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Lectin report end

SO WHAT DOES THIS ALL MEAN TO ME AND WHAT DO 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. 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. 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, adult onset diabetes, and even obesity.. 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. WHERE CAN I GET HELP IN DETERMINING MY INTOLERANCE OR HELP WITH DIET TO TEST OR MAINTAIN?Books mentioned at the beginning of this report by Atkins, Eades, Audette, or Hunt 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 or Hunt's recipes use any major lectin groups. They do have some recipes with nightshades. Watch out for those recipes if you think it is a group you react to. Please note that not everyone will need to eliminate every major lectin group. You have to experiment and see 'who' you are and 'what' your ideal foods are. It is a process. Fallon and Enig's Nourishing Traditions is still a great cookbook just watch out for the lectin containing foods in recipes and avoid them. 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 would like more information or research citations in this area they are available. I can be reached at 1- or send me an e-mail Please note: The following article explains some of the concepts current in lectinology. This article also mentions animal lectins which are not at this time considered to be potential toxins for humans. We are concerned with the more commonly known and studied toxic plant lectins as listed above. Introduction to "Lectin" Jun Hirabayashi (Teikyo University Faculty of Pharmaceutical Sciences) 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;son 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):3277-84 Identification 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.