic enzymes, which brings us to chewing: Quite apart from the esthetic pleasure of an unhurried meal, there are important physiological reasons to chew your food well.
Chewing stimulates saliva production, and the more time you spend chewing, the longer your saliva enzymes have to work in your mouth, lessening the workload of your stomach and small intestine. This is also the reason for the recommendation to avoid chewing gum. Chewing gum fools your body into believing it is digesting something, so it pumps out digestive enzymes unnecessarily.
Digestive Enzyme Supplementation
If you suffer from occasional bloating, minor abdominal discomfort and/or occasional constipation and suspect your enzyme production is low, you might want to consider a digestive enzyme supplement in addition to eating more of your foods raw.
Keep in mind that digestive enzymes should be taken WITH a meal, whereas systemic enzymes, taken for other health reasons, are taken between meals (see following section). There are hundreds of digestive enzymes on the market. Ideally, look for an enzyme formula with the following characteristics:
- It should contain a mixture of different types of enzymes, to help digest all of the different components of your diet (including lipase, protease and amylase)
- The ingredients should be high-quality, all-natural and free of allergens and additives
- The supplement should be labeled as to the enzymatic strength of each ingredient, not just its weight
- It should be made by a reputable company with rigorous quality control and testing for potency
Use of Systemic Enzymes May Improve Your Health
Besides digestive enzyme supplementation, oral enzymes can be used systemically. This requires taking enzymes on an empty stomach between meals so they can be absorbed through your gut into your bloodstream, where your cells can use them metabolically to clear away debris and accumulated metabolic buildups.
However, getting enzymes from your digestive tract into your bloodstream isn’t as easy as it would seem. Enzymes are very susceptible to denaturing and must be helped to survive the highly acidic environment in your stomach. For this reason, they’re often given an “enteric coating” to help them survive the journey through your digestive tract.
Systemic oral enzymes have been used to treat problems ranging from sports injuries to arthritis to heart disease and cancer, particularly in European countries. But most of the research has been published in non-English language journals.
This systemic use of enzymes is still in its infancy in the U.S. Keep in mind that in order for enzymes to be used systemically, they must be ingested on an empty stomach. Otherwise, your body will use them for digesting your food, instead of being absorbed into the blood and doing their work there.
- 1, 9 Johns Hopkins Medicine. Digestive Enzymes and Digestive Enzymes Supplements
- 2 Healthy Diet Healthy You, Digestive Enzymes
- 3 Institute for Integrative Nutrition. Enzymes: The Key to a Long and Healthy Life. August 16, 2017
- 4 Memorial Sloan Kettering Cancer Center. Proteolytic Enzymes: Purported Benefits, Side Effects 7 More
- 5 Medical News Today. Blocking One Enzymes Could Help Treat Many Chronic Disorders. July 27, 2018
- 6 Time October 27, 2016
- 7 Health. Should You Take Digestive Enzymes? October 31, 2023
- 8 Fluoride 2005;38(3):215–219
- 10 Chemistry Explained, Coenzymes
- 11 bodyecology.com, Digestive Enzymes
- 12 J Pharmacol Pharmacother. v.7(2); Apr-Jun 2016
- 13 Medical News Today January 18, 2017
- 14 Drugs Exp Clin Res. 1999;25(6):263-70
- 15 Pharmacological Research 1990 Sep-Oct;22(5):611-7
- 16 Drugs Under Experimental and Clinical Research 1999;25(6):263-70
- 17 Minerva Ginecologica 1990 Jul-Aug;42(7-8):313-5
- 18 Minerva Cardioangiologica 1996 Oct;44(10):515-24
- 19 Journal of Aquatic Food Product Technology 2004: 13(2)
- 20 Int J Mol Med. 2003 Oct;12(4):621-5
- 21 Mol Med Rep. 2010 Jul-Aug;3(4):663-8
- 22 Weston A Price January 15, 2016
What Are the Keys to Optimal Digestion?
Reproduced from original article:
https://articles.mercola.com/sites/articles/archive/2023/10/23/optimal-digestion.aspx
The original Mercola article may not remain on the original site, but I will endeavor to keep it on this site as long as I deem it to be appropriate.
Analysis by Dr. Joseph Mercola October 23, 2023
STORY AT-A-GLANCE
- 60 million to 70 million Americans suffer from gastrointestinal (GI) disease and nearly 40% were prevented from participating in routine activities due to bowel problems in the last year. Chronic constipation affects an estimated 63 million Americans, and gastroesophageal reflux disease (GERD) affects about 20% of the population
- Proper digestion is required to break down food into nutrients your body can use for energy, growth and repair. Poor digestion can have a serious impact on your health as your metabolism and energy production become impaired
- Chewing slowly helps break down your food faster, and saliva, which contains an enzyme called lingual lipase to help break down fats, helps when you swallow. The longer you chew, the more time those enzymes have to start breaking down your food. Eating slowly also lowers your risk for cardiometabolic conditions such as heart disease, diabetes and stroke
- Physical activity, such as walking, helps optimize gut motility and promotes peristalsis, the rhythmic contraction of your digestive muscles that move the food through your small and large intestines. A 2022 meta-analysis found that as little as a two-minute walk within an hour to an hour-and-a-half after each meal can improve your digestion and cardiometabolic health
- Acid reflux is typically caused by a deficiency in stomach acid, not excess. The lower esophageal sphincter is pH sensitive and only closes when there’s a sufficient amount of acid in your stomach
Digestive problems are incredibly common. According to a 2022 survey1 by the American Gastroenterological Association, some 60 million to 70 million Americans suffer from gastrointestinal (GI) disease and nearly 40% stopped routine activities due to bowel problems in the previous year.
Data2 from the National Institute of Diabetes and Digestive and Kidney Diseases confirm these sad statistics. Chronic constipation, for example, affects an estimated 63 million Americans, and gastroesophageal reflux disease (GERD) affects about 20% of the population.
Proper digestion is important because it breaks down food into nutrients your body can use for energy, growth and repair. Poor digestion, therefore, can have a serious impact on your health, especially in the long term, as your metabolism and energy production become impaired. Let me review a few important fundamentals for optimizing your digestion.
Fundamentals: Chew Your Food
Research3 on gut transit times shows food will remain in your stomach anywhere from 0.4 to 15.3 hours before entering your small intestine. It typically takes 3.3 to seven hours for food to pass through the entire small intestine, and whatever is left over that your body could not absorb or use is passed down to your large intestine, where it can remain for 15.9 to 28.9 hours before being expelled into your toilet bowl.
Foods rich in fiber, protein, complex carbs and fats take longer to digest than processed foods, which are deficient in these nutrients. Several lifestyle factors can also affect gut transit time, starting with chewing.
Chewing slowly helps with the mastication-to-digestion process, starting in your mouth. Chewing more slowly helps break down your food faster, and saliva, which contains an enzyme called lingual lipase to help break down fats, helps when you swallow.
The longer you chew, the more time those enzymes have to start breaking down your food. The process makes digestion easier on your stomach and small intestine, because digestion takes a lot of energy. Slowing down makes it easier for your intestines to absorb the nutrients.
One study4 demonstrated this point well: When study participants ate almonds quickly and chewed less (10 times, as opposed to 25 times or 40 times per bite), their bodies failed to take in all the nutrients almonds have to offer; the bits simply passed through largely undigested.
While I am no fan of eating almonds, the study does demonstrate that for those who chewed the most, the particles (hence the nutrition) were absorbed faster.
Chewing slowly and methodically — even thoughtfully — also helps you relax, and this too is important, as stress and anxiety slow motility and reduce blood flow to your gastrointestinal tract. Stress activates the fight-or-flight system, which suppresses digestion in the stomach and small intestine, while stimulating evacuation from the large intestine.
So, if you’re frequently eating on the go, at your desk or in a rush, you may want to reconsider. Making sure you’re relaxed while eating and that you’re chewing your food well are foundational strategies for optimizing your digestion.
Fast Eaters Are at Higher Risk for Metabolic Syndrome
People who wolf down their food in a rush are also at increased risk for cardiometabolic conditions such as heart disease, diabetes and stroke, as evidenced in a Japanese study.5
The study involved 1,083 healthy male and female participants, mean age 51.2 years, who were followed for five years. The participants were divided into three groups, categorized as slow, normal or fast eaters. Over the five years, fast eaters were nearly two times more likely to develop metabolic syndrome compared to their slow-eating cohorts. As reported by the authors:6
“The incidence rates of metabolic syndrome among slow, normal and fast-eating participants were 2.3, 6.5 and 11.6%, respectively. The multivariate-adjusted hazard ratio for incidence of metabolic syndrome in the fast-eating group compared to the normal and slow group was 1.89 …
Eating speed was significantly correlated with weight gain, triglyceride (TG) and high-density lipoprotein cholesterol (HDL-C) components of metabolic risk factors …
Conclusions: Eating speed was associated with obesity and future prevalence of metabolic syndrome. Eating slowly may therefore indicated to be a crucial lifestyle factor for preventing metabolic syndrome …”
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The Impact of Physical Activity
Exercise is another foundational lifestyle aspect that can impact your digestion. Physical activity, such as walking, helps optimize gut motility and promote peristalsis, the rhythmic contraction of your digestive muscles that move the food through your small and large intestines. Frequent inactivity slows everything down and contributes to constipation.
As little as a two-minute walk within an hour to an hour-and-a-half after each meal can improve your digestion and cardiometabolic health.
According to a 2022 meta-analysis and systematic review,7 even as little as a two-minute walk within an hour to an hour-and-a-half after each meal can improve your digestion and cardiometabolic health.
Similarly, a 2015 meta-analysis8 found that low-intensity exercise such as walking after meals was associated with faster gastric emptying. High-intensity exercise, meanwhile, was associated with slower gastric emptying, so more is not better in this case.
2020 research9,10 also found that walking more in general (not necessarily after meals) helped improve IBS symptoms, such as bloating, and reduced their severity.
Digestive Enzymes to the Rescue
For proper digestion, nutrient absorption and elimination, you also need digestive enzymes. When you don’t have enough of these enzymes, or your body doesn’t release them appropriately, you won’t be able to break down certain foods (depending on the enzyme lacking).
When you swallow food, it first enters the upper portion of your stomach. Here, any enzymes inherent in the food itself start to activate, helping to break the food down. As you might expect, the more the food can be broken down here, in the first stage of your gastrointestinal tract, the less labor intensive the digestive process will be later on.
The pH in this upper stomach portion typically ranges from 4 to 6, i.e., slightly acidic. As food enters your stomach, proton pumps lining the lower pyloric part of your stomach starts pumping in hydrochloric acid, and it does this in proportion to the amount of food that you eat. The more food you put in, the more hydrochloric acid is being pumped in to help break down and liquefy that food.
Importantly, hydrochloric acid does not actually help you digest your food. Rather, it activates an enzyme called pepsin, a proteolytic enzyme that helps digest protein. In this lower section of your stomach, the pH ranges from 2 to 4.
As the food is liquefied, it starts dripping into the duodenum, the upper part of your small intestine, triggering your pancreas to secrete alkaline bicarbonates, thereby neutralizing the acidity. The pH of your small intestine typically ranges from 8 to 9.
Pancreatic enzymes are also released, which continue the process of breaking the food down into even smaller constituent parts. In summary, digestion can occur in three areas — your upper stomach, lower stomach and small intestine — and your food choices can significantly influence where and how well digestion occurs in these areas.
Enzyme supplements can influence digestion in each of these areas, and help optimize assimilation and elimination of the foods you eat. There are five primary digestive enzymes, each designed to help break down different types of food:
- Protease, which breaks down protein
- Amylase, which breaks down carbohydrates, sugars and starches
- Lipase, which breaks down fats
- Lactase, which breaks down milk sugar (lactose) in dairy products
- Sucrase, which breaks down sucrose sugars
Often, taking a blend of enzymes is beneficial, as no single enzyme can perform all the necessary functions throughout your digestive tract. That said, if you have irritable bowel syndrome (IBS), cystic fibrosis, celiac disease, no gallbladder or gallbladder dysfunction, and/or obesity, you may benefit from higher levels of lipase in particular. Also, avoid fluoridated water, as fluoride inhibits production of lipase and protease11 — enzymes that break down fats and protein.
Skip the Antacids
If you suffer from digestive reflux, don’t rely on over-the-counter (OTC) antacids (acid neutralizers) or prescription proton pump inhibitors (PPIs). Inhibiting acid production is the last thing you want to do in this situation.12
Acid reflux occurs when contents from your stomach back up into your esophagus, causing stomach acid to irritate the lining of your esophagus. Other common names for this condition include acid indigestion, acid regurgitation, heartburn, and gastroesophageal reflux disease (GERD).
Because stomach acid is involved, and the word “acid” connotes the idea of “burning,” it’s commonly believed that excess stomach acid is the problem. Indeed, the entire antacid industry is built around this idea. Unfortunately, that’s completely backward.
Acid reflux is typically caused by a deficiency in stomach acid, not excess. This makes perfect sense once you realize that the lower esophageal sphincter is pH sensitive and only closes when there’s a sufficient amount of acid in your stomach.13 When low acid is not the cause of heartburn, the culprit can be any of the following:
| A hiatal hernia — The hernia basically forces the LES open, allowing gastric juices to back up into your throat14 |
| Helicobacter pylori infection15 — One 2012 study found 82.5% of GERD patients tested positive for H. pylori infection16 |
| Obesity17 |
| Smoking, by interfering with the LES function18 |
| Certain medications can relax the LES, including bronchodilators, calcium channel blockers (blood pressure meds), valium, nitroglycerine and opioids19 |
| Foods, including fats, chocolate, caffeinated beverages, peppermint and spearmint, sugar, onions, and alcohol can also weaken the LES20 |
| Foods that irritate your stomach can trigger reflux — Common irritants include citrus fruits, tomato, spicy foods, carbonated beverages, coffee, and high-lectin foods21 |
In all these cases, the solution is to address the underlying problem, which would be to fix the hernia, treat the H. pylori infection, lose weight, quit smoking, minimize use of the offending drug (be sure to discuss alternatives with your doctor) and not eating the foods that are causing your LES to relax or that irritate your stomach.
OTC antacids and PPIs are entirely the wrong approach, regardless of the underlying cause, because none of the underlying causes of acid reflux have anything to do with excess stomach acid.
Natural Remedies for Treating Occasional Reflux Problems
Again, stomach acid serves several important functions, such as breaking down proteins, killing ingested pathogens, ensuring optimal nutrient absorption, and regulating the rest of the digestion process. If you use acid-blockers, you’re compromising your entire digestive system.
So, if you suffer from occasional heartburn, indigestion, and other minor reflux symptoms, forgo the PPIs and OTC antacid medications and try one or more of the following nondrug alternatives instead:22,23,24,25,26
| Aloe juice — The juice of the aloe plant naturally helps reduce inflammation, which may ease symptoms of acid reflux. Drink about one-half cup of aloe juice before meals. To avoid its laxative effect, look for a brand in which the laxative component has been removed. |
| Apple cider vinegar (raw, unfiltered) — Take 1 tablespoon of raw unfiltered apple cider vinegar in a large glass of water before or directly after meals. |
| Astaxanthin — When compared to a placebo, this potent antioxidant was found to reduce symptoms of acid reflux, especially for individuals with pronounced H. pylori infection.27 The researchers concluded a daily dose of 40 mg of astaxanthin was effective for reflux reduction. |
| Baking soda — One-half to 1 teaspoon of baking soda (sodium bicarbonate) in an 8-ounce glass of water, or orange juice, will help neutralize your stomach acid and ease the burn of acid reflux. While I do not advise this as an ongoing remedy, it is effective on an “emergency” basis when you are in excruciating pain. |
| Ginger root — Ginger has a gastroprotective effect by suppressing H. pylori. It also accelerates gastric emptying which, when impaired, contributes to heartburn. Add two or three slices of fresh ginger root to 2 cups of hot water and let it steep for several minutes. Drink it about 20 minutes prior to your meal. |
| Sauerkraut — Consuming sauerkraut or cabbage juice will stimulate your body to produce stomach acid. |
| Glutamine — The amino acid glutamine has been shown to address gastrointestinal damage caused by H. pylori. Glutamine is found in many foods, including beef, chicken, dairy products, eggs, fish and selected fruits and vegetables. L-glutamine is widely available as a supplement. |
| Ripe papaya or a papain supplement — Papaya contains papain, an enzyme useful for breaking down both protein and carbohydrates. |
| Fresh pineapple or bromelain supplement — Bromelain is a proteolytic enzyme found in pineapple that helps digest proteins. |
| Pepsin supplement — Like bromelain, pepsin is a proteolytic enzyme involved in protein digestion.28 |
| Betaine HCI supplement — Betaine HCl is the hydrochloride salt of betaine, not to be confused with betaine or trimethylglycine (TMG). As noted in a 2020 review paper:29 “… the most common recommendation for the use of betaine HCl supplements is usually implemented using an empirical test for low stomach acid whereby increasing doses of betaine HCl are given during sequential meals until such time as an uncomfortable sensation is noticed by the patient.
Along with improvements in symptoms of dyspepsia (or laboratory analysis of improved protein digestion), the lack of side-effects acts is an empirical confirmation that low gastric acid production was contributing to poor digestion and/or dyspeptic symptoms.” |
| Bitters — Bitters have a long history of use in herbal medicinal traditions to promote digestion and/or to relieve digestive complaints.30 |
| Slippery elm — Slippery elm coats and soothes your mouth, throat, stomach and intestines, and contains antioxidants that may help address inflammatory bowel conditions. Because it stimulates nerve endings in your gastrointestinal tract, it is useful for increasing mucus secretion, which has a protective effect against ulcers and excess acidity. |
| Vitamin D — Vitamin D is important for your gut health. Once your vitamin D levels are optimized, you will benefit from your body’s production of about 200 antimicrobial peptides that will help eradicate gut infections. |
| Zinc — Your stomach needs zinc to produce stomach acid, so make sure your body has the necessary raw ingredients. The recommended daily amount for adults is 8 to 11 mg. Zinc rich foods include oysters, lobster, beef, cashew nuts, beans and raw yogurt.31 |
Talk to Your Doctor About Getting Off PPIs
If you’re currently on a PPI, I strongly recommend working with your doctor to wean off it, as inhibiting stomach acid can raise your risk of other, far more serious health conditions, including:32
| Asthma | Depression |
| Gallbladder disease | Migraines |
| Macular degeneration | Osteoporosis |
| Autoimmune conditions, including but not limited to Celiac disease, Type 1 juvenile diabetes, Grave’s disease (hyperthyroid), lupus, multiple sclerosis (MS), rheumatoid arthritis and ulcerative colitis |
The best and safest way to do that is to work with your doctor to lower the dose you’re taking while simultaneously implementing the following lifestyle modifications:
- Avoid reflux triggers and/or any food that irritates your stomach
- Avoid processed foods and sugar
- Eat a Mediterranean diet, focused on fruits, healthy fats, lean meats, nuts and vegetables. Research published in the Journal of the American Medical Association Otolaryngology — Head & Neck Surgery found a Mediterranean diet was as effective as PPIs in treating acid reflux symptoms33
- Reseed your gut with beneficial bacteria from traditionally fermented foods or a high-quality probiotic supplement
- Thoroughly chew each bite of food
Once you get down to the lowest dose of the PPI, you can start substituting with an over-the-counter H2 blocker like Pepcid (famotidine) which appears to be the safest of all the options out there. Then, gradually wean off the H2 blocker over the next several weeks.
Other medications are also notorious for slowing down digestion and causing constipation. Opiates and anticholinergic drugs, for example, suppress involuntary muscle movements, thereby inhibiting peristalsis, so if your digestion is impaired and you’re on either of these drugs, you may want to discuss alternatives to these drugs with your doctor as well.
- 1 Gastro.org September 14, 2022
- 2 National Institute of Diabetes and Digestive and Kidney Diseases, Stats for the US
- 3 Journal of Clinical Medicine 2023; 12(16): 5272
- 4 Science Daily July 15, 2013
- 5, 6 Circulation 2017; 136: A20249
- 7 Sports Medicine 2022; 52: 1765-1787
- 8 Sports Medicine 2015; 45: 659-678
- 9 PLOS ONE May 29, 2020 DOI: 10.1371/journal.pone.0234089
- 10 Very Well Fit May 25, 2022
- 11 Fluoride 2005; 38(3): 215-219 (PDF)
- 12, 13, 14, 19, 20, 21, 32 Midwestern Doctor Substack September 16, 2023
- 15 Acta Biomedica 2018; 89(Suppl 8): 40–43, H. pylori and reflux disease
- 16 JSLF April-June 2012; 16(2): 260–263
- 17 Acta Biomedica 2018; 89(Suppl 8): 40–43, Conclusion
- 18 Acta Biomedica 2018; 89(Suppl 8): 40–43, Reflux disease and esophagitis, definition and pathophysiology and Conclusion
- 22 Health January 25, 2016
- 23 Everyday Roots, 15 Natural Remedies for Heartburn & Severe Acid Reflux
- 24, 28, 31 Medical News Today 6 Ways to Increase Stomach Acid
- 25, 29, 30 Integr Med February 2020; 19(1): 32-36
- 26 Drugwatch PI Alternatives
- 27 Phytomedicine June 2008; 15(6-7): 391-9
- 33 Journal of the American Medical Association Otolaryngology – Head & Neck Surgery September 7, 2017; doi: 10.1001/jamaoto.2017.1454
How to Boost Brain Health and Reverse Neurological Disease
Reproduced from original article:
https://articles.mercola.com/sites/articles/archive/2023/07/15/boost-brain-health-reverse-neurological-disease.aspx
The original Mercola article may not remain on the original site, but I will endeavor to keep it on this site as long as I deem it to be appropriate.
Analysis by Dr. Joseph Mercola Fact Checked July 15, 2023
STORY AT-A-GLANCE
- The less inflammatory your diet is, the faster you’re going to get well, because inflammation is nearly always a contributor to neurological dysfunction. Sugar, damaged omega-6 oils, trans fats and processed vegetable oils need to be avoided
- A simple stress reduction technique done before meals can improve your digestion and absorption of nutrients, boost your immune function, and relax your body
- Melatonin provides the best protection for your neurons against free radical damage, and you need a healthy release of melatonin through the night to calm and heal your brain
- As you get older, the enzymatic activity required to produce melatonin becomes impaired. To boost your body’s production, take 5-HTP before bedtime. 5-HTP is converted to serotonin, which is further converted to melatonin
- Natural alternatives to diuretics, commonly prescribed for hypertension, are discussed, as are the many health benefits of proteolytic enzymes
Editor’s Note: This article is a reprint. It was originally published June 10, 2018.
Your brain is a really important part of your body. I’m sure no one would disagree with that. In this interview, Dr. Lee Cowden, co-founder of the Academy of Comprehensive Integrative Medicine (ACIM), discusses some really simple and inexpensive strategies that boost brain health and support neuroregeneration. This is also the topic of this year’s ACIM conference, which will be held in Orlando, Florida, in November.
The Academy of Comprehensive Integrative Medicine was founded in 2008 with the vision of educating integrative practitioners around the globe, for the most part online. “Many practitioners are so busy that they can never take the time to go to all of the meetings they need to go to, to learn what they need to learn,” Cowden says, “so we decided to start putting educational courses online.”
ACIM Offers Training Programs
In 2014, ACIM began offering a 300-hour online integrative medicine fellowship training program. Workshops are held in Dallas every few months to allow practitioners to get hands-on training. In 2018, there were hands-on conferences in July and September 20. Those were all preludes to the main conference in Orlando in November.
“Everything we’re doing this year is focused on the brain [and] neuroregeneration,” Cowden says. “With integrative medicine, we look at the causation, and see if we can resolve the causation of the illness. Once the cause goes away, usually the illness goes away.”
You don’t have to be a health care professional to benefit from ACIM. Even laypeople can study with ACIM.
The academy offers a core wellness coach program that includes 70 hours of training. “I think every integrative practitioner needs to have half a dozen or more wellness coaches working with them to hold the hands of the patients until they get well,” Cowden says.
ACIM Conference 2018: Neuroregeneration
The November conference focused on strategies that can help regenerate all types of neurological conditions, including Alzheimer’s, autism, multiple sclerosis, amyotrophic lateral sclerosis, Parkinson’s disease and other less severe conditions such as the neurological effects of fibromyalgia, and less common conditions such as reflex sympathetic dystrophy and peripheral neuropathy.
“The tendency of the American public is to look for a magic bullet. But, really, for neurological diseases, I haven’t found a magic bullet. There’s a lot of very important pieces.
I call those the foundational pieces: Diet, removing electromagnetic fields (EMFs) from the patient’s surroundings, physical activity, as well as brain games. There are a lot of other emotional issues that impact chronic neurological conditions that we need to address as well.”
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Quenching Inflammation Is a Key Foundational Step
In regard to diet, the less inflammatory it is, the faster you’re going to get well, because inflammation is nearly always a contributor to neurological dysfunction. The most inflammatory of all foods is probably sugar, followed by damaged, oxidized omega-6 oils, trans fats and processed vegetable oils. These all need to be strictly avoided. In addition to an anti-inflammatory diet, nutritional and herbal supplements can offer targeted support.
“Eating a ketogenic diet with clean fats and oils, doing some [intermittent] fasting throughout the week and getting rid of the inflammation-creating things — sugars, omega-6 oils, peanut products that have high arachidonic acid and so on … can make a great start in getting a patient’s neurological condition improved,” Cowden says.
“In 1988, I had a colleague who had a father in a nursing home in Louisiana who had advanced Alzheimer’s. He was a full-care case. In the morning, the nurses would have to get him out of bed, dress him and feed him. He was always pooping and peeing in his pants. He couldn’t remember the names of the nurses, the family members or anybody. My colleague said, ‘Can you give me some ideas of things that will help my father?’
I said, the problem is that it’s going to take a lot of intervention, and getting that at a nursing home is not likely to happen. He said, ‘I’m pretty sure it will happen, because the head nurse of the nursing home has a mother, just like my dad, with severe dementia. She wants to see if what I try on my dad works, so that she can try it on her mom.’
I recommended a regimen: Dietary changes, supplemental nutrients and proteolytic enzymes 30 minutes before food, magnesium, vitamin D3, tocotrienols, tocopherols, bacopa monieri, other herbs, homeopathics and some things to get the metals out … chlorella … dimercaptosuccinic acid (DMSA) and so on.
I said, ‘You need to get your dad out of bed and walk him every day. Get the nurses to do this. Get them to play brain games with him.’
He called me back about four months later. He said, ‘I’ve got to give you an update on this … My dad now gets out of bed, dresses himself, feeds himself, does not poop or pee in his pants anymore. He walks around with the nurses and helps them take care of the other patients in the nursing home.
Then he sits down and plays cards with the nurses, and sometimes wins.’ That’s a big shift in just four months’ time, [and] we’ve had lots of other cases like that with dementia.”
Can You Reverse Autism?
Cowden has also seen near-magical improvements in children with autism. A remarkable case is that of a young man named Bryan. Cowden first met Bryan’s dad when Bryan was just 7 years old. He had neither speech nor socialization skills.
His dad was a restaurant owner who went back to school to become a naturopathic doctor in a desperate attempt to help his son after all of his allopathic doctors told him there was no hope for Bryan — he’d never graduate high school, go to college, hold a job, get married or have children of his own.
Cowden worked with Bryan’s father, and not only did Bryan start speaking within a year or two, he graduated high school at 18, played football in college on a scholarship and got B’s in school. After college, he became a massage therapist; fell in love, married and had two children.
He is now helping autistic children and adult patients with neurological disease to recover. I’ve met Bryan, and this story is all the more remarkable by the fact that he’s one of the healthiest people I have ever met.
There is a very objective heart rate variability test that measures the fitness of your autonomic nervous system and a variety of other variables called HeartQuest. Bryan scored virtually a perfect score on this test. From being an autistic child at age 7 to someone who’s one of the healthiest people around is a rather dramatic example showing that if you apply these principles, they really can work.
“After his dad helped him get to the point where he was able to do a lot of things for himself, Bryan became highly motivated to eat a clean diet, to do a physical activity, to drink enough water, to get enough sleep and so on,” Cowden notes. “He lives right.”
A Simple Stress Reduction Technique That Pays Dividends
The beauty of integrative medicine is that there are literally hundreds if not thousands of tools available, and sometimes the simplest, least expensive ones are among the most effective. One foundational aspect of good health is stress reduction. A stress reduction technique I learned from Cowden that has helped me decrease my sleep latency, allowing me to fall asleep really quickly when done before bed, is performed as follows:
- Place your left index finger and thumb together, then grasp a hold of these two fingers with your right hand (see video demonstration starting around 29:55). It’s important to use your left fingers, as the left side of your body entrains the right side of your body rather quickly, whereas the right side entrains the left very slowly.
- Place your hands on your lap and breathe deeply in through your nose. Hold your breath for one second before breathing out through your mouth. Keep breathing in through your nose and out through your mouth while visualizing yourself in the most relaxing place you have ever been. Be sure to include sound, taste, touch and smell in your visualization and not just the visual component. Really remember that place with all of your senses.
Doing this for four to five minutes before each meal will help improve your digestion and absorption of nutrients, boost your immune function, and relax your body. Done before bedtime, it’ll improve how fast you fall asleep, how deeply you fall asleep and the amount of healing your body can get while asleep as it boosts your immune function. For very little time, energy and effort, at no cost, you can get a lot of improvement. Cowden explains the rationale for these specific finger holds:
“On the index finger, on the middle-finger finger side, the dorsal surface, is the energy pathway for your nervous system. On the palm-side surface of the index finger is the energy pathway for your neurotransmitter system. On the thumb, on the outer aspect, is the pathway for your lymphatic system. Everybody who is chronically stressed has a stressed-out nervous system, stressed-out neurotransmitters and a clogged lymphatic system.
When you hold [your left index finger and thumb] with your right hand, you’re taking the excess energy that’s usually in these other pathways and dissipating that into the pathways that run on the palm surface of your right hand. If there are areas or pathways that are deficient in energy, then energy comes out of the pathways in your right hand and goes into the pathways in your left hand.
The principle is balancing the energy pathways. The Chinese have said for 3,000 years that disease develops whenever energy stagnates. If you stagnate energy, then you’re going to have all kinds of problems, including maldigestion and insomnia … This helps, probably more than anything I’ve found, to balance the sympathetic and parasympathetic nervous system.
The sympathetic is what causes the fight-or-flight. The parasympathetic, which is to balance out the sympathetic, is responsible for digestion, relaxation, sleep and the calming parts of our nervous system. So many people have almost exclusively, sympathetic and almost no parasympathetic function.”
5-HTP Boosts Melatonin and Helps Optimize Sleep
Another gem I learned from Cowden during a visit to my home was the use of 5-hydroxytryptophan (5-HTP). My deep sleep measured at zero minutes, despite spending time at the beach daily to expose myself to bright sunshine and using blackout drapes to sleep in the dark. I also turned off the electricity to my bedroom. I thought that’s all you needed to optimize melatonin. It turns out that’s not the case when you get older. Cowden explains:
“Tryptophan, which you find in turkey and pumpkin seeds, gets converted to 5-HTP. 5-HTP is converted to 5-hydroxytryptamine, also called serotonin. 5-hydroxytryptamine finally gets converted into melatonin. However, as we age, toxins pile up in the enzymes [responsible for these conversions] and prevent those enzymes from performing the work they need to do.
You have, over time, lower and lower levels of 5-HTP, serotonin and melatonin, even though you’re doing everything else right. So, yes, we have to continually detoxify, and also, sometimes, support those enzyme systems by what we call excessive precursor supply. You boost the building blocks to make the final product.
Melatonin is not very well absorbed out the gut. Some people take melatonin, but some people have kind of a paradoxical response from that. But if they take 5-HTP, they can actually make as much 5-hydroxytryptamine as they need to fairly easily, and then they have the serotonin and melatonin.”
Low Serotonin Will Impede Melatonin Production
Once I began taking 100 milligrams of 5-HTP about 20 minutes before bed, my deep sleep rapidly increased to about 30 minutes a night. Since then I’ve also painted my bedroom with grounded shielding paint that provides an ultra-low EMF environment. Turning off the electricity wasn’t enough, as assessed by measuring the electric field’s influence on my body voltage. Hopefully that’ll improve my deep sleep further.
Many are aware that serotonin is important for mood, but if you don’t have enough of it, you can’t make melatonin either, and melatonin is the most important antioxidant nutrient in the brain. As noted by Cowden, melatonin is far more important than the oral antioxidants you may take. It’s even more important than glutathione and superoxide dismutase, because it’s fat-soluble.
Melatonin provides the best protection for your neurons against free radical damage, and you need a healthy release of melatonin through the night to calm and heal your brain.
The enzyme that converts 5-HTP to serotonin requires vitamin B6 as a cofactor, so if you’re taking 5-HTP and not seeing results, that means you probably need to take some coenzymated B6 (pyridoxal 5′-phosphate) sublingually to get enough of the active form of B6 to enable the conversion of 5-HTP to serotonin.
The Many Benefits of Magnesium
Another supplement that is helpful for sleep is magnesium. Cowden prefers magnesium malate, but you can also use magnesium threonate. There are literally dozens of different types of magnesium supplements.
Magnesium threonate has the added benefit of providing some antiretroviral activity, and retroviruses tend to be a challenge inherent with many neurodegenerative diseases. Threonate is also a neurotransmitter, in addition to being an amino acid.
To avoid creating an imbalance, it’s wise to alternate between different forms of magnesium. Cowden prefers magnesium malate because malic acid is a Krebs citric acid cycle intermediate and actually helps generate more ATP energy. If you’re deficient in malic acid inside the cell and you take a magnesium malate, the malic acid is drawn into the interior of the mitochondria and will drag the magnesium in with it.
Without a doubt, magnesium is essential for mitochondrial ATP production. About 50% of the metabolic enzymes in your body require magnesium as a cofactor, so it’s a really important nutrient. It’s also required for conduction of nerve impulses and the contraction-relaxation cycle of muscles, including your heart muscle.
There’s also compelling evidence suggesting magnesium may reduce the impacts and side effects of EMF exposure. Importantly, if you don’t have enough magnesium, your body also cannot absorb potassium. Cowden explains:
“If a person is deficient in magnesium and potassium both, you can give them potassium in large amounts on an ongoing basis, and their potassium levels never come up. But if you give them magnesium and get it repleted, and then give them potassium, then their potassium levels come up.
That’s because the kidney tubules selectively hold on to magnesium and waste potassium into the toilet in order to retain the magnesium. Because, apparently, the body sees the magnesium as being a more vital nutrient than potassium.
One more thing. A lot of people in the United States are on some form of diuretic medication, either for blood pressure, swelling of their legs or for some other reason. When you take a diuretic, it has a magnesium- and potassium-wasting effect on the kidneys. They’re wasting both magnesium and potassium into the toilet. But most doctors only give potassium. They don’t give the magnesium.”
Alternatives to Diuretics
Diuretics are frequently prescribed for high blood pressure and/or swelling in the extremities. As in most cases, drugs are not necessary for treating these conditions. Swelling of the legs is often due to congestion in your lymphatic system, or kidney toxicity preventing your kidneys from properly processing water. Hence the water is retained in your tissues. Sometimes, it’s just severe toxicity in the tissues.
“One of the ways the body protects itself from toxic overload is to allow water to go out into the tissues where the toxins are, to dilute the toxins. If you have enough toxicity in your legs, then you’re going to have fluid accumulation there to try to dilute those toxins,” Cowden explains. “The lymphatic system can get clogged up for lots of different reasons.
The lymphatic system is commonly clogged up in people in the United States, because they have a love affair with dairy products and wheat products, both of which produce thick sticky mucoid material in the lymphatic system, which clogs it up. If they’ll get rid of the dairy and wheat products, then the lymphatic system becomes more fluid and able to clear toxins from the tissues through the lymphatic system.”
If you have an extremely weak heart, you may not be able to pump blood properly. This is also known as right-sided congestive heart failure. A very common cause of that is coenzyme Q10 (CoQ10) deficiency. According to Cowden, taking CoQ10, addressing any emotional issues and eliminating heavy metals will help the swelling to go away even in these more serious cases.
Why Diuretics Are Not Ideal for Treatment of Hypertension
Hypertension is a more complex issue. The first line of treatment and the No. 1 recommended drug for treating hypertension are thiazide diuretics. However, thiazide diuretics cause chromium wasting, which then creates insulin resistance, which in turn raises your blood pressure. As noted by Cowden:
“That seems to be a pretty oxymoronic way to do that. We really need to try to find a better solution. Most people who have hypertension emotionally feel under pressure to do something or not do something. If they can recognize what that is and resolve that emotional conflict, their blood pressure usually goes down quite a bit …
If you get the plaque reversed in the arteries, then the [arteries] are no longer stiff, so then you don’t have a systolic hypertension. You don’t need the drug, because your blood pressure comes down just by getting rid of the plaque in the arteries.
How do you do that? In the early ’90s, I was giving patients with advanced atherosclerotic disease proteolytic enzymes 30 minutes before food, a clean diet, supplements, nutrients, magnesium, vitamin C, vitamin E, etc., and reversing 80% to 90% plaque in the arteries down to 20% and 30% plaque in just three or four months.
We proved that with the ultrasound Doppler duplex imaging. If we can do that, then why are we doing open heart surgeries, carotid endarterectomies and all that other stuff? It’s because people are not educated about what’s possible.
If they haven’t been told that this could be done by their medical doctor, then they don’t believe that it’s possible. Unfortunately, there are a lot of things the medical doctor doesn’t know, because they weren’t taught it in medical school.”
The Benefits of Proteolytic Enzymes
Proteolytic enzymes are an effective strategy not only for decreasing atherosclerotic plaque but also for thinning your blood, lowering your risk of a blood clot. Cowden’s father was placed on Coumadin by his doctor, which caused him to bleed profusely whenever he hurt himself working outside. Cowden suggested proteolytic enzymes instead, which his father was eager to try.
“He started that when he was about 60. He lived to be 80. He was on proteolytic enzymes 30 minutes before food twice a day for 20 years, without any more clots, without any more of the symptoms for which he was being treated with the sodium warfarin or the Coumadin.
Since then, I’ve treated several dozen other patients with the same strategy. As far as I know, there’s no peer-reviewed literature proving that this is so, but we have lots of anecdotal evidence … As far as I know, everybody has remained plaque-free.”
The enzymes Cowden uses for this purpose, in order of effectiveness are:
- Lumbrokinase, made from bacteria that live in the gut of the earthworm
- Nattokinase, a fermented soy product
- Serrapeptase, made from bacteria that grow in the gut of the silkworm
- Bromelain, obtained from pineapple stems
- Papaya leaf enzyme
“A person can be energetically tested for several of these enzymes to see which pair is the best pair and just rotate back and forth. Monday, Wednesday and Friday, one; Tuesday, Thursday, Saturday and Sunday the other.
If they do enough of those, then usually they’ll have no clot formation,” he says. Proteolytic enzymes also combat tiny clots, frequently caused by chronic infections. The infection, wherever it is located, causes your body to produce excessive amounts of fibrin, a clot-producing agent.
This fibrin can plaster itself up against the capillary walls, restricting the delivery of oxygen from red blood cells through the capillary wall into the tissues.
The above-mentioned enzymes will strip away fibrin, allowing oxygen delivery through the capillary walls into tissues. Once the tissues are no longer starved of oxygen, they can go into aerobic metabolism instead of anaerobic metabolism, and when you’re in anaerobic metabolism, you don’t stimulate cancer growth and microbial growth. So, there are many related health benefits.
Could Aspirin Have Cut COVID Deaths in Half?
Reproduced from original article:
https://articles.mercola.com/sites/articles/archive/2023/05/15/aspirin-for-covid.aspx
The original Mercola article may not remain on the original site, but I will endeavor to keep it on this site as long as I deem it to be appropriate.
Analysis by Dr. Joseph Mercola Fact Checked May 15, 2023
STORY AT-A-GLANCE
- There was a massive discrediting propaganda campaign hurled at aspirin by Big Pharma fifty years ago when it came out with expensive and dangerous non-steroidal anti-inflammatories (NSAIDs)
- Aspirin is a staple medicine that is frequently recommended as a remedy to control inflammation and prevent blood clots. It could have helped limit the pandemic death toll, had it not been downplayed and ignored
- According to research published in April 2021, aspirin reduced COVID-19 patients’ need for mechanical ventilation by 44%, ICU admission by 43% and mortality by 47%
- Proteolytic enzymes like lumbrokinase, serrapeptase and nattokinase are safer and perhaps even superior choices to aspirin for its anticlot properties. These enzymes, when taken on an empty stomach, act as natural anticoagulants by breaking down fibrin
- Proteolytic enzymes may also be helpful for long-COVID. Researchers have found that people who die from COVID have extensive lung damage caused by persistent virus-infected cells that cause scar formation. Proteolytic enzymes can help dissolve this scar tissue, as fibrin is a primary component
Aspirin (acetylsalicylic acid) was introduced in 1899 as an alternative to sodium salicylate,1 a pain reliever and anti-inflammatory known for its unpleasant side effects such as stomach cramps, heartburn, nausea and vomiting. It’s been a staple medicine in most households ever since and is frequently recommended as a remedy to control inflammation and prevent blood clots that can lead to stroke and heart attack.
Aspirin also has other health benefits. It helps increase the oxidation of glucose as fuel for your body while inhibiting the release of fatty acids from your fat cells, specifically linoleic acid (LA), an omega-6 fat which I suspect is a primary driver of chronic disease.
This is important because nearly everyone in the U.S. has excessive LA in their tissues, as it takes seven years of a low LA diet to get it down to healthy levels. So, the last thing you want to do is increase the release of LA into your body from fat stores. It is far better to release LA slowly and allow your liver to process it. It is water soluble, so you can urinate it out without it being metabolized into inflammatory prostaglandins.
Importantly, aspirin will also lower your baseline cortisol — indirectly by lowering inflammation, and directly by inhibiting the enzyme 11-beta-hydroxysteroid dehydrogenase Type 1. This enzyme synthesizes active cortisol from the inactive precursor cortisone.
Aspirin lowers the production of stressed induced aldosterone, which can help to lower blood pressure. Aspirin increases your levels of carbon dioxide and progesterone while inhibiting the major inflammatory pathway, NF kappa-B, which will help your body naturally increase the synthesis of two powerfully important hormones that your body needs, testosterone and progesterone.
Aspirin also uncouples mitochondria. Uncoupling of mitochondrial oxidative metabolism from ATP production can help to increase your metabolic rate and help you lose weight. Dinitrophenol (DNP) is a drug that, like aspirin, uncouples mitochondrial metabolism and produces incredible weight loss. Sadly, it has a very low therapeutic index, so its effective dose is close to its toxic dose and is widely considered too dangerous for clinical use and is no longer available in the U.S.
Aspirin Reduced COVID-Related Hospital Deaths by 47%
Aspirin could also have helped limit the pandemic death toll, had it not been downplayed and overlooked. Many news outlets and COVID-specific websites warned against the use of aspirin for COVID infection, saying it could cause serious bleeding.
While bleeding is a potential side effect, aspirin is no riskier than other anticoagulants, such as heparin,2,3,4 which was recommended by the National Institutes of Health.5
According to research6 published in April 2021, aspirin significantly reduced COVID-19 patients’ need for mechanical ventilation, ICU admission and subsequent mortality. The retrospective, observational cohort study included patients admitted for COVID infection at multiple hospitals across the U.S. between March and July 2020. As reported by General Surgery News:7
“The study’s principal investigator, Jonathan Chow, MD, an assistant professor of anesthesiology and critical care medicine at George Washington University, in Washington, D.C., said:
‘At the beginning of the pandemic, in March and April of 2020, my colleagues and I observed that all these COVID patients in the intensive care unit began to develop excess clot formation and complications related to blood clots and microclot formation throughout the body.’
Numerous autopsy studies from last spring showed these patients had activation of platelets throughout the body and an excessive number of precursors to platelets, according to Dr. Chow.
‘That got us thinking, ‘Why don’t we start using an antiplatelet medication, such as aspirin, to treat these patients?’ he said. ‘Aspirin has been studied extensively in cardiovascular disease to prevent clot formation, and it is widely available and inexpensive.’”
Chow and his team reviewed the charts of 412 patients, 23.7% of whom had either received aspirin within 24 hours of admission, or had taken aspirin for at least seven days prior to admission, and 76.3% who did not.
After adjusting for several confounding variables, including comorbidities, aspirin was independently associated with a:
- 44% decreased risk for mechanical ventilation
- 43% reduced risk for ICU admission
- 47% decrease in hospital mortality
Based on this research, it appears COVID-19-related hospital deaths could have been cut nearly in half, had aspirin been routinely used. Chow commented on the results:8
“The results of the study do not really surprise us because we know that COVID causes excess clot formation and we know that aspirin is a very potent blood thinner. So, when you have a disease that causes clots and a medication that thins your blood, that may lead to the protective effects that we found.”
Aberrant Coagulation in Severe Influenza Pneumonia
As in COVID-19, pneumonia caused by influenza also involves microclotting in the lungs. According to research published in 2016, aberrant coagulation is what causes a hyperinflammatory response in severe influenza pneumonia:9
“Dysfunctional coagulation is a common complication in pathogenic influenza, manifested by lung endothelial activation, vascular leak, disseminated intravascular coagulation and pulmonary microembolism.
Importantly, emerging evidence shows that an uncontrolled coagulation system, including both the cellular (endothelial cells and platelets) and protein (coagulation factors, anticoagulants and fibrinolysis proteases) components, contributes to the pathogenesis of influenza by augmenting viral replication and immune pathogenesis.”
This paper also highlighted the benefits of aspirin, noting it:10
- Protects mice from lethal influenza virus infection
- Acts as an anti-influenza virus agent in vitro by inhibiting pro-inflammatory NF-κB activity
- Improves influenza outcomes
- Potentially inhibits platelet activation
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Fibrinolytics May Be the Key
According to the 2016 paper above, “Fibrinolysis is involved in both lung inflammation and the influenza A virus life cycle.” Fibrinolysis is a process that prevents blood clots from forming and growing. This is part of your body’s normal processes, but sometimes the clotting becomes too excessive, requiring a fibrinolytic to help break down the clots that have already formed.
Fibrin is the material that blood clots are made of, and while aspirin can help break them down, I believe proteolytic enzymes like lumbrokinase, serrapeptase and nattokinase are superior choices.
These enzymes, when taken on an empty stomach, away from food, act as natural anticoagulants by breaking down fibrin. They must be taken at least one hour before or two hours after meals containing protein, though. Otherwise, they’ll be wasted in the digestion of the protein in your food and won’t be able to activate their fibrinolytic properties.
Fibrinolytic Enzymes for COVID-19
Another paper11 published in July 2020, this one a case series, also hints at the usefulness of fibrinolytic enzymes for COVID. It presented three case studies of patients with severe COVID‐19 respiratory failure who were treated with tissue plasminogen activator (TPA), a serine protease enzyme found on endothelial cells that is involved in the breakdown of blood clots.12
All three patients benefited from the treatment, with partial pressure of oxygen/FiO2 (P/F) ratios, a measure of lung function, improving from 38% to 100%.
Other research13 has shown that the thrombolytic activity of equivalent amounts of nattokinase and TPA are identical, so nattokinase could be a useful alternative. The benefit of nattokinase is that you can take it at home, without a prescription, while TPA is an emergency stroke treatment that is only given intravenously to patients suspected of having an ischemic stroke.
Considering fibrinolytic enzymes are thrombolytics comparable to both aspirin14 and TPA, it seems reasonable to conclude that they can be helpful in the treatment of COVID-19.
Fibrinolytic Enzymes May Be Useful in Long-COVID as Well
Another paper15 published in November 2020 highlighted that people who died from COVID-19 had extensive lung damage, including clotting and long-term persistence of virus cells in pneumocytes and endothelial cells.
The findings indicate that virus-infected cells may persist for long periods inside the lungs, contributing to scar tissue. In an interview with Reuters,16 study co-author Mauro Giacca, a professor at King’s College London, described “really vast destruction of the architecture of the lungs,” with healthy tissue “almost completely substituted by scar tissue.”
This scar tissue, Giacca said, may be responsible for so-called “long COVID,” in which symptoms persist for months after the infection has cleared up. “It could very well be envisaged that one of the reasons why there are cases of long COVID is because there is vast destruction of lung (tissue),” he told Reuters. “Even if someone recovers from COVID, the damage that is done could be massive.”
The good news is that proteolytic enzymes can help dissolve scar tissue as well, as fibrin is a primary component. I would alternate between lumbrokinase and serrapeptase, as you’ll need to take it for about three months and sensitivity can develop over time if you use any one of them daily without interruption.
A Breakdown of the Top Three Fibrinolytics
While lumbrokinase, nattokinase and serrapeptase are all effective thrombolytics, lumbrokinase is by far the most potent, which is why it’s my personal favorite. Lumbrokinase is 30 times more potent than nattokinase and 300 times more potent than serrapeptase.17,18,19
This means you need much higher doses if you’re taking nattokinase or serrapeptase, compared to lumbrokinase. That said, as just mentioned, if you intend to take a fibrinolytic enzyme daily, I recommend alternating them to prevent a sensitivity or allergy from developing. Also remember that they must be taken on an empty stomach.
Aside from potency, each enzyme also has its own set of benefits that might make one preferable over another:
1. Lumbrokinase — A highly effective antithrombotic agent that reduces blood viscosity and platelet aggregation20 while also degrading fibrin, which is a key factor in clot formation.
I recommend that everyone keep some high-quality lumbrokinase in your emergency kit. A while back I developed a significant bruise from a weight training injury. I took a high dose of lumbrokinase for a week, which cleared it up.
I also took lumbrokinase after being stung by three wasps on my forehead right before bed. The stings swelled to nearly the size of half a tennis ball. Wasp venom contains proteins that fibrinolytic enzymes can break down, so I took half a dozen pills and went to sleep.
The next morning, the swelling was nearly gone. If you are going to try this, the sooner you take it after you’re stung, the better it will likely work as it denatures the venom proteins before they inflict their damage.
2. Serrapeptase — Research has shown serrapeptase can help patients with chronic airway disease, lessening the viscosity of sputum and reducing coughing.21 Serrapeptase also breaks down fibrin and helps dissolve dead or damaged tissue without harming healthy tissue.22
3. Nattokinase — Nattokinase has been shown to break down blood clots and reduce the risk of serious clotting23 by dissolving excess fibrin in your blood vessels,24 improving circulation and decreasing blood viscosity.
Aspirin Has Benefits Similar to Fasting
I have long been a fan of fasting for many reasons, but primarily because it has been known to lower biomarkers of inflammation as well as increase autophagy. Interestingly, there was a study done that suggests that aspirin also does precisely this. The study was in mice and used 8 mg/kg which is the equivalent of about two 5 grain (325 mg) tablets a day.25
The study showed that aspirin, or its active metabolite salicylate, caused autophagy by inhibiting the acetyltransferase activity of EP300 which is a specific gene, also known as p300, which codes for proteins that regulate the activity of many genes in tissues throughout your body. It plays an essential role in controlling cell growth and division, prompting cells to mature and take on specialized functions.
Purchasing Guidelines for Aspirin
Getting back to aspirin, if you do decide to use aspirin, be sure to avoid coated extended-release aspirin. It’s not recommended due to the additives they put in it. Immediate-release aspirin is the preferred version and can be found on Amazon.
Look carefully at the list of inactive ingredients. The only one should be corn starch. I looked long and hard and found one that meets all those criteria. The recommended dose is one 325 milligram tablet per day with your largest meal.
Earlier this year I became convinced of the prophylactic value of aspirin, and I now take 325 mg per day. But I use a version that is not a tablet and is 99% pure USP aspirin. I find its prometabolic, antilipolytic, anti-inflammatory, anticortisol, and anti-estrogen effects very appealing, and its safety is well-established.
It is important to understand that there was a massive discrediting propaganda campaign hurled at it by Big Pharma when it came out with its panoply of expensive and dangerous non-steroidal anti-inflammatories (NSAIDs) fifty years ago. Many may not recall that I was the first person on the internet to warn the dangers of one of these NSAIDs, Vioxx, a year before it was released into the market and killed around 100,000 people.
If you are sensitive to aspirin, it would be best to use a salicylic acid or willow bark supplement. When you consume aspirin, the acetylsalicylic acid is metabolized in your body into salicylic acid, which is the compound responsible for the anti-inflammatory, pain-relieving and antithrombotic effects of aspirin. This can be found in willow bark.
To learn more about the risks and benefits of aspirin, and how it compares to fibrinolytic enzymes, see “Daily Aspirin — Healthy or Harmful?”
- 1 BMJ December 23, 2000; 321(7276): 1591-1594
- 2 Annals of Internal Medicine June 4, 2013; 158(11): 800-806
- 3 University of Maryland Aspirin Study
- 4 University of Maryland Medical Center Press Release January 18, 2023
- 5 NIH Antithrombotic Therapy in Patients With COVID-19, Updated December 1, 2022
- 6 Anesthesia & Analgesia April 2021; 132(4): 930-941
- 7, 8 General Surgery News August 4, 2021
- 9, 10 Cellular & Molecular Immunology April 4, 2016; 13: 432-442
- 11 Journal of Thrombosis and Haemostasis July 2020; 18(7): 1752-1755
- 12 Diapharma, Tissue Plasminogen Activator
- 13 Scientific Reports. Article Number 6210. April 18, 2018
- 14 Lab Anim Res December 2013; 29(4): 221-225
- 15 EBioMedicine November 3, 2020; 6: 103104
- 16 Reuters November 3, 2020
- 17 Townsend Letter May 2018
- 18 Enzymatic Activity Comparison of Common Fibrinolytic Enzymes 2011
- 19 Lumbrokinase Reference List May 2018
- 20 Trials 2022; 23, Article number: 285, Introduction
- 21 Respirology September 2003;8(3):316-20
- 22 International Journal of Surgery April 2013;11(3):209-217
- 23 Scientific Reports 2015; 5: 11601
- 24 Biol Pharm Bull. 1995 Oct;18(10):1387-91
- 25 Cell Rep. 2018 Feb 27; 22(9): 2395-240
Are Fibrinolytics Key to Preventing Clogged Arteries?
Reproduced from original article:
https://articles.mercola.com/sites/articles/archive/2023/04/15/fibrinolytic-enzymes-for-heart-health.aspx
The original Mercola article may not remain on the original site, but I will endeavor to keep it on this site as long as I deem it to be appropriate.
Analysis by Dr. Joseph Mercola Fact Checked April 15, 2023
STORY AT-A-GLANCE
- Lumbrokinase, serrapeptase and nattokinase are proteolytic enzymes that act as natural anticoagulants by breaking down fibrin that forms blood clots
- Fibrinolytic enzymes are antihypertensive, anti-atherosclerotic, lipid-lowering and anti-platelet agents, which also have neuroprotective effects
- Nattokinase at a dose of 10,800 fibrinolytic units (FU) a day for 12 months “effectively managed the progression of atherosclerosis and hyperlipidemia” in one study
- Just one 2,000 FU dose of nattokinase enhanced fibrinolysis and anti-coagulation, activating multiple fibrinolytic and anti-thrombotic pathways simultaneously
- Lumbrokinase is nearly 30 times stronger than nattokinase and 300 times stronger than serrapeptase; if you are using a fibrinolytic enzyme, my strong personal preference and recommendation is to use lumbrokinase
Fibrinolytic agents, sometimes referred to as thrombolytic agents, are capable of dissolving blood clots that may block your veins or arteries. In general, cleaner arteries are a benefit to your cardiovascular health, which is one reason why fibrinolytic enzymes like lumbrokinase, nattokinase and serrapeptase should be on your radar.
In your body, enzymes regulate the rate of numerous biological reactions, speeding them up so necessary functions like digestion, muscle contractions and other aspects of cellular metabolism can occur.1
Lumbrokinase, serrapeptase and nattokinase are proteolytic enzymes that act as natural anticoagulants by breaking down fibrin that forms blood clots. Fibrin, a clotting material that restricts blood flow, is found both in your bloodstream and connective tissue such as your muscles. Fibrin accumulation is also responsible for scar tissue.
It is important to understand that when using these enzymes for fibrinolytic therapy they need to be taken on an empty stomach, at least one hour before or two hours after meals containing protein. Otherwise, these enzymes will be wasted in the digestion of the protein in your food and won’t serve their fibrinolytic purpose.
Fibrinolytic Enzymes Help Manage Heart Disease
Fibrinolytic enzymes are antihypertensive, anti-atherosclerotic, lipid-lowering and anti-platelet agents, which also have neuroprotective effects.2 Much research into fibrinolytic enzymes has focused on nattokinase (NK), an active ingredient in natto, or fermented soybeans. It’s likely due to its high nattokinase content that natto consumption is linked to a decreased risk of heart disease mortality and increased longevity in the Japanese population.3
Nattokinase, produced by the bacteria Bacillus subtilis during fermentation of soybeans to produce natto,4 is a strong thrombolytic,5 comparable to aspirin6 but without the potential side effects. It is important to note, however, that lumbrokinase is nearly 30 times more potent than nattokinase — and 300 times more potent than serrapeptase.7,8,9
So, while all of the fibrinolytic enzymes are effective and beneficial, you’ll need much higher doses of nattokinase and, especially, serrapeptase, than lumbrokinase to achieve similar effects. If you are using a fibrinolytic enzyme, my strong personal preference and recommendation is to use lumbrokinase.
That said, you can get an idea of these enzymes’ health potential via studies done on any of the types. One such study involved 1,062 people with mild hyperlipidemia and/or mild atherosclerosis. They took nattokinase at a dose of 10,800 fibrinolytic units (FU) a day for 12 months, which “effectively managed the progression of atherosclerosis and hyperlipidemia with a significant improvement in the lipid profile.”10
Significant reduction in carotid artery intima-media thickness, a measure of the extent of atherosclerotic vascular disease, was noted, with improvement rates ranging from 66.5% to 95.4%. Those who smoked, drank alcohol or had a higher BMI experienced the greatest lipid-lowering effects. No adverse effects were noted from the nattokinase.
It’s also interesting to note that regular exercise further improved nattokinase’s beneficial effects, and it also worked synergistically with consumption of vitamin K2 and aspirin. At a lower dose of 3,600 FU per day, nattokinase was ineffective at lowering lipids or suppressing the progression of atherosclerosis, highlighting the importance of proper dosing and “challenging the recommended dose of 2,000 FU per day,” the researchers explained. Further:11
“The available data suggest that the antiatherosclerotic effects of NK are due to the collective effects of the combination of the antithrombotic, anticoagulant, antioxidant and lipid lowering properties of NK or the natto extract containing NK … A possible mechanism [for NK’s lipid-lowering effects] is through NK proteolytic activity on certain protein targets involved in lipid metabolism, resulting in changes in lipid metabolism.”
A Single Dose of Fibrinolytics Has Anticoagulant Benefits
A study involving 12 men revealed that just one 2,000 FU dose of nattokinase enhanced fibrinolysis and anticoagulation.12 It activated multiple fibrinolytic and antithrombotic pathways simultaneously, the researchers explained.13 At six and eight hours after the nattokinase was taken, D-dimer concentrations were significantly elevated.
D-dimer is a protein fragment produced by the body when a blood clot dissolves. It’s typically undetectable or present only at very low levels, buts its level may significantly rise when the body is forming and breaking down blood clots,14 as occurred after one dose of nattokinase in this study. The researchers added:15
“Based on NK’s unique, comparatively strong fibrinolytic/anticoagulant activity, stability in the gastrointestinal tract and long bioavailability in vivo, NK would appear to offer potential advantages over other currently used agents for treatment and/or prevention of selected diseases processes …
NK might have an impact on not only fibrinolytic/anticoagulant pathways but also other risk factors for thrombosis, which imply as a NK’s possibility for prevention and/or treatment of the diseases.”
As mentioned, fibrinolytic enzymes inhibit platelet aggregation and the formation of blood clots similarly to aspirin. In an animal study, a 500 mg/kg dose of nattokinase fully prevented a blocked artery, as did aspirin at a dose of 30 mg/kg, demonstrating its effectiveness at improving blood flow:16
“The results indicate that nattokinase extracted from fermented soybean inhibit platelet aggregation by blocking thromboxane [a vasoconstrictor] formation, and thereby delay thrombosis following oxidative arterial wall injury. Therefore, it is suggested that nattokinase could be a good candidate without adverse effects for the improvement of blood flow.”
Brain benefits are also apparent from fibrinolytic enzymes, including nattokinase and serrapeptase (SP). In a study on rats, administering either enzyme for 45 days successfully modulated several markers of Alzheimer’s disease.17 A significant increase in brain derived neurotropic factor (BDNF) was also noted. BDNF is a member of brain growth factors that contributes to neuroplasticity, which greatly enhances cognitive performance.18,19
Download this Article Before it Disappears
Fibrinolytic Enzymes for COVID-19
Another candidate for application of fibrinolytic therapy is COVID-19, as coagulopathy appears to play a role in severe COVID-19. Researchers wrote in the Journal of Thrombosis and Haemostasis:20
“There is evidence in both animals and humans that fibrinolytic therapy in acute lung injury and acute respiratory distress syndrome (ARDS) improves survival, which also points to fibrin deposition in the pulmonary microvasculature as a contributory cause of ARDS.
This would be expected to be seen in patients with ARDS and concomitant diagnoses of DIC [disseminated intravascular coagulation] on their laboratory values such as what is observed in more than 70% of those who die of COVID‐19.”
The researchers reported three case studies of patients with severe COVID‐19 respiratory failure who were treated with tissue plasminogen activator (TPA), a serine protease enzyme found on endothelial cells that’s involved in fibrinolysis, or the breakdown of blood clots.21
All three patients benefited from the treatment, with partial pressure of oxygen/FiO2 (P/F) ratios, a measure of lung function, improving from 38% to 100%.22 An evaluation of organ tissues from people who died from COVID-19 also revealed extensive lung damage, including clotting, and long-term persistence of virus cells in pneumocytes and endothelial cells.23
The findings indicate that virus-infected cells may persist for long periods inside the lungs, contributing to scar tissue. In an interview with Reuters, study co-author Mauro Giacca, a professor at King’s College London, described “really vast destruction of the architecture of the lungs,” with healthy tissue “almost completely substituted by scar tissue,”24 which could be responsible for cases of “long COVID,” in which symptoms persist for months.
“It could very well be envisaged that one of the reasons why there are cases of long COVID is because there is vast destruction of lung (tissue),” he told Reuters. “Even if someone recovers from COVID, the damage that is done could be massive.”25 Dissolving scar tissue is another area in which enzymes, particularly proteolytic enzymes, may be useful.
The potential for blood clots is one reason why board-certified internist and cardiologist Dr. Peter McCullough uses full-dose aspirin — 325 milligrams a day — in almost everyone with long COVID syndrome who doesn’t have a major blood clot, in addition to other medications.26
However, a safer and likely equally effective alternative to aspirin is lumbrokinase and serrapeptase. You can alternate between the two enzymes — one day take lumbrokinase and the next take serrapeptase — because you’ll need to be on it for about three months and you can develop a sensitivity to them over time if you use them daily without interruption.
A Breakdown of the Top Three Fibrinolytics
Fibrinolytic enzymes are ideal for targeted usage; as mentioned, if you intend to use them daily, be sure to alternate through the following types so you don’t develop a sensitivity or allergy to them. Also, remember that they need to be taken on an empty stomach, at least one hour before or two hours after meals containing protein.
1. Lumbrokinase — As I said earlier, this enzyme is about 300 times stronger than serrapeptase and nearly 30 times stronger than nattokinase,27 making it my top recommendation if you are using a fibrinolytic enzyme. Extracted from earthworms, lumbrokinase is a highly effective antithrombotic agent that reduces blood viscosity and platelet aggregation28 while also degrading fibrin, which is a key factor in clot formation.
I recommend that everyone keep some high-quality lumbrokinase in your emergency kit. I recently had a significant bruise from a weight training injury. I took a high dose of lumbrokinase for a week and it cleared right up.
I also took lumbrokinase recently after being stung by three wasps on my forehead just before bed, which swelled to nearly the size of half a tennis ball. It occurred to me since wasp venom contains proteins that fibrinolytic enzymes can break down so I took half a dozen and went to sleep.
I was beyond surprised to see nearly all the swelling decrease. If you are going to try this the sooner you take it to the time you are bitten, the better it will likely work as it denatures the venom proteins before they do their damage to your body.
2. Serrapeptase — Also known as serratiopeptidase, serrapeptase is produced in the gut of newborn Bombyx mori silkworms, allowing them to dissolve and escape from their cocoons. Research has shown it can help patients with chronic airway disease, lessening viscosity of sputum and reducing coughing.29 Serrapeptase also breaks down fibrin and helps dissolve dead or damaged tissue without harming healthy tissue.30
3. Nattokinase — Nattokinase has been shown to break down blood clots and reduce the risk of serious clotting31 by dissolving excess fibrin in your blood vessels,32 improving circulation and decreasing blood viscosity. Interestingly, in one in vitro study, the thrombolytic activity of equivalent amounts of nattokinase and TPA were found to be identical33 — TPA, remember, is the enzyme that led to improvement in the three COVID-19 case studies.34
- 1 Britannica, Enzyme
- 2, 3 Front. Cardiovasc. Med., 22 August 2022, Intro
- 4 Int J Mol Sci. 2017 Mar; 18(3): 523
- 5, 32 Biol Pharm Bull. 1995 Oct;18(10):1387-91
- 6 Lab Anim Res December 2013; 29(4): 221-225
- 7, 27 Townsend Letter May 2018
- 8 Enzymatic Activity Comparison of Common Fibrinolytic Enzymes 2011
- 9 Lumbrokinase Reference List May 2018
- 10, 11 Front. Cardiovasc. Med., 22 August 2022
- 12, 13 Scientific Reports volume 5, Article number: 11601 (2015)
- 14 Lab Tests Online, D-dimer
- 15 Scientific Reports volume 5, Article number: 11601 (2015), Discussion
- 16 Lab Anim Res. 2013 Dec; 29(4): 221–225
- 17 Hum Exp Toxicol. 2013 Jul;32(7):721-35. doi: 10.1177/0960327112467040
- 18 Med. Hypotheses. 2017;106:1–5
- 19 Neurosci. Lett. 2016 Sep 6;630:247-253
- 20, 22, 34 J Thromb Haemost. 2020 May 11; doi: 10.1111/jth.14828
- 21 Diapharma, Tissue Plasminogen Activator
- 23 EBioMedicine November 3, 2020
- 24, 25 Reuters November 3, 2020
- 26 The Texan November 3, 2020
- 28 Trials volume 23, Article number: 285 (2022), Introduction
- 29 Respirology 2003 Sep;8(3):316-20
- 30 International Journal of Surgery, 2013 Apr;11(3):209-217
- 31 Scientific Reports 2015; 5: 11601
- 33 Scientific Reports. Article Number 6210. April 18, 2018
Are Enzymes a Key to COVID Endothelial Injury?
Reproduced from original article:
https://articles.mercola.com/sites/articles/archive/2023/02/10/coronavirus-enzymes.aspx
The original Mercola article may not remain on the original site, but I will endeavor to keep it on this site as long as I deem it to be appropriate.
Analysis by Dr. Joseph Mercola Fact Checked February 10, 2023
STORY AT-A-GLANCE
- Studies suggest damage to the endothelium, which are cells covering blood vessels, is contributing to the development of blood clots, or thrombosis, in the blood vessels of severely ill COVID-19 patients
- Enzymes may turn out to be the missing link in helping to break up clusters of clotting proteins involved in this dangerous thrombosis, which is linked to increased mortality in COVID-19
- Levels of Von Willebrand factor (VWF), a clotting protein released by endothelial cells, were found to be significantly elevated in COVID-19 patients in advanced stages of the disease
- Proteolytic enzymes such as lumbrokinase, serrapeptase and nattokinase also act as natural anticoagulants by breaking down the fibrin that forms blood clots
From Dr. Joseph Mercola
Since COVID-19 first entered the scene, exchange of ideas has basically been outlawed. By sharing my views and those from various experts throughout the pandemic on COVID treatments and the experimental COVID jabs, I became a main target of the White House, the political establishment and the global cabal.
Propaganda and pervasive censorship have been deployed to seize control over every part of your life, including your health, finances and food supply. The major media are key players and have been instrumental in creating and fueling fear.
I am republishing this article in its original form so that you can see how the progression unfolded.
Originally published: November 30, 2020
Enzymes catalyze many biological reactions in your body. They regulate the rate of these chemical reactions, speeding them up so necessary functions like digestion, muscle contractions and other aspects of cellular metabolism can occur.1
Enzymes are also emerging as key players in COVID-19, as studies suggest damage to the endothelium, which are cells covering blood vessels, is contributing to the development of blood clots, or thrombosis, in the blood vessels of severely ill COVID-19 patients.2 Enzymes may turn out to be the missing link in helping to break up clusters of clotting proteins involved in this dangerous thrombosis.
Endothelium Damage Found in Critically Ill COVID-19 Cases
After noticing blackened fingers and toes — signs of what appeared to be microvascular thrombosis, or tiny blood clots in small blood vessels — in COVID-19 patients in advanced stages of the disease, physicians at the Yale School of Medicine began running clotting tests on their patients.3
Levels of Von Willebrand factor (VWF), a clotting protein released by endothelial cells, were found to be significantly elevated, which suggested to hematologist Alfred Lee that damaged endothelial cells may be releasing large quantities of VWF, leading to clots.4 This prompted the team to screen for additional markers of endothelial cell and platelet activation in critically and noncritically ill COVID-19 patients.
The study, which was conducted in April 2020, included 68 hospitalized patients with COVID-19 and 13 asymptomatic controls. VWF antigen was significantly elevated in COVID-19 patients admitted to the intensive care unit (ICU) compared to non-ICU COVID-19 patients,5 as was soluble platelet selectin (sP-selectin), which is sometimes used as a biomarker for infection and mortality.6
Specifically, mean VWF was 565% among ICU patients and 278% among non-ICU patients while soluble P-selectin was 15.9 ng/mL compared to 11.2 ng/mL.7 “Our findings show that endotheliopathy is present in COVID-19 and is likely to be associated with critical illness and death. Early identification of endotheliopathy and strategies to mitigate its progression might improve outcomes in COVID-19,” the researchers concluded.8
Likely not coincidentally, endothelial dysfunction is also associated with insulin resistance and plays a role in the vascular complications of diabetes,9 as well as being involved in obesity and high blood pressure,10 conditions that raise the risk of severe COVID-19.
Even mild obesity may raise the risk of COVID-19 severity — COVID-19 patients with mild obesity had a 2.5 times greater risk of respiratory failure and a five times greater risk of being admitted to an ICU compared to nonobese patients. Those with a BMI of 35 and over were also 12 times more likely to die from COVID-19.11
Another study looking into the impact of coexisting health conditions like high blood pressure, heart disease and diabetes on COVID-19 outcomes found they’re linked to “poorer clinical outcomes,” such as admission to an intensive care unit, a need for invasive ventilation or death.12
It’s possible that the endothelial damage in all of these conditions plays a role in worsening COVID-19 outcomes, but it’s unclear which comes first — endothelial damage or COVID-19.
Endothelial Cells Are the ‘Main Target’ of SARS-CoV-2
Imperial College London cardiologist Thomas Lüscher told The Scientist that the endothelium is the main target of SARS-CoV-2, the virus that causes COVID-19.13 Under healthy conditions, blood cells can pass through the endothelium lining blood vessels, but when exposed to viral infections and other inflammatory agents, the endothelium becomes sticky and releases VWF.
The end result is a cascade of clotting and inflammation, both characteristics of severe COVID-19. According to a case report published April 8, 2020, “A hallmark of severe COVID-19 is coagulopathy, with 71.4% of patients who die of COVID-19 meeting … criteria for disseminated intravascular coagulation (DIC) while only 0.6% of patients who survive meet these criteria.”14
Writing in the European Heart Journal, Lüscher argues, “COVID-19, particularly in the later complicated stages, represents an endothelial disease,”15 which may help explain why multiple organ systems, including the lungs, heart, brain, kidney and vasculature, may be affected.
An additional study by Canadian researchers, published in Critical Care Explorations in September 2020, also revealed elevated VWF and soluble P-selectin levels in COVID-19 patients, along with higher glycocalyx-degradation products,16 a sign of damage to the glycocalyx, which envelops the endothelium.17 This can also be a sign of sepsis. Taken together, the research suggests that therapies targeting the endothelium may be useful for COVID-19, which is where enzymes come in.
Download this Article Before it Disappears
Enzymes Used to Treat COVID-19
With the role of coagulopathy in severe COVID-19 becoming clearer, researchers have experimented with enzymes in the treatment of the disease. Fibrinolytic therapy, which uses drugs or enzymes to break up blood clots, has been used in a Phase 1 clinical trial that showed the treatment reduced mortality and led to improvements in oxygenation.18 Further, researchers wrote in the Journal of Thrombosis and Haemostasis:19
“There is evidence in both animals and humans that fibrinolytic therapy in acute lung injury and acute respiratory distress syndrome (ARDS) improves survival, which also points to fibrin deposition in the pulmonary microvasculature as a contributory cause of ARDS.
This would be expected to be seen in patients with ARDS and concomitant diagnoses of DIC on their laboratory values such as what is observed in more than 70% of those who die of COVID‐19.”
The researchers reported three case studies of patients with severe COVID‐19 respiratory failure who were treated with tissue plasminogen activator (TPA), a serine protease enzyme found on endothelial cells that’s involved in fibrinolysis, or the breakdown of blood clots.20
All three patients benefited from the treatment, with partial pressure of oxygen/FiO2 (P/F) ratios, a measure of lung function, improving from 38% to 100%.21 While it should be noted that several of the authors have patents pending related to both coagulation/fibrinolysis diagnostics and therapeutics, the results suggest such treatments deserve further evaluation in certain COVID-19 patients.
An evaluation of organ tissues from people who died from COVID-19 also revealed extensive lung damage, including clotting, and long-term persistence of virus cells in pneumocytes and endothelial cells.22
The findings indicate that virus-infected cells may persist for long periods inside the lungs, contributing to scar tissue. In an interview with Reuters, study co-author Mauro Giacca, a professor at King’s College London, described “really vast destruction of the architecture of the lungs,” with healthy tissue “almost completely substituted by scar tissue,”23 which could be responsible for cases of “long COVID,” in which symptoms persist for months.
“It could very well be envisaged that one of the reasons why there are cases of long COVID is because there is vast destruction of lung (tissue),” he told Reuters. “Even if someone recovers from COVID, the damage that is done could be massive.”24 Dissolving scar tissue is another area where enzymes, particularly proteolytic enzymes, may be useful.
Three Top Enzymes Act as Natural Anticoagulants
Holistic prophylactic alternatives that might be beneficial against blood clots include proteolytic enzymes such as lumbrokinase, serrapeptase and nattokinase, all of which act as natural anticoagulants by breaking down the fibrin that forms the blood clot. Fibrin is a clotting material that restricts blood flow, found both in your bloodstream and connective tissue such as your muscles. Fibrin accumulation is also responsible for scar tissue.
It is important to understand that when using these enzymes for fibrinolytic therapy they need to be taken on an empty stomach, at least one hour before or two hours after meals. Otherwise these enzymes will be wasted in the digestion of your food and will be unable to serve their fibrinolytic purpose.
As noted in Scientific Reports, some of the key mechanisms by which proteolytic enzymes exert their anticoagulant effect include “defibrinogenation, inhibition of platelet aggregation, and/or interference with components of the blood coagulation cascade.”25 Here’s a closer look at these important enzymes, all of which are available in supplement form or, in the case of nattokinase, via the food natto.
1. Lumbrokinase — This enzyme is about 300 times stronger than serrapeptase and nearly 30 times stronger than nattokinase,26 making it my strong personal preference and recommendation if you are using a fibrinolytic enzyme. Extracted from earthworms, lumbrokinase is a highly effective antithrombotic agent that reduces blood viscosity and platelet aggregation27 while also degrading fibrin, which is a key factor in clot formation.
2. Serrapeptase — Also known as serratiopeptidase, serrapeptase is produced in the gut of newborn Bombyx mori silkworms, allowing them to dissolve and escape from their cocoons. Research has shown it can help patients with chronic airway disease, lessening viscosity of sputum and reducing coughing.28 Serrapeptase also breaks down fibrin and helps dissolve dead or damaged tissue without harming healthy tissue.29
3. Nattokinase — Produced by the bacteria Bacillus subtilis during the fermentation of soybeans to produce natto,30 nattokinase is a strong thrombolytic31 comparable to aspirin but without the serious side effects.32
It’s been shown to break down blood clots and reduce the risk of serious clotting33 by dissolving excess fibrin in your blood vessels,34 improving circulation and decreasing blood viscosity. Interestingly, in one in vitro study, the thrombolytic activity of equivalent amounts of nattokinase and TPA were found to be identical35 — TPA, remember, is the enzyme that led to improvement in the three COVID-19 case studies.36
- 1 Britannica, Enzyme
- 2, 3, 4, 13, 17 The Scientist November 3, 2020
- 5, 7, 8 The Lancet Haematology June 30, 2020
- 6 Biomark Insights. 2017; 12: 1177271916684823
- 9 Diabetes Obes Metab. 1999 May;1 Suppl 1:S17-22. doi: 10.1046/j.1463-1326.1999.0010s1017.x.
- 10 Circulation July 27, 2020
- 11 U.S. News & World Report July 23, 2020
- 12 medRxiv February 27, 2020
- 14 J Thromb Haermost Case Reports April 8, 2020 DOI: 10.1111/jth.14828
- 15 European Heart Journal, Volume 41, Issue 32, 21 August 2020, Pages 3038–3044
- 16 Critical Care Explorations: September 2020 – Volume 2 – Issue 9 – p e0194 doi: 10.1097/CCE.0000000000000194
- 18, 19, 21, 36 J Thromb Haemost. 2020 May 11 : 10.1111/jth.14828
- 20 Diapharma, Tissue Plasminogen Activator
- 22 EBioMedicine November 3, 2020
- 23, 24 Reuters November 3, 2020
- 25 Scientific Reports 2018; 8, Article Number 6210
- 26 Townsend Letter May 2018
- 27 BioMed Research International. Volume 2011 | Article ID 51965. 2003
- 28 Respirology 2003 Sep;8(3):316-20
- 29 International Journal of Surgery, 2013 Apr;11(3):209-217
- 30 Int J Mol Sci. 2017 Mar; 18(3): 523
- 31, 34 Biol Pharm Bull. 1995 Oct;18(10):1387-91
- 32 Lab Anim Res December 2013; 29(4): 221-225
- 33 Scientific Reports 2015; 5: 11601
- 35 Article Number 6210, Lunathrombase has in vitro thrombolytic potency but is devoid of hemolytic activity or cytotoxicity against mammalian cells
Soybean Oil Linked to Genetic and Neurological Damage
Reproduced from original article:
https://articles.mercola.com/sites/articles/archive/2023/01/20/soybean-oil-side-effects.aspx
The original Mercola article may not remain on the original site, but I will endeavor to keep it on this site as long as I deem it to be appropriate.
Analysis by Dr. Joseph Mercola Fact Checked January 20, 2023
STORY AT-A-GLANCE
- Whether partially hydrogenated, organic or genetically modified to be low in linoleic acid, soybean oil can cause dysfunction at a cellular level
- Recent research warns soybean oil can cause neurological and metabolic changes associated with autism, Alzheimer’s, anxiety, depression, obesity, insulin resistance, Type 2 diabetes and fatty liver disease
- The animal study compared the health effects of diets high in conventional soybean oil, GE soybean oil low in linoleic acid and coconut oil. Both types of soybean oil had pronounced effects on the brain
- The soybean diets caused dysfunction in about 100 different genes in the hypothalamus, including one that is responsible for producing oxytocin, which has beneficial effects on your heart
- Potential health hazards of soybean oil include the harmful health effects of unfermented soy, the potential hazards of GE soy, the harm associated with glyphosate-contaminated food, and high amounts of processed omega-6 skewing your omega-3 to omega-6 ratio
Far worse than the biologic damage caused by refined sugar is the molecular havoc caused by processed vegetable oils. Soybean oil in particular has a questionable safety profile for several reasons, and processed foods are positively loaded with it.
Whether partially hydrogenated, organic or genetically modified to be low in linoleic acid, soybean oil can cause dysfunction at a cellular level. Unfortunately, many health authorities have insisted omega-6-rich vegetable oils like soybean oil are healthier than saturated animal fats such as butter and lard, and this myth has been a tough one to dismantle, despite the evidence against it.
An estimated 94% of the soybeans grown in the U.S. are genetically engineered (GE) to tolerate herbicides,1 primarily glyphosate (the active ingredient in Monsanto/Bayer’s Roundup), which cannot be washed off. As a result, most soybean-based products are contaminated with glyphosate, which compounds their toxicity.
Soybean Oil Linked to Genetic and Neurological Damage
Most recently, research2,3,4,5 published in the journal Endocrinology warns soybean oil — the most widely consumed cooking oil in America — can cause neurological and metabolic changes associated with:
| Autism | Alzheimer’s disease |
| Anxiety | Depression |
| Obesity | Insulin resistance |
| Type 2 diabetes | Fatty liver disease |
The study, done on mice, compared the health effects of diets high in conventional soybean oil, GE soybean oil low in linoleic acid and coconut oil. As reported by Neuroscience News:6
“The same UCR research team found in 2015 that soybean oil induces obesity, diabetes, insulin resistance, and fatty liver in mice. Then in a 2017 study, the same group learned that if soybean oil is engineered to be low in linoleic acid, it induces less obesity and insulin resistance.
However, in the study released this month, researchers did not find any difference between the modified and unmodified soybean oil’s effects on the brain. Specifically, the scientists found pronounced effects of the oil on the hypothalamus, where a number of critical processes take place.”
Your hypothalamus7 is a key regulator of homeostasis and metabolism in your body, and also plays a role in your stress response and hormone regulation.
According to the authors, the soybean diets (both conventional and GE), caused dysfunction in about 100 different genes in the hypothalamus, including one that is responsible for producing oxytocin, colloquially known as “the love hormone,” which has beneficial effects on your heart.
Other dysregulated genes included ones associated with “inflammation, neuroendocrine, neurochemical and insulin signaling.” The coconut oil diet had “negligible effect.”
The fact that GE soybean oil that is designed to be low in omega-6 linoleic acid had similar effects as conventional high-linolenic acid soybean oil effects suggests linoleic acid isn’t the problem, as previously suspected. The study also ruled out another suspected soybean chemical, stigmasterol, as coconut oil enriched in stigmasterol had no ill effects.
The team will continue their investigation in an effort to identify the real culprit behind these genetic effects. In the meantime, co-author Poonamjot Deol, an assistant project scientist at the University of California Riverside, urges people to “reduce consumption of soybean oil.”
Unfermented Soy Linked to Many Health Problems
The idea that unfermented soy in general and soybean oil in particular, are healthy is refuted by thousands of studies linking unfermented soy to a wide range of health problems. In her book, “The Whole Soy Story,” Dr. Kaayla Daniel details research implicating unfermented soy in the development of:8
| Malnutrition | Digestive distress |
| Immune system breakdown | Thyroid dysfunction |
| Cognitive decline | Reproductive disorders |
| Infertility | Cancer |
| Heart disease | Food allergies |
Fermented organic soy, on the other hand, has a number of important health benefits, and are the only soy products I recommend eating. Healthy options include:
- Tempeh — A fermented soybean cake with a firm texture and nutty, mushroom-like flavor.
- Miso — A fermented soybean paste with a salty, buttery texture (commonly used in miso soup).
- Natto — Fermented soybeans with a sticky texture and strong, cheese-like flavor.
- Soy sauce — Traditionally made by fermenting soybeans, salt and enzymes; beware that many varieties on the market today are made artificially, using a chemical process.
Problematic Components in Soy
While the featured Endocrinology study was unable to identify the exact soy compound responsible for the genetic damage, there are many plant chemicals found in soy that are capable of causing problems, including:
| Phytoestrogens (isoflavones) genistein and daidzein, which mimic and sometimes block the hormone estrogen — Isoflavones resemblance to human estrogen is why some recommend using soy therapeutically to treat symptoms of menopause.
However, most of us tend to be exposed to too many estrogen compounds and have a lower testosterone level than ideal, so I believe it’s important to limit your exposure to feminizing phytoestrogens. Even more importantly, there’s evidence9 isoflavones may disturb endocrine function, contribute to infertility and promote breast cancer, which is definitely a significant concern. As noted in a 2017 scientific review on dietary phytoestrogens:10
|
| Phytates, which block your body’s uptake of minerals — Phytic acid binds to metal ions, preventing the absorption of certain minerals, including calcium, magnesium, iron and zinc11 — all of which are co-factors for optimal biochemistry in your body.
This is particularly problematic for vegetarians, because eating meat reduces the mineral-blocking effects of these phytates. Sometimes phytic acid can be beneficial, especially in postmenopausal women and adult men, both of whom are prone to excessive iron, a potent oxidant capable of causing significant biological stress. However, phytic acid does not selectively inhibit iron absorption; it inhibits all minerals. This is very important to remember, as many already suffer from mineral deficiencies from inadequate diets. The soybean has one of the highest phytate levels of any grain or legume, and the phytates in soy are highly resistant to normal phytate-reducing techniques such as long, slow cooking. Only a long period of fermentation will significantly reduce the phytate content of soybeans. |
| Enzyme inhibitors, which hinder protein digestion. |
| Hemagglutinins,12 which cause red blood cells to clump together and inhibit oxygen takeup and growth.13 |
| Omega-6 fat (linolenic acid), which is pro-inflammatory — The massive overconsumption of highly refined vegetable oils such as soybean oil is largely due to the wrongful demonization of saturated fats. This has had the effect of turning the average American’s omega-3 to omega-6 ratio upside down, which is a major driver of chronic inflammation, which in turn is an underlying factor in virtually all chronic diseases. |
| “Antinutrients” such as saponins, soyatoxin, lectins and oxalates — While a small amount of antinutrients would not likely cause a problem, the amount of soy and soybean oil that many Americans are now eating is very high. |
| Goitrogens — Goitrogens,14 found in all unfermented soy whether it’s organic or not, are substances that block the synthesis of thyroid hormones and interfere with iodine metabolism, thereby interfering with your thyroid function. |
Another Major Hazard of GE Soybeans: Glyphosate
If you need yet another reason to reconsider your consumption of soybean oil, consider this: In addition to having an unhealthier nutritional profile than organic soybeans, Roundup Ready GE soy has been shown to contain high amounts of glyphosate.15
According to a 2014 study16,17 published in Food Chemistry, which looked at the compositional differences between various types of soybeans, glyphosate readily accumulates in Roundup Ready soybeans, and GE soybeans contained a mean glyphosate residue level of 3.3 milligrams per kilo. The most contaminated samples contained as much as 8.8 mg of glyphosate per kilo.
Meanwhile, a 2010 study18 in the journal Chemical Research in Toxicology found malformations in frog and chicken embryos occurred at 2.03 mg of glyphosate per kilo. The malformations primarily affected the face, skull, brain and spinal cord. According to this study:
“Organic soybeans showed the healthiest nutritional profile with more sugars, such as glucose, fructose, sucrose and maltose, significantly more total protein, zinc and less fiber than both conventional and GM-soy.
Organic soybeans also contained less total saturated fat and total omega-6 fatty acids than both conventional and GM-soy. GM-soy contained high residues of glyphosate and AMPA … Conventional and organic soybean batches contained none of these agrochemicals.
Using 35 different nutritional and elemental variables to characterize each soy sample, we were able to discriminate GM, conventional and organic soybeans without exception, demonstrating ”substantial non-equivalence” in compositional characteristics for ‘ready-to-market’ soybeans.”
It’s important to realize that once applied to crops, glyphosate actually becomes integrated into the cells of the plant, so it cannot be washed off. And, while the chemical industry is still defending the safety of glyphosate, mounting research suggests it can harm health in a number of different ways.
Importantly, the chemical has been shown to decimate beneficial gut bacteria. Glyphosate has also been shown to cause DNA damage19 and to act as an endocrine disruptor.20 For an overview of how glyphosate’s impact affects your health, see “Roundup May Be Most Important Factor in Development of Chronic Disease.”
Safeguard Your Health by Ditching Vegetable Oils
To recap, there are several potential health hazards of soybean oil to consider, either alone or in combination:
- The harmful health effects of unfermented soy
- The potential hazards of GE soy
- The harm associated with glyphosate contaminated food
- High amounts of processed omega-6 skewing your omega-3 to omega-6 ratio
If you want to avoid dangerous fats of all kinds, your best bet is to eliminate processed foods from your diet. My comprehensive nutrition plan offers helpful guidance for this process.
When cooking, coconut oil, butter, lard and ghee are healthy options. Also be sure to swap out margarines and vegetable oil spreads for organic butter, preferably made from raw grass fed milk. Butter is a healthy whole food that has received an unwarranted bad rap.
Other healthy fats to include in your diet are avocados, raw dairy products, olive oil, olives, organic pastured eggs and raw nuts. To further balance your omega-3 to omega-6 ratio you may also need a high-quality source of animal-based omega-3 fat, such as krill oil, if you’re not in the habit of eating small, fatty fish such as sardines, anchovies and mackerel, and/or wild caught Alaskan salmon.
- 1 Economic Research Service, Recent Trends in GE Adoption
- 2 Endocrinology January 8, 2020 DOI: 10.1210/endocr/bqz044
- 3 UC Riverside News January 17, 2020
- 4, 6 Neuroscience News January 17, 2020
- 5 manoramaonline.com January 18, 2020
- 7 Endocrineweb.com, Overview of the Hypothalamus
- 8 Amazon
- 9, 10 British Journal of Pharmacology June 2017; 174(11): 1263-1280
- 11 American Journal of Food Technology 2011; 6(3): 235-243
- 12 The Journal of Biological Chemistry 1965; 241(3): 684-689 (PDF)
- 13 Science Direct Hemagglutinins
- 14 Baillieres Clin Endocrinol Metab. 1988 Aug;2(3):683-702
- 15 Food Chemistry June 15, 2014; 153: 207-215
- 16 Food Chemistry 2014: 153; 207-215
- 17 Foodexposed.co.za January 23, 2014
- 18 Chemical Research in Toxicology 2010; 23(10):1586–1595
- 19 Archives of Toxicology 2012; 86: 805-813 (PDF)
- 20 Toxicology 2009; 262: 184-191 (PDF)
Quercetin’s Effect on Blood Pressure
Reproduced from original article:
https://articles.mercola.com/sites/articles/archive/2022/10/17/quercetins-effect-on-blood-pressure.aspx
The original Mercola article may not remain on the original site, but I will endeavor to keep it on this site as long as I deem it to be appropriate, and will not be bullied into removing it.
Analysis by Dr. Joseph Mercola Fact Checked October 17, 2022
STORY AT-A-GLANCE
- A Japanese study identified one mechanism behind the blood pressure-lowering actions of quercetin. It is related to the action of negative chloride ions in the cell’s cytosol, influencing volume-dependent high blood pressure
- Quercetin is often combined with vitamin C or bromelain, a proteolytic enzyme found in pineapple stems. The combination increases the absorption and bioavailability of the supplement
- Quercetin is known to combat inflammation and support your immune system. It has strong antiviral properties and likely is a far safer alternative to antiviral drugs like Tamiflu, which shortens flu by only hours and has significant side effects such as convulsions, hallucinations and memory deterioration
- Other lesser-known health benefits of quercetin include the prevention or treatment of metabolic syndrome, nonalcoholic fatty liver disease (NAFLD), gout, mood disorders and against aluminum-induced neurodegenerative changes
Quercetin is a flavonol found in red grapes, onions, red leaf lettuce, elderflower and green tea, to name a few.1 Research has demonstrated the positive effect it has on blood pressure. A Japanese study2 identified one mechanism behind the blood pressure lowering actions, which is related to the action of negative chloride ions in the cell’s cytosol.
Flavonols, like quercetin, are antioxidants,3 which scavenge free radicals, helping to prevent DNA damage and cell death. In the past two years, the antiviral benefits of quercetin have been the focus of many studies.4 However, there are also many other lesser-known benefits, making it useful for a variety of different health conditions.
In many instances, quercetin is sold in combination with bromelain or vitamin C.5 Quercetin is not water-soluble which reduces the absorption rate. However, when administered with vitamin C or bromelain, absorption and bioavailability increase.
Bromelain6 is a proteolytic enzyme found in the stem of the pineapple plant, which has been used independently to reduce swelling after surgery or injury and has been used topically to help treat burns.
Quercetin can reduce the effectiveness of some antibiotics7 and enhance the effect of blood thinners. This can increase the risk of bleeding. It may also interact with corticosteroids, cyclosporine, digoxin and fluoroquinolones.
Quercetin Influences Volume-Dependent Blood Pressure
According to the Department of Health and Human Services,8 nearly 1 out of every 2 adults have high blood pressure in the U.S., and most are recommended prescription medication with lifestyle changes. High blood pressure increases the risk for stroke and heart attack, which are two of the leading causes of death in the U.S.
The featured study9 evaluated the blood pressure-lowering actions of quercetin on the body. According to the researchers, there are many factors that help to regulate blood pressure, including the nervous system, cardiac output, total blood volume and the renin-angiotensin system.
The researchers noted several past studies that demonstrated taking between 150 mg per day and 730 mg per day could lower high blood pressure, decreasing systolic and diastolic pressures.
The scientists wrote quercetin’s antihypertensive actions operated through a modification of a variety of factors, including vascular compliance and resistance, total blood volume and the autonomic nervous system. In addition to these global actions, quercetin appears to have a unique ability to regulate gene expression that is mediated by controlling negative chloride actions in the cell’s cytosol.
Negative chloride ions help control the intracellular activity of many other ions10 in the cytosol, which is the water-based fluid that surrounds intracellular structures. The gene expression that controls the chloride ions triggers sodium reabsorption, which then reduces body fluid volume and therefore influences volume-mediated high blood pressure.
Quercetin Combats Inflammation and Supports Immunity
A 2016 study11 in the journal Nutrients detailed quercetin’s properties for combating inflammation and supporting immunity. The mechanisms of action were many and included, but we’re not limited to, inhibiting:
- Lipopolysaccharide (LPS)-induced tumor necrosis factor α (TNF-α) production in macrophages. TNF-α is a cytokine involved in systemic inflammation, secreted by activated macrophages, a type of immune cell that digests foreign substances, microbes and other harmful or damaged components
- LPS-induced mRNA levels of TNF-α and interleukin (IL)-1α in glial cells, resulting in “diminished apoptotic neuronal cell death”
- The production of inflammation-producing enzymes
- Calcium influx into the cell, which in turn inhibits:
- Proinflammatory cytokine release
- Histamine and serotonin release from intestinal mast cells release
According to the researchers, quercetin stabilizes mast cells, has cytoprotective activity in the gastrointestinal tract and “a direct regulatory effect on basic functional properties of immune cells,” which allows it to inhibit “a huge panoply of molecular targets in the micromolar concentration range, either by down-regulating or suppressing many inflammatory pathways and functions.”12
In a 2016 paper13 published in the journal Molecules, the researchers wrote that the anti-inflammatory and immunomodulating properties can be used in the treatment of restricted peanut-induced anaphylactic reactions, allergic rhinitis and bronchial asthma response. They concluded:
“Plant extract of quercetin is the main ingredient of many potential anti-allergic drugs, supplements and enriched products, which is more competent in inhibiting of IL-8 than cromolyn (anti-allergic drug disodium cromoglycate) and suppresses IL-6 and cytosolic calcium level increase.”
Quercetin Is a Far Safer Alternative to Antiviral Drugs
In the past two years, research into quercetin’s antiviral properties has risen dramatically. In fact, this is one of the most well-studied attributes of quercetin. One study14 funded by the U.S. Defense Advanced Research Projects Agency (DARPA) used an animal model demonstrating subjects treated with quercetin had lower morbidity and mortality after being challenged with the highly pathogenic H1N1 influenza virus.
Multiple other studies have also demonstrated quercetin’s effectiveness against a variety of viruses including influenza A and B,15 and a wide variety of influenza viruses, including H1N1, H3N2 and H5N1.16
Combining quercetin with bromelain or vitamin C has been a component of several successful COVID-19 protocols. Quercetin is a zinc ionophore,17 which helps improve the cell’s ability to absorb zinc where it is effective as an antiviral. Dr. Vladimir Zelenko was among the first doctors to discover and implement a treatment utilizing zinc and an ionophore that has been credited with saving millions of lives around the world.18
The early protocol used hydroxychloroquine,19 which is another zinc ionophore. However, as research showed quercetin was as effective as hydroxychloroquine, early treatment protocols for low-risk patients included quercetin with vitamin C and zinc.20
Considering the powerful antiviral effects of quercetin, it is sensible to use it before resorting to antiviral drugs like Tamiflu. Not only has Tamiflu been shown to shorten the duration of flu symptoms by only hours,21 scientists have also warned that the risks of Tamiflu far outweigh the benefits.22
Lesser-Known Health Benefits From Quercetin Supplements
In addition to lowering blood pressure, there are also other, less known benefits and uses for this supplement, including the prevention and/or treatment of:23,24
| Cardiovascular disease | Asthma | Allergic reactions |
| Metabolic syndrome | Diabetes | Certain kinds of cancer |
| Neurodegenerative disease | Nonalcoholic fatty liver disease (NAFLD) | High Blood Pressure through vasodilation |
| Age-Related disorders | Arthritis | Learning and emotional function |
Additionally, quercetin is also helpful for aluminum-induced neurodegenerative changes, such as those seen in Alzheimer’s, Parkinson’s and amyotrophic lateral sclerosis (ALS). As noted in a 2016 study:25
“Administration of quercetin (10 mg/kg body wt/day) reduced aluminum (10 mg/kg body wt/day)-induced oxidative stress (decreased ROS production, increased mitochondrial superoxide dismutase (MnSOD) activity).
In addition, quercetin also prevents aluminum-induced translocation of cyt-c, and up-regulates Bcl-2, down-regulates Bax, p53, caspase-3 activation and reduces DNA fragmentation …
Further electron microscopic studies revealed that quercetin attenuates aluminum-induced mitochondrial swelling, loss of cristae and chromatin condensation. These results indicate that treatment with quercetin may represent a therapeutic strategy to attenuate the neuronal death against aluminum-induced neurodegeneration.”
More Natural Ways to Lower High Blood Pressure
Quercetin is just one option to help you naturally lower high blood pressure. Other strategies include stress management and exercise along with the following:
• Potassium/Sodium balance — People who eat a lot of processed foods and very few fresh vegetables likely have an imbalance in their sodium-potassium ratio. The key to relaxing your arterial walls and reducing blood pressure is the ratio between sodium and potassium. If you’re unsure of your sodium and potassium intake, use chronometer.com/mercola, which is a nutrient tracker that allows you to enter foods and then calculates the ratios automatically.
Generally, it’s recommended that you eat five times more potassium than sodium, but most Americans eat twice as much sodium as potassium. The American Heart Association26 recommends a low-salt diet, but the ratio between potassium and sodium is far more important than your overall salt intake.27
It’s also a better strategy to promote public health and focus on a high-quality diet rich in potassium, as it is a nutrient that helps offset the hypertensive effects of sodium.
• Aged Black Garlic — According to research data, eating aged black garlic has demonstrated improvement in different cardiovascular disease risk factors, including helping to lower diastolic blood pressure.
The objective of one study28 was to analyze how daily consumption of aged black garlic extract with standardized s-allyl-L-cysteine (SAC) could impact cardiovascular risk in people who had moderate hypercholesterolemia and who also followed dietary recommendations.
At the end of the study, the researchers found that those taking the aged black garlic extract had a reduction in systolic blood pressure of 5.85 mmHg as compared to those who took the placebo. According to Medscape,29 the researchers concluded from the data that lowering diastolic blood pressure by 5 mmHg could lower the risk of death from stroke by 40%, and the risk of ischemic heart disease or other vascular death by 30%.
• Inspiratory Muscle Strength Training — Another study30 evaluated the effect that inspiratory muscle strength training (IMST) could have on reducing blood pressure and thus reducing the risk of cardiovascular disease. While aerobic exercises are a foundational strategy for controlling high blood pressure, fewer than 40% meet the current recommended guidelines.31
IMST was originally developed for critically ill patients with respiratory diseases. It helped to improve the strength of their inspiratory muscles by using a handheld device that provides resistance while inhaling.
The study engaged 36 adults ages 50 to 79 who had above normal systolic blood pressure, half the participants used high resistance IMST and half use low resistance IMST for 6 weeks. At the end of the intervention, the group using high resistance had a nine-point reduction in their systolic blood pressure.
– Sources and References
- 1 Superfoodly, 100 Quercetin Foods
- 2, 9 Molecules, 2017;22(2)
- 3 Mount Sinai, Quercetin
- 4 Research International Journal of Endocrinology and Diabetes, 2020; 1(1)
- 5 Sciencedirect, Quercetin
- 6 National Center for Complementary and Integrative Health, Bromelain
- 7 Mount Sinai, Quercetin, 45% DTP Precautions
- 8 Million Hearts, Estimated Hypertension Prevalence, Treatment, and Control Among U.S. Adults, key findings bullet one
- 10 PNAS, 2015;112(3)
- 11 Nutrients 2016 Mar; 8(3): 167, 5.2.1 Animal Models
- 12 Nutrients 2016 Mar; 8(3): 167, 5.1.2 Mechanism of Action
- 13 Molecules, 2016;21(5)
- 14 American Journal of Physiology August 1, 2008
- 15 Antiviral Research 2010 Nov;88(2):227-35
- 16 Viruses 2016 Jan; 8(1): 6
- 17 Frontiers in Immunology, 2020; doi.org/10.3389/fimmu.2020.01712
- 18 America’s Frontline News, July 1, 2022
- 19 YouTube, May 14, 2020
- 20 Vladamir Zelenko, COVID-19 Treatment Protocol
- 21 Forbes April 10, 2014
- 22 Cochrane Database of Systematic Reviews 2014, Issue 4. Art. No.: CD008965
- 23 Defence Life Science Journal 2017;2(2)
- 24 Molecules, 2022; 27(8)
- 25 Neuroscience 2016;324:163
- 26 American Heart Association
- 27 Healthy Food. The Sodium-Potassium Balancing Act
- 28 Nutrients, 2022; 14(3)
- 29 Medscape, April 15, 2022, page 2 PARA 8
- 30 Journal of the American Heart Association, 2021;10:e020980
- 31 News Wise, June 30, 2021