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Krispin Sullivan, CN 01/17/15
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 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. Newer books include the Paleo and Caveman Diest and later versions of Low Carbohydrate diets. 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
Higher protein has been shown clinically to improve many of these conditions but not all and it is not a wide enough connecting link. Lowering of fasting insulin explains some but not all connections.
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
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, malt vinegars), peanut butter, cereal, or legume oils (soy, canola, corn), additives, thickeners and products containing malt vinegar, as well as beers and ales. Grape based alcoholic beverages and DISTILLED grain based alcohols are 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.High degree of resistance to gut proteolysis.Binding to brush border cells; damage to microvillus membrane; shedding of cells; reduction in the absorptive capacity of the small intestine.Increased endocytosis; induction of hyperplastic growth of the small intestine; increased turnover of epithelial cells.Interference with the immune system; hypersensitivity reactions. Interference with the microbial ecology of the gut; selective overgrowth.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.
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, malt 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-
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.
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.
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.
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 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.
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
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: 17 January, 2015
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