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We are indeed much more than what we eat, but what we eat can nevertheless help us to be much more than what we are.
–Adelle Davis
he current cultural trend towards a more natural way of eating could turn out to have great benefits for public health. But despite the rampant promotion of natural products and foods today, the very real issue of defending against natural food–based toxins is rarely addressed. Ironically, by selectively distorting the historical and biological significance of foods and food–based substances, the profit–at–all–costs mentality of the emerging "natural" industry could just as easily turn out to make public health worse in the years to come, as incessant marketing often muddles our perception of the type of nutrition for which our bodies were designed.
Consider, for example, the fact that many of the most potent food–based toxins yet identified have been isolated, and are currently being offered to the public at large in the form of "nutritional supplements." Plant hormones from soy, flax, and most recently, various vine species (i.e., resveratrol); digestion–inhibiting bean extracts; and the allergenic and metabolically–disruptive wheat gluten (often seen in protein supplements under the inappropriate designation of "glutamine–peptides") are all being aggressively marketed as health–promoting substances. In reality, however, the existing scientific literature provides many reasons to avoid consuming such substances in artificially high "supplemental" amounts. This sort of nutritional perversion is clear evidence that a rational and holistic perspective of food–based toxins is desperately needed.
Mother Nature has endowed plant species with numerous substances designed to protect the plant and its offspring from the harsh environment; and from destruction by way of pathogenic microbes and foraging animals. Even our highly evolved, and relatively resilient, human bodies may suffer damage from some of these same substances when consumed in excess or over long periods of time. This fact is of pressing significance considering that these subtly toxic substances can be found in the plants which comprise the majority of human food - most notably, dietary staples such as wheat, rice, corn, beans, nuts, and legumes.
Some such food–based chemicals of plant defense are increasingly being implicated as contributing factors in the modern degenerative diseases of Western culture. As we discussed in the previous edition of the Integrated Supplements Newsletter, certain carbohydrate–binding proteins, called lectins, are prime examples.
Culling from thousands of years of empirical observation (known colloquially as trial and error), traditional cultures often employed diets and methods of food preparation which largely inactivated problematic plant–defense chemicals. At the same time, traditional methods of food preparation also supported the body's defenses against food–based toxins by supporting the integrity of the gastrointestinal barrier.
But, when viewed in relation to harmful food–based elements, the foods produced in just the last 50 years exhibit a striking divergence when compared to the foods consumed throughout the rest of human history. Our intake of certain food–based toxins (like the lectins in wheat, for example) is likely to be much higher today than in most traditional cultures. And it's additionally problematic that the traditional "defenses" against these toxins have become almost non–existent in our modern diet - both through changes in the foods we eat and through changes in how foods are prepared.
In the previous Integrated Supplements Newsletter, we took a look at what modern science has to say about the role of food–based lectins in disease. Our task, now then, becomes to design a plan of proper diet and rational supplementation to build our bodies' defenses against them in our modern age.
Reducing Lectin–Induced Damage
The damage lectins are able to inflict has much to do with the types of cellular sugars to which they bind. Because the food we eat comes, more or less, in direct contact with our intestines, the chain reaction of lectin–induced damage often begins when lectins attach to the glycoconjugates (protein–sugar molecules) of the gastrointestinal tract. We have seen that food–based lectins can exert a great amount of damage by:
Adhering to glycoconjugates in the intestine.
Altering the bacterial/microbial population of the intestines towards one that fosters disease.
Increasing gastrointestinal permeability.
Imparing the healing of this gastrointestinal damage.
Allowing intestinal bacteria and other microbes to enter the bloodstream, thus taxing the liver, stimulating inflammation, and compromising immune function.
Interestingly, much of what makes certain viruses and bacteria harmful is their ability to adhere to, enter, and disrupt cells by way of lectins on their surface. Like food–based lectins, microbial lectins "seek out" and bind to sugar–containing molecules on cell surfaces. For this reason, it's likely that many food–based anti–microbials may offer benefits in combating food–based lectins as well.
In fact, the structural similarities between dietary lectins, and the lectins of viruses and bacteria present to us several approaches to maximize our defenses against both, including:
Binding lectins with specific foods
Supporting the healthy structure of the intestines and the protective gastrointestinal mucosa
Similarly, binding and/or inactivating harmful microbes to impair their binding with the gastrointestinal tract or other cells.
Cellular Sugars
The biologically active sugars most people recognize are usually those which the body can metabolize as fuel sources - sugars like glucose, fructose, sucrose, and lactose. But many other sugars happen to play important roles, not as sources of energy, but as integral elements of cellular structure. The following sugars are components of the glycoconjugates which emanate from the surfaces of cells, and are important for proper cellular communication and immune function:
Fucose
Galactose
Glucose
Mannose
N–acetylgalactosamine (GalNAc)
N–acetylglucosamine (GlcNAc)
N–acetylneuraminic acid (Neu5Ac, Neu5Gc), forms of sialic acid
Xylose
We know that these are the cellular sugars to which lectins (from food, viruses, and bacteria) bind, so it's conceivable that food sources of these sugars could act as nutritional "decoys" allowing lectins to bind to the sugars contained in these foods instead of the same sugars in our cells.
Perhaps the best known example of inhibiting lectin adhesion via dietary means comes from the well–known practice of drinking cranberry juice to prevent or treat urinary tract infections. Lectins on the E. coli bacteria responsible for urinary tract infections happen to bind strongly with the sugar, mannose - which is found in high concentrations in cranberries and cranberry juice. When humans eat mannose, it's not converted to glycogen (a storage form of sugar used by working cells) - so, much of it is quickly filtered by the kidneys and is delivered to the bladder for excretion in the urine. As mannose is excreted, the E. coli bacteria bind to it preferentially, instead of the cellular sugars on the cells of the urinary tract - thus causing the bacteria to be excreted along with the ingested mannose.
Study Link – Reduction of Escherichia coli adherence to uroepithelial bladder cells after consumption of cranberry juice: a double–blind randomized placebo–controlled cross–over trial.
Quote from the above study:
Cranberry juice consumption provides significant anti–adherence activity against different E. coli uropathogenic strains in the urine compared with placebo.
Of interest is the observation that cranberry juice often rectifies existing urinary tract infections. This fact seems to provide evidence that lectins bound to human cells may continue to do so only "until something better comes along" i.e., until they encounter sugar–containing molecules to which they can bond more tightly. If dietary lectins do bind to cellular structures long–term (such as the cells of the gastrointestinal tract, or the insulin receptor as we saw in the previous Integrated Supplements Newsletter), this may help to explain the difficulty often encountered in treating disorders which have a large dietary component – like obesity and numerous digestive disorders. These disorders often stubbornly persist even after the diet has been altered, but with what we know about lectins, it may be possible to develop effective treatments for such disorders, in part, by providing concentrated sources of specific sugars and saccharides (chains of sugar molecules).
Certain sugars and glycoproteins (protein–sugar molecules) found in the diet may impart protective benefits by binding lectins directly. They may also act simply as the building blocks needed to heal damaged tissue. The gastrointestinal epithelium (surface) is covered by a protective gel of mucus comprised largely of glycoprotein–containing structures called mucins. Because this protective gastrointestinal mucosa is made up of the same cellular sugars to which lectins from food, viruses, and bacteria can bind, lectins are likely to initiate their metabolic disruption via contact with the gastrointestinal mucosa. As we've seen, food–based lectins and intestinal microbes synergize to create a potent one–two punch against the integrity of the delicate gastrointestinal mucosa and, ultimately, the epithelium underneath. For this reason, ensuring the integrity of the protective gastrointestinal mucosa is of the utmost importance in protecting against harmful lectins.
Licorice and Peptic Ulcer
Take, for example, the disorder of peptic ulcer disease. Peptic ulcers are painful erosions in the lining of the stomach, or the upper part of the small intestine (i.e., the duodenum). Ideally, the mucins of the stomach and small intestine should be resilient enough to maintain the gastric mucosa, even in the presence of highly acidic digestive secretions. Obviously, however, when ulcers develop, something has gone awry in the body's ability to maintain this barrier of protection. In years past it was often assumed that ulcers were caused by things like stress or spicy foods, but more recently, scientists have shied away from this line of thinking and have implicated infection with the H. pylori bacteria as the causative factor in the vast majority of cases of peptic ulcer disease.
But deeming H. plyori to be the cause of peptic ulcer only serves to raise other pressing questions. Like, why, for example, do the vast majority of people infected with H. pylori not develop peptic ulcers? It's been estimated that 20% of the U.S. population under the age of 40, and a full 50% of the people over age 60, are infected with H. pylori - yet only 10% of Americans will ever experience a peptic ulcer.
So, clearly there are other factors involved in the development of peptic ulcer besides the mere presence of H. pylori. The question naturally arises, then: what additional factors cause H. Pylori to initiate ulcerations in some people, but not in others?
Dietary lectins have been proposed as a contributing factor. Damaged tissue is well–known to be a breeding ground for pathogenic bacteria, and, as we saw in the previous Integrated Supplements Newsletter, dietary lectins are able to damage the gastrointestinal mucosa and alter the bacterial balance of the gastrointestinal tract towards increased levels of pathogenic organisms. It's also been noted that certain lectins can cause a discharge of histamine from gastric mast cells, which stimulates gastric acid secretion (the over–secretion of gastric acid is known to exacerbate the symptoms and hinder the healing of peptic ulcers - for this reason, antacids are commonly employed as first lines of peptic ulcer treatment). Collectively, these effects of lectins create the ideal environment for the development of peptic ulcers:
Editorial Link – Do dietary lectins cause disease? The evidence is suggestive – and raises interesting possibilities for treatment.
Quote from the above editorial:
Among the effects observed in the small intestine of lectin fed rodents is stripping away of the mucous coat to expose naked mucosa and overgrowth of the mucosa by abnormal bacteria and protozoa. Lectins also cause discharge of histamine from gastric mast cells, which stimulates acid secretion. So the three main pathogenic factors for peptic ulcer - acid stimulation, failure of the mucous defense layer, and abnormal bacterial proliferation (Helicobacter pylori) are all theoretically linked to lectins. If true, blocking these effects by oligosaccharides [chains of sugars] would represent an attractive and more physiological treatment for peptic ulcer than suppressing stomach acid.
In keeping with this assessment, it's interesting to find that traditional herbal remedies for peptic ulcers often contain saccharides which support the gastrointestinal mucosa and inhibit the binding of H. pylori. Licorice root is one such example:
Study Link – Aqueous extracts and polysaccharides from Liquorice roots (Glycyrrhiza glabra L.) inhibit adhesion of Helicobacter pylori to human gastric mucosa.
Quote from the above study:
Aqueous extracts and polysaccharides from the roots of Glycyrrhiza glabra are strong antiadhesive systems, which may be used as potent tools for a further development of cytoprotective preparations with anti–infectious potential.
De–glycyrrhizinated licorice (DGL) has been shown in many (but not all) studies to be helpful in peptic ulcer disease - and to reduce the intestinal damage caused by NSAID drugs such as aspirin. But some studies on licorice showed no such effect. These conflicting results may actually provide further evidence that licorice exerts its protective effects by directly binding the lectins of H. pylori and/or healing the gastrointestinal mucosa. Studies using chewable licorice tablets - which deliver the active saccharides directly to the stomach and upper gastrointestinal tract - have been found to be significantly more effective than the same licorice delivered in capsules - which is more likely to be released further down the gastrointestinal tract:
Study Link – Comparison between cimetidine and Caved–S [containing licorice] in the treatment of gastric ulceration, and subsequent maintenance therapy.
Quote from the above study:
To achieve gastric ulcer healing the liquorice must be partly released within the stomach and absorbed through the gastric mucosa. The liquorice in Ulcedal [the encapsulated licorice used in other studies] would appear to be released and presumably absorbed lower down in the gastrointestinal tract. Deglycyrrhizinated liquorice has been shown in animals to protect the gastric mucosa from the damaging effect of both aspirin and bile.
Many plants in addition to licorice produce polysaccharide gels, called mucilage - each with unique saccharide compositions. Okra, a common ingredient in Southern cooking (e.g., gumbo) produces mucilage containing abundant galactose polysaccharides. Galactose is a component of the human intestinal mucosa, and certain E. coli bacteria and various plant lectins initiate their damage by binding to galactose in the mucosa and on cell structures. Okra mucilage is likely able to reduce such damage:
Study Link – Characterization of the okra mucilage by interaction with Gal, GalNAc and GlcNAc specific lectins.
Quote from the above study:
...this polysaccharide contains the Gal alpha 1––>4Gal sequence, which is the ligand for the uropathogenic Escherichia coli and toxic lectins... The results obtained suggest that this polysaccharide is a valuable reagent to differentiate Gal specific lectins from the GalNAc and/or GlcNAc specific series.
Other plants which produce mucilage often happen to be traditional folk remedies used to soothe the gastrointestinal tract. Aloe vera gel is well–known for its unique polysaccharides, as are herbs such as slippery elm and marshmallow.
N–Acetyl Glucosamine
In the previous Integrated Supplements Newsletter, we cited research indicating that a lectin–fraction of the wheat protein, gluten, is responsible for triggering gastrointestinal damage in people with (and even in people without) the gluten–sensitivity disorder known as celiac disease. Both mannan (i.e., chains of the aforementioned sugar, mannose) and the amino–sugar, N–acetylglucosamine (GlcNAc) have been shown to protect the intestinal mucosa from wheat–based lectins.
Study Link – Mannan and oligomers of N–acetylglucosamine protect intestinal mucosa of celiac patients with active disease from in vitro toxicity of gliadin peptides.
Quote from the above study:
Mannan, acetylglucosamine, and its oligomers (N,N'–diacetylchitobiose and N,N',N"–triacetylchitotriose) were able to prevent and reverse cell agglutination induced by peptides from all the toxic cereals. Moreover, mannan and N,N',N"–triacetylchitotriose exhibited a protective effect on intestinal mucosa specimens of patients with active celiac disease cultured with wheat protein–derived peptides. These data are consistent with the hypothesis that the agglutinating and toxic peptides are bound by carbohydrates.
Preliminary research in children with inflammatory bowel disease (IBD - including Crohn's disease and ulcerative colitis) has shown promising results when N–acetyl glucosamine was administered:
Study Link – A pilot study of N–acetyl glucosamine, a nutritional substrate for glycosaminoglycan synthesis, in paediatric chronic inflammatory bowel disease.
Quote from the above study:
GlcNAc shows promise as an inexpensive and nontoxic treatment in chronic inflammatory bowel disease, with a mode of action which is distinct from conventional treatments. It may have the potential to be helpful in stricturing disease.
Autism is a disorder which is commonly associated with gluten intolerance and subsequent gastrointestinal disturbances like diarrhea. Preliminary research in autistic children has shown glucosamine to relieve diarrhea in the majority of children studied - possibly due to its ability to bind the problematic lectins from wheat gluten:
Study Link – Glucosamine and Plant Lectins in Autistic Spectrum Disorders: An Initial Report on Six Children with Uncontrolled Diarrhoea.
Quote from the above study:
Gluten contains a plant lectin that binds glucosamine. Glucosamine binds to potato lectin in the same manner and may protect the gut in responsive children. This is reflected in a change in bowel habit, indicating a possible protective activity.
N–acetyl Glucosamine (not to be confused with the more common, but structurally different, glucosamine sulfate) is available as a dietary supplement. Some research even suggests that N–acetyl Glucosamine may be able to combat certain autoimmune diseases, which, as we have seen, have been linked with lectins in the diet. Where the effects of long–term supplementation with N–acetyl Glucosamine have yet to be studied, its use may be best suited for short–term situations where significant gastrointestinal disturbance is a concern - like times of infection or extreme stress.
Luckily, many other substances which may protect against lectins are found in traditional foods (or in nutritional supplements which deliver some of the benefits of the traditional foods not commonly available to us today).
Whey Protein and Glycomacropeptide
A properly–prepared undenatured whey protein will contain numerous substances which seem tailor–made to support gastrointestinal health - and it's likely that much of the protection whey protein offers stems, directly or indirectly, from its ability to combat bacterial and food–based lectins.
Unbeknownst to most people, several whey fractions contain unique saccharides - including a group of monosaccharides collectively called sialic acid (aka N–acetylneuraminic acid). Sialic acid serves as a "cap," so to speak, on the mucins which make up the gastrointestinal mucosa. In a sense, it's a chemical which signals that the building process of a particular mucin is complete. In this role, sialic acid helps to protect the more delicate saccharide structures in the mucosa, and the gastrointestinal epithelium itself, from damage.
Many intestinal viruses and bacteria, however, contain sialidases (aka neuraminidases) which are enzymes specifically suited to cleaving sialic acid from mucins. The virus can then gain access to the mucin saccharides, epithelium, and ultimately, our bodies. We saw in the previous Integrated Supplements newsletter, that the influenza virus does just this, and because sialidase exposes the gastrointestinal saccharides - making us particularly susceptible to the harmful effects of food–based lectins - there may be justification for the folk–wisdom of "starving a fever" when infected with influenza.
But, a particular protein fraction found in some whey protein supplements, called glycomacropeptide (GMP), may be able to offer significant protection against food and microbial lectins. GMP contains sialic acid, and has been shown to prevent intestinal infection by inhibiting both bacterial and viral adhesion:
Study Link – Prevention of intestinal infection by glycomacropeptide.
Quote from the above study:
GMP showed the ability to bind to Salmonella enteritidis and enterohemorrhagic Escherichia coli O157:H7 (EHEC O157). This binding ability was decreased by a sialidase treatment and completely eliminated by periodate oxidation...Our results indicate GMP to be a promising agent for preventing intestinal infection.
Study Link – Inhibition by kappa–casein glycomacropeptide and lactoferrin of influenza virus hemagglutination.
In experimental studies, certain chemicals are often administered to mimic the development of human disease. The hapten–chemical, trinitrobenzenesulfonic acid (TNBS), for example, is administered to rats to induce inflammatory intestinal lesions similar to those of human colitis.
Although much more potent, TNBS acts to disrupt the mucosal barrier of the intestines in a fashion similar to that of some dietary lectins. When tested in this model of colitis, glycomacropeptide was found to be equally as protective as the colitis drug, sulfasalazine - but unlike the pharmaceutical treatment, glycomacropeptide was also able to reduce the weight loss associated with the disease:
Study Link – Bovine Glycomacropeptide Is Anti–Inflammatory in Rats with Hapten–Induced Colitis.
Quote from the above study:
Our results demonstrate that GMP gavage results in significant protection from inflammatory damage in TNBS–induced colitic rats. Thus GMP reduced the colonic damage score, weight:length ratio, and extent of necrosis, and increased AP colonic activity and iNOS expression. Furthermore, these effects did not differ from those obtained with sulfasalazine, an established drug treatment for IBD...Unlike sulfasalazine, GMP had a significant effect on anorexia and weight loss.
Also relating to gastrointestinal health, glycomacropeptide may exhibit a "prebiotic" effect, as it has been shown to selectively enhance the growth of protective Bifidobacteria species of intestinal bacteria:
Study Link – Growth–promoting Effects of N–Acetylneuraminic Acid–containing Substances on Bifidobacteria.
Quote from the above study:
This study demonstrated the growth–promoting effects of NeuAc–containing substances on B. breve, B. bifidum, and B. infantis.
As an interesting and related aside, glycomacropeptide may even be able to improve dental health. Sialic acid derives its name from its original discovery as a component of saliva. Certain bacteria (e.g., Streptococcus mutans) are known to initiate the development of dental caries (cavities), and it's thought that the sialic acid in saliva is a necessary factor in preventing the adherence of these acid–producing bacteria to the tooth surface. A great number of studies have shown various dairy products to possess anti–cavity activity, and some evidence suggests that glycomacropeptide may be particularly beneficial in this regard. It's likely that the sialic acid it contains may inhibit the binding of oral bacteria to the tooth surface, preventing cavities, and possibly even allowing for the remineralization of tooth enamel:
Study Link – Incorporation of caseinoglycomacropeptide and caseinophosphopeptide into the salivary pellicle inhibits adherence of mutans streptococci.
Quote from the above study:
The protective effects of milk and milk products against dental caries have been demonstrated in many animal studies. We have shown that this effect was mediated by micellar casein or caseinopeptide [glycomacropeptide] derivatives. A reduction in the Streptococcus sobrinus population in the oral microbiota of animals fed diets supplemented with these milk components was consistently observed.
Taken together, these studies provide evidence that glycomacropeptide may support the integrity of the mucosal lining and provide significant protection against bacterial and viral infections by way of the lectin–binding activity of its sialic acid–containing structures. Properly prepared whey protein, then, is likely to be a unique tool in our defense against all manner of harmful lectins. When it comes to glycomacropeptide, however, all whey proteins are not created equal. Great care must be taken in production methods to ensure the presence and biological activity of glycomacropeptide in whey protein.
Processing (both industrial processing and simple cooking) often alters the native protein structures of food via a general process known as denaturation. Oftentimes, this denaturation can be benign, as our digestive enzymes will break down protein structures similarly after the food is digested. Other times, certain types of "processing" may even be beneficial, as is the case when processing breaks down protein–based antinutrients - the cooking of egg whites, for example, denatures and inactivates a protein which blocks the absorption of biotin. We can even see evidence of the denaturation of proteins as the egg white turns from translucent to opaque as it's cooked.
But there are many times when processing serves to denature or alter protein structures in a decidedly negative way. As we have repeatedly seen, the remarkable health–promoting benefits of whey protein are dependent upon intact protein structures found uniquely in whey protein. For example, it's been found that mixtures of isolated amino acids which mimic whey protein composition do not possess the same health benefits as undenatured whey protein.
In recent years, some whey proteins have been introduced to the supplement industry in which "hydrolyzed" whey protein is used. Hydrolyzed proteins are "broken" by enzymes or chemicals, often in an attempt to reduce the allergenicity of things like infant formula. In the fitness realm, hydrolyzed protein supplements are often marketed as "fast" proteins, i.e., proteins which are absorbed into the bloodstream quickly. But hydrolyzed proteins are, by definition, highly denatured, and it's likely that much of the functional benefit of undenatured whey protein is lost when whey is hydrolyzed.
The supposed benefits of "fast–absorbing" hydrolyzed proteins are mostly products of marketing hype not supported by the majority of research on whey protein - especially considering the fact that undenatured whey protein is absorbed very quickly in its own right. Keeping in mind the remarkable benefits of many of the whey fractions we've discussed in the Integrated Supplements Newsletter (e.g., glycomacropeptide and lactoferrin) we can clearly see that the existing research indicates that whey protein should ideally be consumed in as undenatured a state as possible.
Additionally, some types of whey protein, although they contain some intact whey microfractions, will not contain glycomacropeptide. For example, because of the chemical affinity of the resins used in its production, whey protein isolate produced by what's known as the ion–exchange method will be almost completely lacking in glycomacropeptide. Ceramic filtered whey isolate, on the other hand, will contain up to 21% glycomacropeptide - a significant difference which often goes completely unrecognized by consumers of whey protein.
As an additional note regarding protein supplements, several protein–supplement producers specifically add hydrolyzed wheat gluten to their protein powders. Where wheat gluten is a protein which happens to be high in the amino acid glutamine, these companies misleadingly label the ingredient as "glutamine peptides." But unlike glutamine (which has been shown to have protective effects upon gastrointestinal integrity), "glutamine peptides" in this form are likely to do damage to the gastrointestinal tract. When studied, hydrolysates of wheat gluten were shown to possess significant allergenicity, which is evidence of intact lectins in the product:
Study Link – Profile analysis and immunoglobulin E reactivity of wheat protein hydrolysates.
Quote from the above study:
These results suggested that the uptake of wheat protein enzymatic hydrolysates might still have the possibility of causing food allergic reactions in patients allergic to wheat and the processed foods containing them.
Of course, despite the marketing hype, the real reason for the use of wheat gluten in these products is that glutamine happens to be a relatively expensive amino acid in its free form, whereas wheat gluten is remarkably inexpensive.
Gelatin
Gelatin–rich foods, like soups made with bone broth, are eaten relatively rarely today, but were staples of traditional diets in numerous cultures. Their unique healing effects often made broths and soups uniquely therapeutic foods - especially for disorders of digestion and gastrointestinal health. Though research on gelatin is sparse today, researchers from the early part of the 20th Century often reported that the proteins in wheat, oats, beans, and barley were better digested if gelatin was added to the meal. Where the plant lectins in these foods represent a type of anti–nutritional storage protein, it's possible that gelatin may help to break down lectins directly, or may help to improve digestive capacity enough so that lectins are more apt to be broken down and inactivated during the digestive process.
Gelatin also contains numerous polysaccharides which may provide unique protection to the gastrointestinal mucosa:
Study Link – The Distribution of Mucoprotein in Gelatins and Fractionated Gelatins.
Recent research by Russian scientists has found that gelatin (and some of its constituent peptides) is able to protect the gastric mucosa from ethanol–induced ulceration:
Study Link – Protection of gastric mucosal integrity by gelatin and simple proline–containing peptides.
Quote from the above study:
We have observed that gelatin as feed supplement protected against ethanol–induced mucosal damages in rats. Intraperitoneally given peptides PG and PGP had similar effects.
The intestinal epithelium and mucosa are constantly being rebuilt, and this rapid turnover is likely to proceed all the more efficiently if we introduce the unique proteins and polysaccharides from gelatin into our daily diet. Ideally, slow–cooked bone broths and soups are about the best way to accomplish this (this way is likely to also deliver other protective components of cartilage, besides just gelatin) - but in our fast–paced world, this isn't always realistic. For this reason, gelatin supplements are an excellent alternative.
Unlike whey protein, the beneficial effects of gelatin seem to persist even though the protein (when found in powdered form) is hydrolyzed. Many of the peptides in gelatin are simple and relatively small when compared to the larger and more complex proteins in whey. Numerous studies on gelatin in relation to joint health show that hydrolyzed gelatin peptides still possess unique biological activity (they are preferentially incorporated into the structure of connective tissue when ingested). Free glutamate, or MSG, production from hydrolyzed gelatin doesn't generally appear to be problematic either, as the glutamate content of gelatin is relatively low and somewhat balanced by other amino acids. Those sensitive to glutamate may want to choose gelatin with higher bloom strength - a measure of the gel strength of gelatin. The higher the bloom strength, the less hydrolyzed the gelatin will be, and the firmer it will be if allowed to gel. Higher bloom strength gelatins generally won't dissolve in cold water, but can be added to hot beverages or soups.
Seaweed
Though a relatively rare food in the United States, various forms of edible seaweeds are staples of various diets throughout the world. Asian cultures, like those of China, Korea, and Japan are known to include seaweed as a part of the diet as do cultures in many coastal regions of Europe including, Ireland, Iceland, Norway, and France.
In a general sense, seaweeds contain numerous unique sulfated polysaccharides which, for better or for worse, have been shown to possess significant biological function. We've previously discussed the harmful pro–inflammatory effects of the common food additive, carrageenan, which is derived from certain species of red seaweed. Due to its unique chemical structure, carrageenan has been found to hinder immune function either by causing the destruction of, or by interfering with the function of, immune cells called macrophages:
Study Link – A re–evaluation of the role of macrophages in carrageenan–induced immunosuppression.
Quote from the above study:
The immunosuppressive properties of carrageenan are well documented. In the present study this suppression seemed to be mainly related to responses involving T lymphocytes, dependent on the time of carrageenan administration and associated with a regulatory role of macrophages.
It's especially interesting to note that carrageenan's effects of stimulating gastric ulceration and triggering immune–system disruption mimic many of the harmful effects of lectins.
But fortunately, the toxic effects of carrageenan don't hold true for all other types of seaweed - numerous other seaweed species, in fact, have been shown to exert remarkably beneficial effects on immune function, inflammation and the health of the gastrointestinal tract.
Like many of the foods previously mentioned, seaweed contains various chains of sugar molecules known as polysaccharides, many of which also exhibit gelling characteristics (some seaweeds, like agar, are even used as functional vegetarian replacements for gelatin).
These seaweed polysaccharides often exhibit protective effects upon the gastric mucosa. Like animal–based gelatin, the brown seaweed known as Sargassum polycystum has been shown to protect the gastric mucosa against injury:
Study Link – Efficacy of brown seaweed hot water extract against HCl–ethanol induced gastric mucosal injury in rats.
Quote from the above study:
These results suggest that the seaweed extract contains some anti–ulcer agents, which may maintain the volume/acidity of gastric juice and improve the gastric mucosa antioxidant defense system against HCl–ethanol induced gastric mucosal injury in rats.
Similarly, saccharides from Japanese mozuku seaweed (Cladosiphon okamuranus) have been shown to inhibit the binding of H. pylori to gastric cells:
Study Link – Inhibitory effect of Cladosiphon fucoidan on the adhesion of Helicobacter pylori to human gastric cells.
Quote from the above study:
...this fucoidan blocks both Leb– and sulfatide–mediated attachment of H. pylori to gastric cells. Furthermore, fucoidan–binding proteins were found on the H. pylori cell surface by Western blot analysis. Thus, the inhibitory effect exerted by Cladosiphon fucoidan on binding between H. pylori and gastric cells might result from the coating with this component of the bacterial surface.
But, unlike the other foods we've mentioned, seaweeds are unique, in that they contain saccharides consisting of the sugar, fucose. Polysaccharides consisting of fucose are known collectively as fucoidan, and are among the most intriguing substances in modern nutritional research. These seaweed polysaccharides have been researched as possible treatments for a wide range of disorders, including: arthritis, heart disease, cancer, liver disease, and even hormonal abnormalities. As we've repeatedly mentioned in previous newsletters, the health and integrity of the gastrointestinal tract always plays a fundamental role in all aspects of health and disease. It's likely that the far–reaching health benefits of seaweed have much to do with its unique ability to bind food and microbial lectins in the gastrointestinal tract - ultimately taking an enormous burden off of the liver and immune system.
As relates to dietary lectins, fucoidan has been shown to inhibit liver damage inflicted by the jack–bean lectin, concanavalin–A:
Study Link – Fucoidan prevents concanavalin A–induced liver injury through induction of endogenous IL–10 in mice.
Quote from the above study:
These findings suggest that fucoidan prevents Con A–induced liver injury by mediating the endogenous IL–10 production and the inhibition of proinflammatory cytokine in mice.
Various seaweeds have also been found to protect the liver in the animal model of fulminant hepatic failure:
Study Link – Effect of dietary fiber in edible seaweeds on the development of D–galactosamine–induced hepatopathy in rats.
Quote from the above study:
...the serum AST and ALT levels in the rats fed fucoidan were significantly low in comparison to those of the other groups fed the dietary fibers and the control. These results suggest that the protective effect of the three kinds of brown seaweeds Laminaria sp., Sargassum fulvellum and Eisenia bicyclis against D–GalN–hepatopathy was caused at least in part by fucoidan.
And a very interesting pilot study using the edible seaweed Fucus vesiculosus (also known as bladderwrack - a common nutritional supplement) in pre–menopausal women found that seaweed consumption could significantly reduce estrogen levels while simultaneously increasing levels of progesterone. The effects noted are generally considered to be in line with the reduced risk of estrogen–related disease noted in many Asian cultures:
Study Link – The effect of Fucus vesiculosus, an edible brown seaweed, upon menstrual cycle length and hormonal status in three pre–menopausal women: a case report.
Quote from the above study:
These pilot data suggest that dietary bladderwrack may prolong the length of the menstrual cycle and exert anti–estrogenic effects in pre–menopausal women. Further, these studies also suggest that seaweed may be another important dietary component apart from soy that is responsible for the reduced risk of estrogen–related cancers observed in Japanese populations.
The authors of this study noted that the cholesterol–reducing properties of the seaweed may have been responsible for its effects, but it's more likely that the liver–protective effect of the seaweed had more to do with it. Substances which "cleanse" the intestines (e.g., laxatives, antibiotics) are often shown to improve estrogen detoxification (along with improving PMS symptoms, etc.) via taking a significant burden off of the liver.
In keeping with this sort of protective anti–microbial function, seaweed polysaccharides have been shown to possess a wide range of antiviral antibacterial, and antifungal effects:
Study Link – Toxicity of an algal mucopolysaccharide for Escherichia coli and Neisseria meningitidis strains.
Study Link – Selective interaction of a Fucus vesiculosus lectin–like mucopolysaccharide with several Candida species.
We know that excessive immune stimulation, and an excessive release of inflammatory chemicals is often destined to inflict severe "collateral damage" to cells. It's also been well–documented that chronic inflammation is a contributing factor in nearly every degenerative disease of aging.
Knowing this, it's all the more encouraging to find that seaweed polysaccharides generally exert their anti–microbial effects simply by inhibiting adhesion of pathogen lectins to the body's cells - and not by increasing the inflammatory response of the immune system:
Study Link – Promising Antiviral Glyco–Molecules from an Edible Alga.
Quote from the above study:
In the time–of–addition experiments, the most sensitive stage of viral replication to the fucoidan was shown to be earlier than that to a neuraminidase inhibitor oseltamivir. The binding of the virus to host cells and the penetration into host cells were inhibited by the fucoidan.
Heeding the Signs
The signs of lectin–induced damage are often, at first, subtle. Those of us with no known food sensitivities may not connect the dots between food lectins and the common symptoms of fatigue, headache, water retention, chronic infection, joint stiffness, abdominal bloating, indigestion, stubborn weight loss, acne, and allergies (to name just a few). But armed with the knowledge that lectins lead to such symptoms - and ultimately, to many of the most prevalent degenerative diseases of our culture - the task of building our bodily defenses against them seems all the more worthwhile.
Though the effects of lectins have only relatively recently been elucidated by science, traditional foods like those mentioned here have historically protected humanity against numerous food–based toxins, including lectins. With our modern diet, however, our defenses have become few and far between. Though a return to a truly traditional manner of eating may be impossible, modern science has given us sufficient clues as to how to construct an effective defense against food–based toxins through proper diet and intelligent supplementation.
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