Ultra Simple Diet

[Approaching Infinity]

What I've found is that quinoa is GREAT when you cook it with some chicken or lamb broth. If you make some meat, just keep the broth and substitute it for water next time you cook quinoa. Even if it's just one cup, and the rest water, it tastes great.

 

[Gimpy]

What I've found is that quinoa is GREAT when you cook it with some chicken or lamb broth. If you make some meat, just keep the broth and substitute it for water next time you cook quinoa. Even if it's just one cup, and the rest water, it tastes great.

I'm finding that any grain is best done maybe once a week or even once a month. :( I'm going to start a rotation, because just eating meat and veg may not be enough nutrition. The latest experiment with buckwheat made me quite ill, so I'll be stopping that one for a few weeks before trying it again.

Currently I'm still weak, so it will be broth and soft veggies before I can try a grain again. Sheesh....now that I'm clear of dairy, gluten, and legumes.....once I eat something that may be iffy, it really knocks me down.


Does detoxing help with this?

 

[herondancer]

I've found that quinoa is sort of a blank slate grain. You can pretty much do anything with it, sweet, savory, whatever you are in the mood for. On it's own I find it pretty bland. Salt doesn't seem to be enough to save it.

After being off brown rice for a month, I find I really prefer quinoa. Buckwheat is a lifesaver too. I'm a type A, so D'Adamo turns out to be right for me. I still have that crisp/starch craving ("oh, for toast", she sighs), but crispy pancakes are filling the gap nicely. We're trying to work out a recipe for buckwheat crackers with flax and other kinds of seeds for snacks. Life can still be crunchy even without gluten!

Herondancer

 

[Gaby]

Does detoxing help with this?

Well, detoxifying makes your more sensitive in a sense. You can tell easier when something is bad for you. Perhaps you are one of those who do better on a "paleo diet". There is a blog here with some recipes that might be useful: http://www.marksdailyapple.com/ If you tested other sensitivities with the elimination diet, you will know better which recipes you can have and which ones you have to variate. You should be able to feel energetic.

Sending you some strength

 

[Gimpy]

Does detoxing help with this?

Well, detoxifying makes your more sensitive in a sense. You can tell easier when something is bad for you. Perhaps you are one of those who do better on a "paleo diet". There is a blog here with some recipes that might be useful: http://www.marksdailyapple.com/ If you tested other sensitivities with the elimination diet, you will know better which recipes you can have and which ones you have to variate. You should be able to feel energetic.

Sending you some strength

Thank you muchly! :) I really don't want to be more sensitive.....but detoxing has helped in so many other ways I need to stick with it. I'll look over the blog and see what I can do next. Thank you Psyche.

 

[Gimpy]

After doing some digging into my symptoms with the buckwheat, it appears the reaction I had resembles leaky gut in nine out of 24 listed symptoms here: http://www.jigsawhealth.com/resources/leaky-gut-syndrome-recommendations

Granted, its a vitamin site, but other sites were dismissive of the syndrome. (Like Wikipedia) I can't find my Sherry Rogers book at the moment, but when I do I'll it'll be time to get some more supplements on order. My Hubby was ready to cart me off to the ER so apologies if I vanish for a while to start taking care of this.

Another odd fact: the same day I had the attack, I had just finished talking to my Mother, who had the exact same symptoms nearly flatten her while out to a local play. Unlike me, she passed blood clots and did have to see a doctor, and is scheduled to have an MRI of her colon soon. She has a platelet disorder, her body eats its platelets and her blood doesn't clot well. She's also on large dose prednisone.

Could it be possible that I'm just worried for my Mother and 'sharing' her symptoms? :(

Thoughts?

 

[Avi]

I have been reading Ultra Mind Solution and started experimenting with elimination diet. It is obvious now how negatively gluten and sugar affect me after going a few days or week without and then having say a slice of pizza or something similar. Dairy is also one I have left behind for weeks if not months now and only really used it in coffee or tea, but now use rice milk and dont drink coffee anymore. I used to love cheese, but have not bought any for longer than I can remember. I thought I missed ice-cream until I had one a couple weeks ago and it sent me spinning! :O

I am sure it is not new to you all how resistant we can be sometimes, but looking at my resistance on this is really eye-opening! For I can realize the importance of cleaning the machine in all manners, physical detox being one of them, so intend to keep this going, resistance be damned!

I am not quite where I want to be but am farther along than the start of this year in terms of diet, detox and food I eat. Pretty simple, fish, chicken, beef, rice, veggies and fruit. Take daily 5-HTP and St. Johns Wart with a good multi and garlic capsules, still need to get the detox supplements advertised (such as DMSA) but thought I would chime in here with some of my experience and support for the entire concept of diet and detox.

:)

 

[Laura]

It's important to work on healing the leaky gut first of all. Perhaps the buckwheat is too much for some who are extra sensitive and have leaky gut.

 

[Gaby]

Here is some information on lectins

The Lowdown On Lectins

http://www.marksdailyapple.com/lectins/

Little known to the public at large. Little understood by the health community. Omnipresent in our conventional food culture. Proven to be at least mildly detrimental for everyone and downright destructive for the more sensitive (and often unsuspecting) among us. We’re talking lectins today: common natural agents on the one hand, cloaked thugs of the anti-nutrient underworld on the other. Our popular health media, if they’ve heard of lectins, certainly never make mention of them. Famous health gurus never deign to speak of them. In short, lectins thrive in the American diet basically unfettered, unscrutinized. Make no mistake, however. They’re a menacing power to be reckoned with. I’ve addressed them on Mark’s Daily Apple in the past (Why Grains Are Unhealthy) and in my book (The Primal Blueprint), but I still get a fair number of emails and forum questions asking for more info. As I always say, let’s break it down….

What Are They?

Before Monsanto, Mother Nature had her own pesticide strategy. (Humans being among the “pests” to be warded off.) In order to avoid being completely decimated by insects, foraging animals and Groks, plant species evolved assorted anti-nutrients that would make said pests regret their gorges with a variety of mostly digestive related ailments. Low grade toxins, in a sense. A workable balance developed between plants that were able to safeguard their species’ survival and the “pest” patrons that were able to benefit from the plants’ nutrition but learned to partake more sensibly from their supply. Given that our primal forefolk foraged widely and ate a surprisingly diverse diet, the system worked.

Lectins are essentially carb-binding proteins universally present in plants (and animals). Just as they protect plant species from Grok-sized predators, lectins also support other immunological functions within plants and animals (against pathogense, parasites, etc.) They also assist in other functions like protein synthesis and delivery in animals. They’re relatively sticky molecules, which makes them effective in binding with their sought after sugars but undesirable for our digestion, in which their binding powers can lead them to attach to the intestinal lining and wreak havoc. (More on this in a minute…)

Given their omnipresence in nature, a certain amount of lectin consumption has always been inevitable. To the benefit of the plants, lectins are also hard to break down. Regular old digestive enzymes only do about half the job. Human ingenuity evolved across traditional cultures to “predigest” lectins through food preparation practices (fermenting, soaking, etc.). In our contemporary dietary culture, however, we too commonly skip these practices yet rely on the highest lectin-containing foods for our primary food sources.

What Foods Contain Them?

The short answer here is basically all plants and animal products (PDF) to varying degrees. Nonetheless, lectins are concentrated more in some sources than others. Foods with the highest lectin activity include: grains of all kinds (especially wheat), legumes (especially soy), nuts, dairy, and nightshade plants (e.g. eggplant, tomatoes, potatoes, peppers, etc.). Add to this list the oils and other derivative products from these food sources. And yet another, lesser known category: GMO food, since lectins are often spliced into modified varieties in order to enhance “natural” pest and fungal resistance.

What Do They Do To The Body?

Let’s go back to the intestine again. (Some field trip, eh?) Lectins’ stickiness allows them to bind with the lining, particularly the villi, of the small intestine. The result? Intestinal damage (with impaired cellular repair potential), cellular death as well as compromised intestinal villi, which means reduced absorption of other nutrients, including minerals and protein. Add to this altered gut flora, which can allow certain harmful bacterial strains like E. coli to run rampant. Furthermore, because the body is now responding full-time to the needs of the injured gut lining, proteins and other resources are redirected from other basic growth and repair processes. Furthermore, lectins have been associated with leptin resistance (PDF), a pre-diabetic condition linked to obesity.

Perhaps the most insidious impacts lectins can leave in their wake is this: leaky gut. Leaky gut is a term for the breach in the intestinal lining created by lectins hand in hand with other antinutrients. Once the intestinal breach exists, lectins and other particles (like partially digested food, toxins, etc) can “leak” into the bloodstream.

Once lectins open the door, so to speak, out of the small intestine, they and other fugitive particles are now free to move about the body and bind to any tissue they come across (anything from the thyroid to the pancreas to the kidneys). Of course, the body reacts to these invaders by directing an attack on these particles and the otherwise perfectly healthy tissue they’re attached to. Enter autoimmune mayhem. That’s why lectins are linked with autoimmune disorders like IBS, Crohn’s, colitis, thyroiditis, fibromyalgia, chronic fatigue syndrome, and arthritis. Specific lectins have been associated with particular ailments (like wheat with rheumatoid arthritis), but more research is needed to trace and confirm these connections. What is clear, however, is the potent autoimmune destruction that can result when the intestinal lining experiences this level of damage.

Primal Advice For Limiting Lectins

As mentioned, lectins are literally everywhere. Although it’s impossible to eliminate them altogether, you can significantly reduce your intake.

* Purge the worst offenders. That means grains and soy more than anything, but I’d add other legumes to the list as well. Eliminating the foods that contain the highest lectin activity will slash your overall lectin intake – and impact.

* Cut back on other higher lectin sources. Not everyone wants to nix every dairy or nightshade option. Look at how you can reduce your overall intake of these items while keeping enough to enjoy their flavor and nutrient advantages.

* Gauge your sensitivity. For those of us who are most sensitive to lectins, more dramatic measures might be needed. If you know or believe that you’ve already suffered some serious intestinal damage, you might do well to steer clear of as many high and moderate lectin level foods as possible. That means perhaps forgoing nightshades, dairy, legumes and even nuts and eggs in addition to all grains and processed foods. Reintroduce desired foods back into your diet by “family” (e.g. dairy, etc.) and be mindful of any physiological effects (however minor) that accompany them.

* Take up old traditions like soaking, sprouting and using bacterial fermentation techniques for any moderate/high lectin foods like beans you choose to keep in your diet. Fermentation methods are especially effective, virtually eliminating lectins in one study of lentils. All those kitchen rituals you remember from Grandma? They’re adaptive, essentially pre-digestive techniques practiced by traditional cultures around the globe. Going old school on your favorite nut varieties, for example, cuts those lectin levels dramatically.

* Don’t go wholly raw. Yes, there are legitimate reasons to enjoy raw plants in your diet, but I don’t support the practice as a movement or exclusionary principle for eating. Humans have been cooking for well over a hundred thousand years. Some nutrients are enhanced by heat. Some anti-nutrients (like lectins) are at least partially “disarmed” by it. Cooking methods with a mind toward maximizing overall nutrient value and bioavailability make good Primal sense and can lower your exposure to lectins.

* Diversify! Restrictive diets make us even more susceptible to the downsides of our foods. (Soy formula fed babies being a dramatic example of this principle.) Make Grok proud and forage more widely for your dinner. Research shows that simply rotating primary foods was enough to limit lectin-related damage in rats that were given rounds of soy feed. A healthy, mostly low lectin diet will offer enough balance and protective nutrition to blunt the impact of the occasional moderate level lectin sources.

* Avoid GMOs. Hidden lectin is just one more reason to leave GMO products on the shelf.

* Maintain good overall gut health. Our modern existence sometimes seems like one giant assault against our digestive tracts. Minimize cumulative negative effects and increase positive, protective factors. Eat a healthy diet with Primal doses of probiotics, prebiotics and good fats. Limit stress and the use of medications like aspirin, NSAIDs and antibiotics (as well as secondary exposure through antibiotic-administered livestock). A healthy gut will be better equipped to weather the effects of inevitable but reasonable lectin intake.

 

[Gaby]

More info:

Essential Sugars and Plant Lectins

http://www.plantpoisonsandrottenstuff.info/content/toxins/essential-sugars-plant-lectins.aspx

Dietary lectins are associated with some intolerance reactions to food. Lectins are not considered a part of the food chemical intolerance syndrome, though they can cause similar negative reactions in vulnerable people. The effects of lectins are dose-related, and lectins can produce illness in any individual.

What are Essential Sugars?

"Essential sugars" is a bit of a misnomer, but one that is widely used. "Biologically active" sugars or "glyconutrients" is a more appropriate term, because like "essential fatty acids" from fish oils, we can actually make these valuable nutrients in our bodies. It's just that our bodies would rather not go to the effort of making these nutrients because the process is laborious, inefficient, and sometimes lacking.

Some people, such as the very young and old, the sick, and those with chronic health problems such as thyroid, adrenal, blood sugar, or hormonal problems, people with certain ancestries, or those whose bodies are under stress due to toxicity reactions or a lack of nutrients have difficulty making essential fatty acids, and the same seems to apply to essential sugars.

Essential sugars are sugars that have specific biological functions within the body. Different types of sugars coat the surfaces of cells and help them to communicate with each other. These sugars are monosaccharides (made from one molecule) like glucose or fructose, not disaccharides like sucrose (which is a molecule of glucose and fructose joined together) or lactose (which is a molecule of glucose and galactose joined together.

So far eight sugars which have specific biological functions in the body have been found. They are:

* Fucose
* Galactose
* Glucose
* Mannose
* N-acetylgalactosamine (GalNAc)
* N-acetylglucosamine (GlcNAc)
* N-acetylneuraminic acid (Neu5Ac), a form of sialic acid
* Xylose

All eight sugars are found in the myelin sheath that coats nerves and are important in correct nerve transmission inside and outside the brain. The sugars are woven together with amino acids to produce special protective proteins called glycoproteins. Low levels of glycoproteins have been connected to diseases like MS and schizophrenia. Salicylates are known to depress the ability of the body to produce essential sugars, particularly xylose, and weave sugars into glycoproteins, which is why they are relevant to failsafers.

Essential sugars are found in high concentrations in the kidney tubules suggesting they are important in correct kidney function, as well as in the testes where they may play a role in reproduction. They also have an important part to play in immune system modulation and normalisation and are found in white blood cells, macrophages and T cells.

They are also found in mucus and mucins (the excretions of the mucus membranes, both in the mouth and the intestines) which protect the body from invading pathogens and as such help the body to defend itself from infection. They may be relevant factors in preventing GERD, stomach ulcers, intestinal infections and diseases like Crohn's, coeliac, and ulcerative colitis.

Fucose
Fucose (not fructose, which has no biological function) is found in certain mushrooms, seaweeds including kelp, and beer yeast. As well as the above functions, Fucose also suppresses inflammatory reactions in the skin and can kill invading bacteria.

Galactose
Galactose is found in the lactose of dairy products, and as a monosaccharide in many fruits and vegetables. Galactose is known as "the brain sugar," and is vital for the correct brain development of babies and children (part of the reason that genuine lactose intolerance is extremely rare in babies). Excess galactose can be stored as glycogen and converted easily to glucose, though it does not stimulate insulin release by itself.

Glucose
Glucose is found in or can be made from all carbohydrate foods, as well as from some amino acids and even the glycerine component of fats. Its primary role is in correct brain function and energy production associated with insulin release and glycogen storage. The body's glucose storage capacity is limited and excess glucose is made into triglycerides (fats). Glucose also appears to have some body-building functions as it is present in the myelin sheath and the kidney tubules.

Mannose
Mannose is found in cranberries, blueberries, black and red currants, gooseberries, green beans, fenugreek, capsicum, cabbage, aubergine, tomatoes, turnips, shiitake mushrooms, kelp, and aloe vera. It is vital in preventing and curing urinary tract infections and stomach ulcers. E. coli and salmonella, common food-poisoning bugs, are vulnerable to mannose supplementation. Mannose is antibacterial, antiviral, antifungal, and antiparasitic. Mannose also stimulates collagen production and therefore plays a role in preventing arthritis and heart disease.

N-acetylgalactosamine (GalNAc)
Galactosamine is similar in structure to galactose. It is found in bovine and shark cartilages and is a constituent of chondroitin sulphate, one of the building blocks of collagen. It appears to play a role in preventing inflammation and in joint function and collagen formation and is a popular arthritis remedy. When taken together with glucosamine, the absorption of both is enhanced.

N-acetylglucosamine (GlcNAc)
Glucosamine is found in bovine and shark cartilage and in shiitake mushrooms. It is the major component of the arthritis remedy glucosamine sulphate.It too plays a role in preventing inflammation, in joint function, and collagen formation and repair. It is also found in the thyroid gland, the sebaceous glands of the skin, and the retinal tissues of the eyes. Glucosamine has been shown to decrease insulin secretion. When taken together with galactosamine the absorption of both is enhanced.

N-acetylneuraminic acid (Neu5Ac), a form of sialic acid
Sialic acid is found in eggs and the whey component of dairy. Most animals produce a different form of sialic acid (Neu5Gc) which humans cannot use directly due to a mutation in our genetic makeup. Neu5Gc is particularly found in red meats and the whey component of dairy and may be a potential hapten-style allergen. Sialic acid is a particularly important immune modulator. High levels are found in the brain, kidneys, bronchial tubes and upper airways, skin and reproductive organs and it may play a role in protecting the lungs and skin from infection and disease, in intelligence, and in fertility.

Xylose
Xylose is found in guava, pears, blackberries, loganberries, raspberries, kelp, echinacea, boswellia, psyllium, broccoli, spinach, eggplant, peas, green beans, okra, cabbage, corn, and aloe vera. Xylose is antibacterial and antifungal. It is a team player, and is a key sugar in cellular communication, forming the outermost protective layer of many cells.

Several of the essential sugars are found in aloe vera juice, which is used widely in the field of alternative health for preventing inflammation and easing digestive aliments such as stomach ulcers, and may have some use in Crohn's, coeliac, and other inflammatory bowel diseases. Essential sugars work best as a team and most have overlapping functions in the body, so supplementation with essential sugars works best when they are taken in combination.

For more on glyconutrients visit:

* Dr David Bird's glyconutrient site

What are Plant Lectins?

Plant lectins are poisonous proteins. Ricin is a lectin made from castor beans, and a well-known poison that has been used by the KGB and terrorists in the USA that causes massive blood clotting. Lectins have a wide variety of different structures and are grouped together under the term "lectin" based on their effects on human blood. Lectins are carbohydrate-binding proteins that attach themselves to essential sugars in the human body. They are glycoproteins just like their protective counterparts. Essential sugars typically coat the surfaces of cells and help them to communicate. Lectins bind to the essential sugars and disrupt cellular communication. When they do this, they can cause agglutination – that is, the blood may clump together. It is thought that plant lectins exist as defence mechanisms. Many have lethal effects on various insects and cause stomach upsets in foraging animals – and humans.

Plant lectins act directly to cause disruption in the functions of essential sugars. Pathogenic microbes make lectins and use them to attach themselves to potential host cells. The human body contains its own innate lectins that perform friendly roles in the body, such as on vascular endothelial linings to allow blood to escape into the tissues, in the liver to capture microorganisms, and as part of the immune system where they bind to antigens to make them vulnerable to destruction by white blood cells.

Plant lectins are found largely in:
* Legumes (all beans including kidney, chickpea, soy, and peanuts)
* Grains and seeds (wheat, quinoa, rice, buckwheat, oats, rye, barley, millet and corn)
* Nightshades (potatoes, eggplants, tomatoes, peppers)

They can also be found in:

* Nuts
* The Allium family (onions, leeks, garlic, shallots)
* Some vegetables (cabbage, herbs, celery, cucumber), peas, squashes, and fruits
* Dairy (being dependent on the lectin content of the diet of the animal)

"My grandmother would have laughed her head off if I told her that 20 years ago I got something like half a million dollars to find out whether uncooked kidney beans were good or not for us." - Dr. Arpad Pusztai, plant lectin specialist.

A well-known lectin, phytohaemagglutinin (PHA), is found in kidney beans and other legumes in the kidney bean family (black beans, pinto beans, etc). PHA binds to many essential sugars; it agglutinates white blood cells, reacts with mast cells (immune system cells) causing excessive histamine release, binds to the insulin receptors of fat cells mimicking insulin, and is highly toxic. When eaten in significant quantities, PHA causes gastrointestinal upset identical to food poisoning. A misguided hospital "healthy eating day" lead to one such mass poisoning event.

In addition to PHA, wheat germ agglutinin, concanavalin A (found in jack beans), and several other lectins are known to be insulin mimetics and are probably best avoided by those wishing to prevent unexpected blood sugar fluctuations.

Other lectins target specific essential sugars. For example the following lectins all work by specifically binding glucosamine:

* Barley (Hordeum vulgare)
* Potato (Solanum tuberosum)
* Rice (Orysza sativa)
* Rye (Secale cereale)
* Tomato (Lycopersicon esculentum)
* Wheat Germ (Triticum aestivum) aka (T. vulgare)
* Blackberry (Rubus fruticosus)
* Pumpkin, Marrow, Winter Squash (Cucurbita maxima)
* Tamarillo, Tree Tomato (Cyphomandra betacea)

And the following work by binding galactosamine:

* Soybean (Glycine max)
* Corn, Maize (Zea mays)
* Lima Bean (Phaseolus limensis) aka (P. lunatus)

We know that deficiencies in the essential sugars are associated with a variety of ailments. For example, deficiency and dysfunction of galactosamine and glucosamine are associated with many cases of rheumatoid arthritis, an autoimmune condition where the body attacks its own cartilage. It is also known that many cases of rheumatoid arthritis are diet-responsive, and that by removing the above list of foods from the diet, rheumatoid arthritis can be halted, reversed, and even in some cases effectively cured so long as the individual abstains from eating these particular foods. It may be that some diseases suffered by failsafers, such as arthritis, progress through the effects of a combination of food chemicals. For example, salicylates first depress xylose production, followed by a lectin binding to the exposed sugars underneath.

Plant lectins have also been associated with behavioural and neurological problems, such as autism and ADHD, and schizophrenia and MS. Indeed a complex carbohydrate free diet has proven useful for children with autism. Perhaps part of the real reason for this is that the diet cuts out beans and grains, the two biggest suspects in lectin-related diseases.

Many pathogens act by producing lectins, including the streptococcus bacterium family which is often responsible for respiratory tract infections and skin infections. Helicobacter pylori is the bacterium responsible for stomach ulcers. H. pylori has a special affinity for blood type O glycoproteins. It acts by binding to several essential sugars, in particular mannose, fucose and glucosamine. The mucous lining in the stomach is designed to prevent such infections by providing essential sugars onto which the bacteria can attach and be washed away, rather than allowing it to attach to the sugars in the stomach wall. Dietary lectins, particularly ones that react with mannose such as:

* Broad bean, Fava bean (Vicia faba)
* Corn, Maize (Zea mays)
* Garden Pea (Pisum sativum)
* Garlic (Allium sativum)
* Jackfruit - tropical relative of breadfruit (Artocarpus heterophyllus)
* Leek (Allium porrum)
* Lentil (Lens culinaris)
* Onion (Allium cepa)
* Shallot (Allium ascalonicum)
* Taro (Colocasia esculenta)

And fucose such as:

* Garden Pea (Pisum sativum)
* Lentil (Lens culinaris)

As well as the glucosamine list mentioned above (that contains many grains including wheat and several nightshades including tomato and potato), work by stripping away this essential mucous in vulnerable individuals and allowing h. pylori to gain a foothold into the stomach lining. There the h. pylori lectins act by disrupting the communication of immune system cells, which stimulates excessive histamine production, which in turn stimulates excessive acid production. A reasonable approach therefore, for controlling stomach ulcers is to remove lectins from the diet, remove salicylates from the diet (they depress production of protective glycoproteins), take antibiotics that kill h. pylori, and feed the body a combination of essential sugars.

Eating too many lectin-containing foods or catching a lectin-producing pathogen can lead to autoimmune disease. It is frequently observed that autoimmune conditions (where the body mistakenly attacks itself) often arise after a serious infection. Rheumatoid arthritis, multiple sclerosis, Guillian-Barre syndrome, Type 1 diabetes, and a whole host of other autoimmune conditions are associated with both infections and with eating lectin-containing foods. It is thought that lectins work by stripping away certain essential sugars from cell surfaces, making them display incorrect antigens and appear to be foreign to the body's immune system. They may also work simply by binding irreversibly to particular cells or proteins, forcing them to be taken out of circulation by white blood cells. These are the mechanisms through which coeliac (celiac) disease is thought to be mediated. Food allergies may also be mediated by lectins.

"Lectins stimulate class II HLA antigens on cells that do not normally display them, such as pancreatic islet and thyroid cells. The islet cell determinant to which cytotoxic autoantibodies bind in insulin dependent diabetes mellitus is the disaccharide N-acetylgalactosamine, which must bind tomato lectin if present and probably also the lectins of wheat, potato, and peanuts. This would result in islet cells expressing both class II HLA antigens and foreign antigen together---a sitting duck for autoimmune attack. Certain foods (wheat, soya) are indeed diabetogenic in genetically susceptible mice. Insulin dependent diabetes therefore is another potential lectin disease and could possibly be prevented by prophylactic oligosaccharides." - David L J Freed, Do Dietary Lectins Produce Disease?

The good news is that the effects of dietary lectins only extend for as long as they are in the body, and the effects of both dietary and pathogen produced lectins can be reduced with supplementation of essential sugars. Furthermore some lectins in foods can be reduced (but not eliminated) by a variety of methods:

* A minimum ten minute boiling period (skimming off the scum), in beans and grains
* Cooking thoroughly, in vegetables
* Sprouting beans and grains
* Fermenting of bean and grain products

The bad news is that not all lectins are completely destroyed by these methods, and that some particularly stubborn lectins in beans remain no matter how lengthy the treatment. Soy (soya) lectins, for instance, are virtually impossible to destroy. To learn more about lectins, visit:

* Do Dietary Lectins Cause Disease?
* The Lectin Report
* Plant Lectins
* Lectins in Foods
* Lectins: Their Damaging Role in Intestinal Health, Rheumatoid Arthritis and Weight Loss

This information is complementary to our favorite article: Opening Pandora's Bread Box: The Critical Role of Wheat Lectin in Human Disease, where it refers to the supplementation of this essential sugars as follows:

One way to gauge just how pervasive the adverse effects of WGA are among wheat-consuming populations is the popularity of the dietary supplement glucosamine.In the USA, a quarter billion dollars' worthof the glucosamine is sold annually.The main source of glucosamine on the market is from the N-Acetylglucosamine rich chitin exoskelotons of crustaceans, like shrimp and crab. Glucosamine is used for reducing pain and inflammation. We do not have a dietary deficiency of the pulverized shells of dead sea critters, just as our use of NSAIDs is not caused by a deficiency of these synthetic chemicals in our diet. When we consume glucosamine supplements, the WGA, instead of binding to our tissues, binds to the pulverized chitin in the glucosamine supplements, sparing us from the full impact of WGA. Many millions of Americans who have greatly reduced their pain and suffering by ingesting glucosamine and NSAIDs may be better served by removing wheat, the underlying cause of their malaise, from their diets. This would result in even greater relief from pain and inflammation along with far less dependency on palliative supplements and medicines alike.

 

[Gaby]

Continuing on the lectin subject:

THE LECTIN REPORT

http://www.krispin.com/lectin.html

Krispin Sullivan, CN 03/19/10

While research in lectinology is in its infancy this information is critical to your health and it is important to begin to understand lectins NOW. Read the following report carefully. I'll get specific about how this all applies to you. ALL foods contain lectins. Some are your friends, others neutral, and others may be your enemies. Know your lectins. Avoid your enemies.

* Lectins in plain English, do lectins cause disease?
* What makes someone lectin intolerant?
* What do lectins have to do with me?
* How can I tell if I am lectin intolerant?

LECTIN

ID: lectin
PART OF SPEECH: n
SYNONYM: Plant Hemagglutinin
TERM ELEMENT: Hemagglutinin

DEFINITION
Protein or glycoprotein substances, usually of plant origin, of non-immunoglobulin nature, capable of specific recognition of and reversible binding to, carbohydrate moieties of complex glycoconjugates without altering the covalent structure of any of the recognized glycosyl ligands. This group includes monovalent lectins (i.e. bacterial and plant toxins). These lectins bind to sugar moieties in cell walls or membranes and thereby change the physiology of the membrane to cause agglutination, mitosis, or other biochemical changes in the cell. (agglutination- clumping; mitosis-multiplication or division of a cell forming two daughter cells)

Lectins were first described in 1888 by Stillmark working with castor bean extracts. Many members of the lectinic protein family agglutinate (clump together) red blood cells. Research done by Ehrlich, considered to be the father of immunology, has shown that feeding small amounts of lectin containing seeds to rabbits caused partial immunity to the toxicity demonstrating lectins are also antigenic (able to induce antigen antibody reactions).

High levels of lectins (specialized proteins) may be found in grains (also known as cereals or pulses), legumes (that is 'beans' including peanuts), dairy and plants in the nightshade family. Many other foods contain lectins but are less well studied and the amounts of lectins present are not thought to be as high or as potentially toxic.

Lectins purified from the germinating seeds of wheat (Triticumspp.); bind to carbohydrate moieties on cell surface glycoproteins and are used to identify certain cell populations and inhibit or promote some immunological or physiological activities.

Lectins purified are used to determine one's blood type (ABO). Lectins from the castor bean are highly toxic and can kill if ingested in even small amounts. Lectins from kidney beans have been implicated as cause in an outbreak of 'food poisoning' with no known pathogen.

Think of a lectin as a protein containing a key that fits a certain type of lock. This lock is a specific type of carbohydrate. All life forms, plant and animal, insect and fungus have cell membranes that contain carbohydrates that sit within and project from the membrane. If a lectin with the right key comes in contact with one of these 'locks' on the gut wall or artery or gland or organ it 'opens the lock', that is disrupts the membrane and damages the cell and may initiate a cascade of immune and autoimmune events leading to cell death.

Lectins can be inactivated by specific carbohydrates (technically known as mono and oligosaccarides) which can bind the 'key' and prevent the protein from attaching to the carbohydrate 'lock' within the cell membrane. Glucosamine is specific for wheat lectin and it is this specificity that may protect the gut and cartilage from cell inflammation and destruction in wheat (or gluten) responsive arthritis.

While various foods and supplements may inactivate some of these toxic lectins it is impossible for such substances to protect the body from them completely. The safest path is avoidance of known toxic lectins. Common foods with known toxic lectins include all soy and wheat products including oils from these substances.

I have always promoted adequate protein in all of my dietary programs with moderate 'good' fats and moderate complex carbohydrates and plenty of fruits and vegetables. For some clients consistently eating enough protein was and is difficult. They (and the culture in which we currently reside) tend to diminish protein's important contribution to health, both mental and physical. When protein intake is maximized clients have found this moderate, easy to follow, program has aided them in restoring function of body and mind.

For some of my most difficult clients this simple basic program just hasn't given them the level of health and well being they so very much desire. Some of these most difficult clients have reported improvement in health using high protein, low carbohydrate diets. Some of the very best results came when switching to the so-called Paleolithic Diet. These programs included The Zone by Sears (the least effective of the bunch and the highest in lectins); D'Adamo's Blood Type Diet (the second highest in lectins and also not as effective); Eades Protein Power ; Atkins Diet Revolution ; The Specific Carbohydrate Diet from Breaking the Vicious Cycle by E Gottschall; and Neanderthin by Audette; and the Crook Candida Diet. The commonality is higher protein (and often natural unprocessed fats) and a reduction in carbohydrates, especially carbohydrates high in lectins.

Research shows a connecting link between these diets and the improvement in health being reported. Some of the symptoms and conditions that have been reported to respond include

* arthritis, both rheumatoid and osteoarthritis;
* allergy;
* asthma;
* high cholesterol;
* atherosclerosis;
* congestive heart failure;
* high blood pressure;
* diabetes;
* low blood sugar;
* hyperinsulinemia;
* chronic fatigue;
* fibromyalgia;
* all forms of IBS, Crohn's, colitis, celiac;
* chronic candida, repeated gut pathogen infections;
* malabsorption syndromes;
* failure to thrive;
* autoimmune diseases such as thyroiditis, lupus, MS, Parkinson's;
* dementia, Alzheimer's;
* autism;
* ADD/ADHD;
* Schizophrenia;
* osteoporosis;
* cancer, several types including breast;
* hypercortisolemia and hypocortisolemia;
* adrenal insufficiency;
* post viral syndrome;
* post traumatic stress syndrome;
* post polio syndrome;
* obesity;
* hormonal imbalances including low testosterone, low DHEA, PMS, and peri-menopausal symptoms and PCOS.

Higher protein has been shown clinically to improve many of these conditions but not all and it is not a wide enough connecting link.

In the 1970s research on lectins, lectinology, began increasing worldwide. For a more scientific overview see the end of this report.

Take a moment and visit the link below before continuing, to see Dr. Freed's concept of the lectin problem.

BMJ 1999;318:1023-1024 ( 17 April )
Editorials
Do dietary lectins cause disease?

Now my explanation of the problem-.

In Plain English

Lectins are found in ALL foods, certain foods more than others, and the same food may contain varying amounts of lectins depending on processing, when and where the plant was grown, and species.

The most common potentially 'toxic' lectin containing food groups are

*grains, especially wheat and wheat germ but also quinoa, rice, buckwheat, oats, rye, barley, millet and corn.
*legumes (all dried beans, including soy and peanuts),
*dairy (perhaps more so when cows are feed grains instead of grass, a speculation based on research showing transference of lectins into breast milk and dairy.
*nightshade (includes potato, tomato, eggplant and pepper).

Dairy may be potentially more harmful in pasteurized, processed milk because of the reduction of SIgA, an immunoglobulin that binds dangerous lectins , Biol Neonate 1991;59(3):121-5 Davin JC et al The high lectin-binding capacity of human secretory IgA protects nonspecifically mucosae against environmental antigens.), NOTE: Only breast milk is good for babies.

Each of these groups has a history of being implicated as allergenic. Also note that we are including all foods made from these substances, (these substances in all forms, milled grains, flours, oils, vinegars), peanut butter, cereal or legume oils (soy, canola, corn), additives, thickeners, grain vinegar and products containing grain vinegar, grain alcohol including grain based vodka, and all beers and ales. The only non-grain based alcohols are 100% Agave tequila and 100% potato vodka. Grape based alcoholic beverages are probably allowed if you know you tolerate them.

There has been some information that lectins may be inactivated by soaking, sprouting, cooking or fermenting. Soaking legumes over night, draining the water, rinsing and draining again does seem to remove or inactivate many of the lectins. Heating seems to remove others in some foods but not all. There is little data to prove that any of these methods remove lectins completely as few foods have been tested and of those that have lectins many seem to remain after processing.

Excerpt from Plant Lectins , Pusztai A, Cambridge University Press 1991 pg.108

Nachbar and Oppenheim (1980) found 30% of fresh and PROCESSED foods contained active lectins. Lectins from green salads, fruits, spices, seeds, dry cereals and nuts (even after roasting) showed activity of potentially toxic lectins. Some of these lectins interact with serum or salivary components and bacteria from the oral cavity (Gibbons & Dankers, 1981).

Another example of the hardiness of lectins is the study by Klurfeld DM and Kritchevsky D Lipids 1987 Sep:22(9):667-8,

Isolation and quantitation of lectins from vegetable oils.

Results-Unrefined soy oils contained 858-2983 mcg/kg. After refining oils contained 24-55 mcg/kg. Both refined and unrefined soy oil contained soy lectins.

From Plant Lectins A Pusztai 1991 Table 6.9 page 179

Common features of toxic (non-nutritive) effects in lectin-gut interactions.

1. High degree of resistance to gut proteolysis.
2. Binding to brush border cells; damage to microvillus membrane; shedding of cells; reduction in the absorptive capacity of the small intestine.
3. Increased endocytosis; induction of hyperplastic growth of the small intestine; increased turnover of epithelial cells.
4. Interference with the immune system; hypersensitivity reactions.
5. Interference with the microbial ecology of the gut; selective overgrowth.
6. Direct and indirect effects (hormones, etc.) on systemic metabolism.

Especially note #5. The popular Candida Diet is essentially a high protein, low carbohydrate diet which limits starches and sugars and thereby limits lectins. If lectins are a problem for this person (the so-called 'candida' patient) lectin ingestion may be associated with overgrowth of various gut pathogens that may include yeasts and removal of lectins would restore the gut ecology and the gut immune system. If this is true, the diet does not get rid of yeast but relieves the person from symptoms and pathogenic consequences caused by ingestion of lectins to which he or she is intolerant..

Lectins are hardy proteins that do not break down easily. They are resistant to stomach acid and digestive enzymes.

Lectins may bind to the gut wall and damage the gut lining, are not altered by digestive enzymes, and may alter gut permeability and pass through the gut into general circulation.
Lectins can cause alterations in gut function that may be related to colitis, Crohn's Disease, Celiac-Sprue, IBS and gut permeability.

Lectin damage to the gut wall may allow other non-lectin proteins to cross undigested into general circulation and cause allergic reactions, including anaphylaxis.
Having gained access to general circulation various lectins may bind to surface cell membranes in arteries and vessels, organs and glands, including the thyroid, pancreas, kidney and adrenals, in susceptible animals and humans.

This binding may begin antigen antibody reactions leading to autoimmune disorders and so-called degenerative diseases.
Different lectins have been implicated in different diseases. Dairy lectins have been implicated in juvenile onset type I diabetes. Wheat lectins have been implicated in juvenile nephropathy.

Type or types of lectin and one's susceptibility (genetic susceptibility) cannot be determined by blood type. D'Adamo tested lectins with blood cells. Lectin intolerance reactions occur in the gut, general circulation (artery walls and the like), brain, gland or organ as well as red blood cells. Sensitivity of one type of cell does not necessarily determine whether another type cell will or will not react.

SIgA, and other immune factors may, if sufficient in quantity, help protect against some exposure to toxic lectins. See abstract at end of report.

GM (genetically modified foods) are modified by splicing 'lectins' from one plant family to another. This is extremely problematic. If you know you react to a particular plant family but that lectin has been put in a plant not of that family you may consume the 'toxic to you' lectin, have the reaction/response and not know the cause.
We are or become lectin sensitive because of

* genetics, our ancestors just didn't evolve eating this type of food and our immune system can't handle it;
* a failure of SIgA barrier protection, genetic or environmentally induced;
* bacterial or virus infection, certain bacteria and virus, including the influenza virus, can damage our cells making them susceptible to lectin antibody/antigen reactions
* or by the use of NSAIDS (non-steroidal anti-inflammatories) or other drugs which increase gut permeability and allow lectins to enter general circulation.

Historically diagnosis and treatment of Celiac-Sprue related to 'gliadin' (also known as gluten) sensitivity. Gliadin is found in wheat, rye, barley, oats, and foods containing these grains (including beer, grain based alcohols, mayonnaise, grain vinegar, etc). Some Celiacs did not respond to elimination of gluten/gliadin. In 1951 Drs. Sidney V. and Merrill P. Haas published Management of Celiac Disease documenting treatment and cure of celiac and cystic fibrosis of the pancreas with a carbohydrate limiting diet introduced as the 'Specific Carbohydrate Diet'. More information about this diet can be gotten from Breaking the Vicious Cycle E Gottschall, BA, MSc. Kirkton Press Ltd. Baltimore, Ontario, Canada 1998.

In many cases cited in the book, elimination of certain carbohydrates 'cured' diagnosed Celiacs after one year and they were able to return to eating gluten containing foods. In hindsight many of the foods eliminated in this plan are high lectin foods known to be associated with gut and systemic inflammatory reactions. Celiac-Sprue is a genetic disorder treated by elimination of offending foods. The response of some to the specific carbohydrate elimination diet would likely mean that the patients who responded did not have classic gluten intolerance, Celiac-Sprue, which requires life long elimination of gluten/gliadin. It suggests that other lectins may cause similar symptoms and overlapping diagnostic and treatment difficulties.

If all cases of lectin intolerance were genetically based reversal of intolerance would not be possible. There must therefore be a subgroup of IBS, Crohn's, Celiac, colitis that is related to sensitization to food lectins that can be reversed by avoidance of these lectins and a restoration of gut function including SIgA and other immune protectors. Bacteria, virus, or other conditions, drugs or injurious substances acting directly on the gut wall may cause sensitization.

Tests are available to determine SIgA levels, and gut immune reactions to soy, dairy, wheat and egg. These tests do not cover the entire family of lectins, nor would blood or skin tests necessarily show sub-clinical sensitivity reactions. Most of the conditions associated with sub-clinical lectin intolerance appear to be degenerative, often taking extended periods of time to appear and longer to reach life threatening or painful (such as arthritis) stages. Many lectin related conditions may be considered to be 'autoimmune'.

Awareness of genetically based intolerance to one or more lectin groups is important family information. If you or another family member has such an intolerance other family members need to be aware and test themselves to prevent problems before they begin.

Infectious or drug related food intolerance responses need to be prevented or reversed. These antigen/antibody responses may be reversible but avoidance of offending lectins should be considered for a minimum of one year before reintroduction to test.

Lectins and their possible involvement in degenerative and autoimmune disease is a relatively new science.

This report, as presented, is hypothesis, not yet fully supported by clinical trials and not yet at a stage where we have any idea of how to connect 'family' with lectin response. What facts can be supported include-

* Proteins institute most allergic and antigenic responses.
* Lectins are proteins found in large amounts in the foods as above.
* Lectins are not easily removed from foods or rendered harmless to animals and humans.
* Lectins from soy, peanut and other beans, wheat germ and wheat, milk, peanut oil (and perhaps other seed oils including soy oil) and nightshades, in a variety of clinical studies have shown various damage to gut lining, joints, kidney, pancreas and brain (even able to cross the blood-brain barrier).
* Lectins found in peanut oil have been implicated in atherosclerosis. Leaving open the possibility that other seed oils contain damaging lectins and that polyunsaturation and free radicals may not be the full picture on the dangers of polyunsaturated fats.
* You may react to lectin toxicity due to genetics, intensity of exposure, failure of immune factors to protect you, viral infection, bacterial infection or gut permeability induced by medication or infection.
* Lectin toxicity (antigen-antibody response) can be 'sub-clinical' not showing obvious symptoms for many years.

SO WHAT DOES THIS MEAN TO ME AND WHAT CAN I DO?

Lectin intolerance is not an 'allergy'. A person may be lectin intolerant and not have antibodies to the suspect food when given an allergy test whether blood or skin or saliva. A person may be lectin intolerant and because of the damage done by lectins end up having allergic reactions to a food (that does not contain lectin or may have other lectins), other chemicals or the environment. Lectin intolerance means the inability to deactivate the toxic lectin (prevent its binding to your cells) in the confines of your own body, be it in the gut, artery, organ, gland or brain. The lectin then proceeds to invoke immune responses that damage the cell to which it attaches and possibly surrounding cells. This antigen/antibody response may be the key to many or even most autoimmune diseases and many degenerative diseases may need to be reclassified as autoimmune.

If you or other family members are suffering from any of the symptoms, conditions or diseases mentioned in this report consider an elimination diet to test for lectin sensitivity. If you have been diagnosed with Celiac-Sprue by blood and biopsy testing you must remove gluten/gliadin for the rest of your life. For help with this visit http://www.csaceliacs.org/ If, however, elimination of this glycoprotein does not resolve your problem consider other lectin families as possible offenders. It is also possible to be gluten intolerant and intolerant to one or more of the other lectin families.

Elimination Diet: Remove all suspect lectin families (legumes, dairy, etc) for 7 days. Make sure to read labels so that you aren't consuming a part of the lectin family hidden in a food. On day 8 reintroduce several of the family members, such as, if testing dairy, milk, cheese and sour cream or legumes, soy, kidney bean and peanut butter. Eat some of the family at each meal. Stop all of the family for the next two days. That is 7 days off, one day on and 2 days off. Check your symptoms on the day of testing and the following 2 days. Look for changes in energy, appetite, bowel function, mood, sleep, skin, digestion, anything suspicious. Test only one 'family' at a time. You may remove as many groups as you feel are suspect but only reintroduce one family at a time. If you find you must eliminate one or more lectin families retest every six months to see if the intolerance is genetic or induced.

Common groups: Dairy; legumes (includes soy and peanuts); nuts; seeds; nightshades, includes potato, tomato, eggplant; eggs; grains, esp. gluten grains such as wheat, rye and barley but corn can be an antigen too. Millet, wild rice and plain white rice are usually safe substitutes while testing grains.

Most persons are aware that there are certain foods they seem to 'react' to. Symptoms could be obvious, such as gas, bloating, diarrhea or constipation (or both, alternating). Less obvious symptoms may include headache, fatigue, 'indigestion', skin problems including hives, psoriasis, swollen joints or water retention. While some symptoms while resolve quickly after eliminating an offending family other symptoms may take 6-12 months. Be patient. If you are genetically intolerant you will never be able to consume that group of foods safely.

Some symptoms may occur chronically and may seem in no way related to a gut/food or lectin intolerance reactions. This group of symptoms includes the so-called degenerative diseases and autoimmune diseases like those mentioned in the list at the beginning of this report including atherosclerosis, hypertension, osteoporosis, senile dementia, osteoarthritis and rheumatoid arthritis, inflammatory joint diseases, fibromyalgia, chronic fatigue, and adult onset diabetes. Obesity has been associated with consumption of 'enemy' lectins.

If your condition responds to elimination of one or more of the high lectin groups, consider your intolerance to be at minimum, induced by the environment (infection or medication induced), and continue to restrict your diet for one year before testing a food-lectin group for re-inclusion. If you again react consider your intolerance a probable genetic inheritance and avoid this type of lectin containing food group as completely as you are able.

For severe symptoms or conditions eliminate all of the major suspect groups, all grains, all legumes, and all dairy. Add the nightshades, potato, tomato, eggplant and pepper, to your restricted list if your symptoms are associated with rheumatic or arthritic complaints. If you respond to this elimination diet by a resolution of symptoms keep out the food group/s for a minimum of six months to one year before reintroducing the group/s. If symptoms reappear consider lifelong avoidance. Rarely does a person have to eliminate more than one or two of the lectin families on a long-term basis. You must let your body decide.

WHERE CAN I GET HELP IN DETERMINING MY INTOLERANCE OR HELP WITH DIET TO TEST OR MAINTAIN?

Throughout our history our ancestors had limited exposure to many lectin families depending on location. In our modern world it is common to believe that we can eat any food we like. We can but the food we eat may not like us. Some persons (a minority) can tolerate all foods. For the rest of us most will find one or more lectin groups they do not tolerate. Of those who experience antigen responses most will not need to eliminate more than one or two major lectin groups. You have to experiment and see 'who' you are and 'what' your ideal foods are. It is a process.

Consider the group most likely to be causing a problem.

* Deadly nightshades including tomato, potato and eggplant.
* Glutens found in wheat, rye, barley, malt, and oats.
* Legumes, all beans including soy and peanut.
* Dairy including all milk products, milk, cheese, cottage cheese, yogurt, kefir.
* Eggs

These are the most common lectin families that cause problems. Eliminate the suspect group for 7-10 days. Don't eat any of the group. Check to make sure none of the lectins are contained in other foods you consume. Example: Vinegar is made from grain and contains gluten unless it is apple cider vinegar or wine vinegar. Mayonnaise contains gluten because it is made with grain vinegar.

After abstaining for 7-10 days eat a significant amount of the suspect group over one day. Eat other foods as well. Do not eat any more of the test group for two days after the test day.

Look for symptoms of intolerance: bowel changes, sleep changes, mood changes, memory impairment or any other significant changes you can relate to the ingestion of the food group. It may take a day or so for the symptoms to appear. If you think you have found a lectin incompatibility avoid the food. You can test again in a few weeks. If every time you avoid the food your symptoms resolve and every time you eat it they return you have found a lectin you should not eat.

Books mentioned at the beginning of this report by Atkins, Eades, Audette, or any of the authors promoting the Paleo Diet (Hunter-Gatherer) are good resources for menus. Eades and Atkins have some recipes that include dairy, soy and nightshade, some of the suspect foods, so don't choose those recipes. None of Audette's recipes use any major lectin groups. It does have some recipes with nightshades. Watch out for those recipes if you think it is a group you react to. Fallon and Enig's Nourishing Traditions is still a great cookbook just watch out for the lectin containing foods, from the group/s you are avoiding, in recipes.

There are support groups for gluten intolerance, dairy intolerance and soy intolerance but since the idea of lectin intolerance and the broadness of the groups is so new you will have difficulty finding support and information in one place.

If you or your physician need more information, support or research citations I can be reached at K. Sullivan, PO Box 6988, Incline Village, NV 89450-6988. 1-775-831-0292. As I am a educator/consultant and this is how I pay my bills there is a consult fee for my time. I cannot provide individual consultation/information to persons who are not my private clients for both legal and medical reasons. Using the elimination and reintroduction technique describe above will allow most persons to determine their lectin sensitivities.

The following link takes you to an article that explains some of the current concepts in lectinology.
Introduction to "Lectin"

Jun Hirabayashi (Teikyo University Faculty of Pharmaceutical Sciences)

This article also mentions animal lectins which are not at this time considered to be potential toxins/allergens for humans. We are concerned with the more commonly known and studied potentially toxic/allergenic plant lectins as listed above.

OK, kind of technical but you get the idea. Lectins are

* important,
* in most foods, with plant foods containing the highest levels of known toxic lectins and
* while they have existed as long as life has existed they are not yet well researched or understood. See the first line of the above paragraph to understand how this is just the beginning of this base of knowledge.
* Lectins can be extremely toxic, causing rapid death, or
* may in some situations and in some species be useful in preventing or reversing conditions and illnesses such as cancer.
* Most lectins fall somewhere in between these two extremes allowing the possibility of subclinical conditions which appear over time and which don' t appear to be directly related to lectin exposure.


Biol Neonate 1991;59(3):121-5 The high lectin-binding capacity of human secretory IgA protects nonspecifically mucosae against environmental antigens. Davin JC, Senterre J, Mahieu PR Department of Pediatrics, State University of Liege, Belgium.

The anti-infectious role of human milk may be, at least partly, ascribed to its content in secretory IgA. As lectins are present in various infectious antigens, the binding of different types of IgA to three lectins (concanavalin A, peanut agglutinin, wheat germ agglutinin) was studied by Elisa. The specificity of those bindings was assessed by inhibitory experiments performed with the corresponding oligosaccharides. The following were found for the three lectins: (1) the lectin-binding capacity of colostrum secretory IgA was markedly greater than that of normal plasma IgA1 (p less than 0.001); (2) the lectin-binding capacity of polymeric IgA1 was greater than that of monomeric IgA1 (p less than 0.001). This property of mucosal IgA may be responsible of a nonimmune opsonization able to prevent the early step of some infectious mucosal diseases, i.e. the attachment of bacteria to epithelial cells by lectin-like bonds and also the penetration into the body of some antigens able to favor the development of allergy. Milk mucosal IgA, present in significant amounts in human colostrum and mature milk - but not in infant formulas - may therefore play an important polyvalent protective role in newborns.

IgA antibodies to dietary antigens and lectin-binding IgA in sera from Italian, Australian, and Japanese IgA nephropathy patients. Coppo R;Amore A;Roccatello D;Gianoglio B;Molino A;Piccoli G;Clarkson AR;Woodroffe AJ;Sakai H;Tomino Y

We studied serum IgA as antibodies to dietary antigens (Ag), as lectin- binding molecules, and as conglutinin-binding immune complexes (IgAIC) in people from geographical areas in which IgA nephropathy (IgAGN) is particularly frequent. Sera from 63 Italian, 21 Australian, and 25 Japanese patients affected by IgAGN and 24 Italian, 20 Australian, and 40 Japanese healthy controls were studied. Increased values of IgAIC were detected in 42.8% of Italian patients, while only in 23.8% and 8% of Australian and Japanese patients, respectively. Mean values were significantly increased only in Italian patients (P less than 0.0001). Positive values of IgA antibodies against dietary Ag had variable prevalences, but again Italian patients showed the highest frequency, from 19% to 28.5% versus 0 to 38% in Australians and 0 to 16% in Japanese. Mean values of these antibodies were not significantly increased in any patient groups in comparison to the corresponding healthy populations. However, patients with elevated values of IgAIC had significantly higher serum concentrations of antibodies to alimentary components and a linear correlation was found between IgAIC and some IgA antibodies to food components. The relationship between these two series of data was particularly evident for Italian and Australian IgAGN patients. Moreover, the patients with positive data tended to have a cluster of increased levels of IgA antibodies against several alimentary Ag at the same time. A linear correlation was evident between values of IgA antibodies to gluten fractions and to heterologous albumins. None of these correlations was evident among healthy controls.(ABSTRACT TRUNCATED AT 250 WORDS)

Invest Ophthalmol Vis Sci 1991 Dec;32(13):3277-84Identification of lectin binding proteins in human tears. Kuizenga A, van Haeringen NJ, Kijlstra A
Biochemical Laboratory, Netherlands Ophthalmic Research Institute, Amsterdam.

The identity of glycoproteins in stimulated normal human tears was investigated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) of tears onto minigels, blotting, and subsequent incubation with different biotinylated lectins (concanavalin A [Con A], peanut agglutinin [PNA], glycine max agglutinin [SBA], Phaseolus vulgaris agglutinin, wheat germ agglutinin [WGA, native form], Artocarpus integrifolia agglutinin [Jacalin], and Pisum sativum agglutinin). Control proteins included purified secretory immunoglobulin A (sIgA) from human colostrum, human milk lactoferrin, and chicken-egg lysozyme. All samples were prepared in a denaturing (SDS) buffer under nonreducing and reducing conditions. The sIgA in tears and IgA (alpha) heavy chain fragments (reduced sample) were identified with most of the lectins tested. A particular high molecular weight (greater than 200 kD) protein fraction in tears that just entered the separation gel on SDS-PAGE was detected with WGA and Jacalin. This fraction stain poorly with silver. Tear lactoferrin was identified with all lectins used, although binding was low with SBA. Purified milk lactoferrin showed a poor reaction with Jacalin, but a protein in tears of similar mobility bound this lectin (nonreduced samples). Under both nonreducing and reducing conditions, tear-specific prealbumin in tears did not bind any of the lectins tested. Tear lysozyme only reacted with lectin after reduction. The techniques described may provide additional valuable information in addition to commonly used methods for tear protein analysis and further knowledge concerning the role of glycoproteins on the ocular surface.

Last modified on: 19 March, 2010

 

[Gaby]

Lectins: Their Damaging Role in Intestinal Health, Rheumatoid Arthritis and Weight Loss

By Carolyn Pierini, CLS (ASCP), CNC

http://www.vrp.com/articles.aspx?ProdID=art2009&z

Located on the surface of cells of all living things lay many thousands of different complex sugar molecules (glycoconjugates) projecting outward from their loose anchors like moving antennae. Genetically unique, these molecules comprise a protective coating for the cell and perform many functions including cell recognition and signaling. Lectins are a class of protein molecules capable of using these sugar moieties to bind to the surface of cells. Lectins provide the way for one molecule to stick to another molecule without any immunity involved. Lectins play a wide role in health, but their ability to influence the inflammatory process indicates they are involved in inflammatory bowel disease, rheumatoid arthritis and even weight gain. Lectins’ potential involvement in many aspects of our health caused DJ Freed, MD to state, “Lectins are causes in search of diseases.”

This article will introduce you to the world of lectins, the “sticky proteins” we deal with from day to day in our diets and our bodily systems. Furthermore, you will learn how you can build up your defenses against what could be a hidden cause behind many of our health concerns.

Learning About Lectins

Lectins, not to be confused with the endocrine hormone leptin, are types of proteins commonly found in nature in foods such as fruits, vegetables, and seafood, but especially grains, beans and seeds. They are present in about 30 percent of the American diet and are not degraded by stomach acid or proteolytic enzymes, making them virtually resistant to digestion. Microbes carry lectins and use them for attachment to the host cells. The human body contains lectins: 1) On the vascular endothelial linings (selectins) in order for blood cells to escape into the tissues; 2) In the liver to capture microorganisms, and 3) As opsonins, substances that coat foreign antigens, making them more susceptible to phagocytosis (the process where immune cells digest and destroy foreign invaders) by the white blood cells. C-reactive protein (CRP) and mannose-binding protein (MBP) are two examples of opsonins.

The word “lectin” comes from the Latin phrase, “I choose,” a befitting word choice since lectins are very specific as to what they will bind to. Lectins are also called agglutinins because in their binding to many cell surfaces they cause agglutination (cell clumping) reactions. Ricin, for example, from castor beans is such a potent lectin that just a minute amount is capable of causing death due to massive clotting of red blood cells from agglutination. Ricin even has been used as a murder weapon in espionage.

A lectin serves the plant as a type of primitive protection system analogous to an antibody but in a non-immune model. Likewise, human lectins in our bodies also act protectively but as part of an immune system. Known for a century, lectins form a diverse group of molecules of varying molecular weights and shapes and contain multiple binding sites. The only thing lectins have in common with each other is their ability to bind to sugars. Lectins bind to the terminal sugar, the “glyco,” portion of glycoconjugates found on cell membranes. If the sugars are bound to proteins they are called glycoproteins or bound to fats they are called glycolipids. Collectively they are called glycoconjugates of which 11 percent of the human body is composed.

The important point is that some of the lectins consumed in everyday foods act as chemical messengers that can in fact bind to the sugars of cells in the gut and the blood cells, initiating an inflammatory response. In wheat, gliadin, a component of gluten and an iso-lectin of wheat germ agglutinin (WGA), is capable of activating NF kappa beta proteins which, when up-regulated, are involved in almost every acute and chronic inflammatory disorder including neurodegenerative disease, inflammatory bowel disease, infectious and autoimmune diseases.1 WGA needs more recognition as an important dietary problem. Scientific literature shows that dietary lectins can dramatically reduce natural killer (NK) cell activity directly and through disruption of intestinal flora. Natural killer cells are one of the body’s most important defenses against viruses and other invaders.

Most dietary lectins will also stimulate polyamine production in the gut. Polyamines are important growth factors that may have negative effects if levels become imbalanced. Excess polyamine production initiated by lectins may be the result of an effort to repair the damage to intestinal microvilli caused by lectins. In addition, a high polyamine level may also decrease NK cell populations2, can contribute to halitosis (bad breath), and is considered an important biological marker for colonic precancer. 3-6 A number of animal studies have shown that an increase in polyamines caused by a high lectin diet resulted in increases in the size of the intestines, liver, and pancreas.7

Lectins, Food Allergies and Intestinal Concerns

There is an abundance of literature from the most prestigious journals that lectins such as WGA initiate allergic reactions in the gut causing the release of IL-4, IL-13, and histamine from human basophils producing noticeable allergic symptoms.8-9 WGA has also shown to interfere with protein digestion and increase gut permeability.10-11 Peanut lectin, kidney bean and soybean lectins are other examples of lectins that have influences on bodily tissues. On the bright side, the lectins in broad beans (VFA), jackfruit (JAC), and culinary mushrooms (agraricus bisphorus) have been shown to slow the progression of colon cancer.12-13
Lucretius said, “One man’s food is another man’s poison” and lectins give us part of the reason why. It is our individual genetic inheritances that determine how and to what degree lectins can affect us. Almost everybody has antibodies to some dietary lectins in their bloodstream. Many food allergies are actually immune system reactions to lectins.14

The trend toward consumption of less processed grain foods, although more nutritious in many respects, results in consumption of more lectins. After ingestion, most dietary lectins bind to the absorptive microvilli of the small intestine (the microvilli are the tiny finger-like projections on the epithelial cells). From there lectins may gain access into the blood and lymph system through a process called endocytosis which carries the intact lectin across the microvilli membranes as a vesicle.15 Then, the lectins may enter the liver, pancreas and systemic circulation. It is estimated that about 5 percent of ingested lectins enter the body systemically, where, depending on the lectin and depending on the person’s unique glycoconjugates, lectin binding occurs on other tissues such as nervous and connective tissue and the bladder, which are very sensitive to the agglutinating effects of lectins. It is a clinical observation that the complete avoidance of wheat lectins will help ameliorate the symptoms of interstitial cystitis. The reactions of lectins in the gut are more potent since the gut is more heavily glycosylated (more sugar receptors). As intestinal cells age they become less glycosylated due to the loss of glycoconjugates. The intestinal lining of people with Crohn’s disease and IBS (irritable bowel syndrome) appear to be more sensitive to the effects of food lectins because the lining is constantly being replaced by new tissue that is made up of immature cells that are more glycosylated and thus more susceptible to lectin attachment. It becomes a vicious cycle. Blood group antigens as glycoconjugates are found on the surface of cells lining the digestive tract in addition to the blood cells and are frequently the target of specific lectins resulting in agglutination reactions. The same reactions in vitro are conducted daily in the clinical lab blood bank as “blood typing.”

Lectins have many other applications in the clinical laboratory from identification of microorganisms to cancer research where lectins serve as probes to investigate the working of the cell through its surface biology. Lectins have been used as carriers for the delivery of chemotherapeutic agents. Mitosis (cell division) can be enhanced with lectins such as pokeweed lectin (PWA).

Lectins and Rheumatoid Arthritis

The fact that lectins appear to aggravate existing inflammatory conditions can be seen in the example of rheumatoid arthritis.16-18 The RA antibody is different structurally from a normal antibody in that the side-chain sugar, galactose, is replaced with N-acetyl glucosamine, the sugar for which the wheat germ lectin (WGA) is highly specific. This may point to why patients with rheumatoid arthritis feel better on a wheat-free diet. The defective RA antibody has also been shown to be reactive with the lectin found in the common lentil bean. According to the eminent immunologist David Freed, “Of the various rheumatogenic foods, wheat and other grains top the list. Avoidance of these is frequently the only dietary maneuver required, especially in early cases.” He proposed that ingested wheat lectin (and other dietary lectins) enter the bloodstream from the intestine and bind strongly to connective tissues (which contain considerable quantities of glycoprotein) and skin proteoglycans making them stiff.19 It is a clinical observation that inflammation of the gut is associated with inflammation of the joints. It has been also observed that the pain and inflammation of fibromyalgia may stem from or be contributed to by intolerance to wheat lectins. In fact, lectins are capable of intensifying the effects of autoimmune disorders in general. Nightshade vegetables like potatoes and tomatoes are very high in lectins and are known to trigger the symptoms of arthritis.

Sticky Proteins in Weight Management

A very important and interesting feature of some lectins is their ability to mimic hormones. As one can imagine, this could contribute a significant impact on metabolism. The hormone insulin stores excess carbohydrates (glucose) as fat. It accomplishes this by attaching itself to the insulin receptor found on the fat cell. Under stimulation from insulin, the fat cell becomes more permeable to glucose, which would otherwise remain in circulation. With mission accomplished, the insulin hormone then disconnects to its receptor. In many people, lectins found in lentils, green peas, corn, potatoes but especially wheat germ agglutinin (WGA), are known to bind to the insulin receptor giving the fat cell the same message that insulin gives, namely to make fat. The lectin, however, due to a lack of feedback inhibition, remains indefinitely attached to the receptor giving the cell a constant message to make fat.20-25 This perhaps explains why many weight loss programs that include a moderate-to-high amount of carbohydrate (especially modern grain) fail.

One other point with regard to lectin contribution to weight gain is the fact that lectins have been shown to block digestive hormones. WGA can bind to the receptor for cholecystokinin (CCK), a hormone involved in appetite control, suppressing its function.26-27 This essentially leads to an increase in appetite and impairment in the release of digestive enzymes.

Detrimental Dietary Component

Consider the fact that there are many varieties of wheat grown worldwide. Ancient wheat species had much lower protein contents than the modern varieties. Lectins are proteins. Increasing the protein component has also increased the lectin load with the resultant potential for inflammation and metabolic disruption. Genetic altering of grain plants (GMO) has also changed the lectin content.

Interestingly, lectins are destroyed in the sprouting process, which allows for a safer form of grain consumption, not to mention that the sprout is generally higher in overall nutritional value than the seed. Organic, sprouted grain bread products (with no added gluten) appear to be the safest and healthiest way to reap the nutritional benefit of grain without the lectin burdens.

Some lectins are resistant to heating by cooking. As a side note, soaking beans before cooking them reduces the lectin content dramatically. Most people do not know why beans prepared this way makes them easier to digest but it is simply because the water-soluble lectins have been nearly completely removed through the changing of the water during soaking.

Protecting Against Lectins

Because lectins are so prevalent in a typical diet, undertaking a supplement regimen to help combat the damaging effects of lectins can help contribute to optimal health, improve the health of the intestinal tract and contribute to weight loss. Certain seaweeds, especially those high in the sugar fucose (Bladderwrack) and mucilaginous vegetables like okra have the ability to bind to lectins in a way that makes them unavailable to the vulnerable cells of the gut. These foods act as sacrificial decoys and attach to the problematic lectins that would ordinarily attach and bind to gut epithelial cells. A specific glycoprotein, N-acetylglucosamine (NAG), is also a favorite target for dietary lectins and is concentrated in connective tissue. Supplementation with NAG is an excellent strategy for lectin protection. Another sugar with similar activity is D-mannose, which is capable of binding to lectins located on the cells of microorganisms. Some bacteria responsible for urinary tract infections contain lectins specific for the sugar mannose and use these lectins to bind tightly to mannose-rich tissue in the bladder walls, initiating urinary tract infections (UTIs). 28 As with Bladderwrack and NAG, supplementation with D-mannose provides a decoy for these lectins and protects the bladder. Supplementing prior to a meal with these decoy sugars allows for the binding of potentially harmful lectins and protection from attack. This concept of lectin-shielding devices has exciting clinical application now and in the future.29

Conclusion

The subject of lectins is very broad and deserves more discussion. There are even some lectins that are beneficial to the body, such as those found in some species of edible snails, which may be capable of preventing the metastasis of cancer cells. 30 The involvement of lectins in our health and their relationship to degenerative disease is still an emerging science. Studies performed on animals will continue to be the model in the future for the study of lectins. The glycosylation of the human gut is basically similar to that of higher animals and it may be confidently predicted that the effects of dietary lectins will have similarities in both humans and animals. In short, dietary lectins, by their chemical reactivity with cell surface receptors on the intestinal epithelium, are metabolic signals for the gut and are capable of modulating immune and hormone functions.14

References

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3. Chamaillard L, Quemener V, Havouis R, Moulinoux JP. Polyamine deprivation stimulates natural killer cell activity in cancerous mice. Anticancer Res. 1993 Jul-Aug; 13(4):1027-33, Jun; 115(6):600-2.
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10. Falth-Magnusson K., et al. Elevated levels of serum antibodies to the lectin wheat germ agglutinin in celiac children lend support to the gluten-lectin theory of celiac disease. Pediatr Allergy Immunol. May 1995; 6(2): 98-102.
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[LQB]

Great info Psyche - Thanks Very Much for this!

Sounds like Ultra/elimination diet testing is very important for routing out the personal sensitivities. What I also got out of this is:
1) the possible importance of diet diversity to reduce lectin impact
2) possible usefulness of traditional preps - soaking, sprouting, fermenting, etc
3) possible food/meal combining to lessen lectin impact
4) possibly moving more in the direction of high protien/low carb

 

[Mikey]

On page 103 of the Book The Ultra Simple Diet, Dr. Hyman adds to the UltraBroth recipe:

Cool, strain (throw out the cooked vegetables), and store in a large, tightly sealed glass container in the fridge.

[...]

When you are done making the broth, you may discard the vegetables as they are not intended to be eaten (but make sure you keep the broth!).

I would like to keep the vegetables, since throwing them away would be a waste and they still taste good and make a good snack.

Does anything speak against that?

Maybe Dr. Hyman wrote this because he didn't want to ask from his audience to eat overcooked vegetables?

 

[3DStudent]

Data, I remember Laura or Psyche saying that they sometimes eat the vegetables used to make the broth. But I cannot find that post. I think it would be a waste too, or you could compost it. FWIW