BT004O

Deflect® O


TAGS:    ANTI-INFLAMMATORY    |   DIGESTION    |   MICROBIOME SUPPORT    |   WEIGHT MANAGEMENT

ABO-Specific Lectin Blocker

INTRODUCTION

Deflect dietary supplements are designed by the distinguished naturopath Dr. Peter D’Adamo, author of the best-selling book Eat Right 4 Your Type. Deflect products provide anti-adhesive therapy to lectin sensitive individuals. These ABO specific formulas block the effects of dietary lectins before they cause damage, by providing a source of free blocking carbohydrate. Since each blood type is susceptible to lectins with different carbohydrate specificities, we’ve designed formulas that block lectins by using mono and polysaccharides specific for each blood type. Deflect products are also an excellent source of soluble and insoluble fiber for that particular blood type.


DESCRIPTION/ BACKGROUND

Deflect™ products provide anti-adhesive therapy to lectin sensitive individuals. These ABO specific formulas block the effects of dietary lectins before they cause problems, by providing a source of free blocking carbohydrate. Deflect is a natural product composed of ‘blocking sugars’ designed to interfere with the adherence of troublesome dietary lectins. Since many lectins are ABO blood type specific, there are 4 different Deflect formulas: one for each blood type. The blocking sugars in Deflect can be considered ‘sacrificial molecules’ that attach to carbohydrate receptors on the lectins, rendering them unable to bind to the cells of the body.

According to an old definition ‘lectins are carbohydrate-binding proteins or glycoproteins.’ William Boyd therefore coined the term lectin in 1954, deriving it from the Latin word legere meaning ‘to choose.’ Boyd was also the first researcher to identify the blood type specificity of many common dietary lectins.

 

Highlights of the Deflect O formula include:

N-Acetyl-Glucosamine (NAG).  Lectins found in foods, in particular wheat and other grains have a particular structure that allows them to have a high affinity for glucosamine, NAG and its polymers. By introducing NAG in Deflect O, these lectins will be distracted and bind to the Deflect O rather than systemic NAG. This may explain the benefits seen with diet-responsive rheumatoid arthritis . (1, 2)

Bladderwrack (Fucus vesiculosus).  The mechanism behind Fucus is suspected to be from the unique structure of the sugar polymers. Interestingly blood type O antigen is characterized by a terminal fucose. The fucoidan found in bladderwrack inhibits the growth of many unfriendly bacteria and viruses. Some of the viruses this compound is antagonistic to include herpes simplex virus, human cytomegalovirus, and human immunodeficiency virus. Bladderwrack has been found to agglutinate the cells of several strains of Candida. Bladderwrack also has a toxic effect on some strains of E. coli and all strains tested of Neisseria meningitidis. Therefore, providing Fucus in Deflect O will act to bind to these foreigners rather than to the intestinal tract. (3-7)

 

Lectins

Typically, lectins can bind to many of the carbohydrate antigens found in the gut and immune system, causing a variety of health problems. These can include intestinal dysbiosis, intestinal permeability, immune dysfunction, food sensitivities and systemic inflammation. This is usually accomplished by direct agglutination of the target cells. However more recent evidence has suggested several other mechanisms as by which lectins may disrupt health. Specific lectins may disrupt the actual integrity of the intestinal barrier, and recent work on zonulin has shown we can now measure intestinal permeability. (15) Intestinal epithelial cells have receptors specific to certain lectins, when these lectins come in contact with these receptors they can disrupt the protective barrier and allow these macromolecules to enter the blood stream exciting an immune response. (16) Once the lectins, or glycoproteins, enter the blood stream they can bind to various tissues which then causes the body to attack that body tissue as non-self. Therefore, not only do these lectins elicit a weakening of the intestinal barrier, which alone increases susceptibility to illness, but the immune system is then exposed to foreign antigens resulting in inflammation and a dysfunctional cellular membrane. (17)

Lectins can occur in very common foods in the diet, and the majority is specific for the carbohydrates of the ABO blood typing system. In one study, the edible parts of 29 of 88 foods tested, including common salad ingredients, fresh fruits, roasted nuts, and processed cereals were found to possess significant lectin-like activity as assessed by hemagglutination and bacterial agglutination assays.

Several common lectins, in particular, wheat germ agglutinin, are known to bind to insulin receptors and mimic the hormonal effects of insulin on adipose tissue, an under-appreciated action which can account for why individuals on high carbohydrate diets often have difficulty controlling their weight (18-23). Soybean agglutinin as well has been shown to increase body weight and organ fat deposition, independent of insulin suggesting the agglutinating impact of lectins may go beyond insulin dysregulation. (24, 25) Thus, lectin blocking is a safe and rational method for enhancing weight loss.

In the words of one lectin researcher:

“Most lectins in our diet are resistant to breakdown during gut passage and are bound and endocytosed by epithelial cells. These lectins are powerful exogenous growth factors for the small intestine, can induce dramatic shifts in its bacterial flora and interfere with its hormone secretion. In addition, lectins that are transported across the gut wall into the systemic circulation can modulate the body’s hormone balance, metabolism and health. Although these physiological effects are mediated or reinforced by immune responses, they are primarily the result of the specific chemical reactivity of lectins with cell surface receptors of the gut.”



AGENT/ INGREDIENT ROLE
N-acetylcysteine (NAC)
Bladderwrack (Fucus versiculosus)
n-acetyl glucosamine (NAG)
Larch arabinogalactan

TABLE 1: Key agents in Deflect® O.

ACTIONS/ INDICATIONS

The Deflect formulas provide a source of free blocking amino acid sugars (blue) which bind and block lectins before they can attach to the cells. Since each blood type is susceptible to lectins with different carbohydrate specificities, Dr. D’Adamo designed formulas to block lectins by using mono and polysaccharides specific for each blood type.

The amino sugars in Deflect encourage healthy bowel flora, although they do not provide a source of flora themselves. These same amino sugars are healthy enhancers of joint gliding surface and synovia as well.

Situations where Deflect products may be indicated include:

  • Carbohydrate intolerant individuals who typically gain weight on high carbohydrate diets
  • ‘Leaky Gut’ and intestinal dysbiosis
  • Food sensitivities
  • Individuals with a low inflammatory threshold

 

One way this repair mechanism works is by ‘prying off’ lectins which have already adhered to cellular receptors, such as insulin. Since insulin blockage by dietary lectins has been linked to both insulin resistance and obesity, using Deflect can help accelerate weight reduction in diet-compliant individuals by speeding up the time it takes for the regeneration of new insulin receptors or the ‘cleansing’ of the old ones. This can take upwards of one year in some individuals who just follow the diet, and explains why some dieters do not see weight loss in the early stages of the program. It is because of this ‘lectin-locking’ function that many other diets (which do have accelerated weight loss in their early stages) cause their followers to lose muscle mass and fat -when what we want is to lose only the fat. If the weight loss in ER4YT is occasionally slow, at least it is healthy: Losing only body fat means that that a person’s weight loss can sometimes be only 50% as rapid as other programs which are destroying muscle and fat. The problem is that muscle is hard to get back, and any drop in muscle mass results in a lower metabolic rate, leaving the dieter more likely to gain back the weight, but this time only in body fat.

Many lectins can amplify the effects of auto-immune disease, such as thyroiditis, rheumatoid arthritis, scleroderma, fibromyalgia and pemphigus. Research shows that some of the lectins that can cause this may actually be manufactured by the body itself (serum lectins). Lectins may actually change the function and structure of lymphocytes stimulating molecular-mimicry, where the immune system will cross-react foreign lectins with particular tissue antigens, such as those of the joints, thyroid, intestinal tract, kidneys, etc. (19) By acting as sacrificial molecules, Deflect can block this action.

Many people with ‘food sensitivities’ or ‘leaky gut’ have a phenomenon called ‘active endocytosis’ where prior lectin damage results in an intestinal absorption surface that actively scoops up macromolecules. Because these larger molecules are very antigenic, then tend to increase local inflammation and thus increase the leaky gut. This may be further potentiated by any intestinal dysbiosis, where bacterial lipopolysaccharides and toxins can incite an immune response and inflammation. (26-28) By acting like ‘sacrificial molecules’ Deflect can block this, while also inhibiting bacterial adhesion to the gut as well (bacteria use their own lectins to attach to the intestines) a secondary cause of leaky gut. The amino sugars in Deflect can also help prevent re-infection by H. pylori and many gram-negative bacteria which cause bladder infections, by flooding their own lectin receptors, thereby preventing adhesion, the first step needed for infection.


TYPICAL DOSAGE

2 capsules, 2-3 times daily with meals.

PRODUCT HISTORY

This product was introduced by NAP in 2000 after first being specifically designed for use in the D’Adamo clinic.

REFERENCES

  1. Freed DJ Dietary Lectins in Food Allergy and Intolerance Brostoff and Callacombe Editors Bailliere Tindall Publishers, London
  2. Pusztai A, Ewen SW, Grant G, Brown DS, Stewart JC, Peumans WJ, Van Damme EJ, Bardocz S Antinutritive effects of wheat- germ agglutinin and other N-acetylglucosamine-specific lectins. Br J Nutr 1993 Jul;70(1):313-21.
  3. Zapopozhets TS, Besednova NN, Loenko IuN. Antibacterial and immunomodulating activity of fucoidan. Antibiot Khimioter 1995;40:9-13. [Article in Russian]
  4. Baba M, Snoeck R, Pauwels R, de Clercq E. Sulfated polysaccharides are potent and selective inhibitors of various enveloped viruses, including herpes simplex virus, cytomegalovirus, vesicular stomatitis virus, and human immunodeficiency virus. Antimicrob Agents Chemother 1988;32:1742-1745.
  5. Criado MT, Ferreiros CM. Selective interaction of a Fucus vesiculosus lectin-like mucopolysaccharide with several Candida species. Ann Microbiol (Paris) 1983;134A:149-154.
  6. Criado MT, Ferreiros CM. Toxicity of an algal mucopolysaccharide for Escherichia coli and Neisseria meningitidis strains. Rev Esp Fisiol 1984;40:227-230.
  7. Zapopozhets TS, Besednova NN, Loenko IuN. Antibacterial and immunomodulating activity of fucoidan. Antibiot Khimioter 1995;40:9-13.
  8. Knudson, W., Gundlach, M. W., Schmid, T. M., & Conrad, H. E. (1984). Selective hydrolysis of chondroitin sulfates by hyaluronidase. Biochemistry, 23(2), 368–75.
  9. Domenici, L., Monti, M., Bracchi, C., Giorgini, M., Colagiovanni, V., Muzii, L., & Benedetti Panici, P. (2016). D-mannose: a promising support for acute urinary tract infections in women. A pilot study. European Review for Medical and Pharmacological Sciences, 20(13), 2920–5.
  10. Sharon, N., Eshdat, Y., Silverblatt, F. J., & Ofek, I. (1981). Bacterial adherence to cell surface sugars. Ciba Foundation Symposium, 80, 119–41.
  11. Howell, A. B., Reed, J. D., Krueger, C. G., Winterbottom, R., Cunningham, D. G., & Leahy, M. (2005). A-type cranberry proanthocyanidins and uropathogenic bacterial anti-adhesion activity. Phytochemistry, 66(18), 2281–2291.
  12. Lu, Y., Zhang, M., Zhao, P., Jia, M., Liu, B., Jia, Q., … Li, J. (2017). Modified citrus pectin inhibits galectin-3 function to reduce atherosclerotic lesions in apoE-deficient mice. Molecular Medicine Reports, 16(1), 647–653.
  13. Svensson, S et al. Arabinogalactans, their preparation and compositions using same. European Patent Application Pub # 0138784 A2. European Patent Office. Filing Date: 8/20/84
  14. Adams MF and Ettling BV. Industrial Gums, 2nd Edition: 1973, Academic Press
  15. Fasano, A. (2012). Zonulin, regulation of tight junctions, and autoimmune diseases. Annals of the New York Academy of Sciences, 1258(1), 25–33. https://doi.org/10.1111/j.1749-6632.2012.06538.x
  16. Pérez-Maceda, B., López-Bote, J. P., Langa, C., & Bernabeu, C. (1991). Antibodies to dietary antigens in rheumatoid arthritis--possible molecular mimicry mechanism. Clinica Chimica Acta; International Journal of Clinical Chemistry, 203(2–3), 153–65.
  17. Miyake, K., Tanaka, T., & McNeil, P. L. (2007). Lectin-based food poisoning: a new mechanism of protein toxicity. PloS One, 2(8), e687. https://doi.org/10.1371/journal.pone.0000687
  18. Ruhlmann J, Sinha P, Hansen G, Tauber R, Kottgen E Studies on the aetiology of coeliac disease: no evidence for lectin-like componentsn wheat gluten. Biochim Biophys Acta 1993 Jun 19;1181(3):249-56
  19. Freed DJ Dietary Lectins in Food Allergy and Intolerance Brostoff and Callacombe Editors Bailliere Tindall Publishers, London
  20. Gendel, Steven M. (1998) Sequence Databases for Assessing the Potential Allergenicity of Proteins Used in Transgenic Foods. Advances in Food and Nutrition Research 42; 63-92.
  21. Forssell F, Wieser H [Spelt wheat and celiac disease]. Z Lebensm Unters Forsch 1995 Jul;201(1):35-9
  22. 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. 1995 May;6 (2):98-102.
  23. Brady PG, Vannier AM, Banwell JG Identification of the dietary lectin, wheat germ agglutinin, in human intestinal contents. Gastroenterology 1978 Aug;75(2):236-9
  24. Zang, J., Li, D., Piao, X., & Tang, S. (2006). Effects of soybean agglutinin on body composition and organ weights in rats. Archives of Animal Nutrition, 60(3), 245–253.
  25. Thevaranjan N, Puchta A, Schulz C, et al. Age-Associated Microbial Dysbiosis Promotes Intestinal Permeability, Systemic Inflammation, and Macrophage Dysfunction. Cell Host Microbe. 2017;21(4):455-466.Zang J, Li D, Piao X, Tang S. Effects of soybean agglutinin on body composition and organ weights in rats. Arch Anim Nutr. 2006; 60(3): 245-253
  26. Cordain, L., Toohey, L., Smith, M. J., & Hickey, M. S. (2000). Modulation of immune function by dietary lectins in rheumatoid arthritis. The British Journal of Nutrition, 83(3), 207–17.
  27. Thevaranjan, N., Puchta, A., Schulz, C., Naidoo, A., Szamosi, J. C., Verschoor, C. P., … Bowdish, D. M. E. (2017). Age-Associated Microbial Dysbiosis Promotes Intestinal Permeability, Systemic Inflammation, and Macrophage Dysfunction. Cell Host & Microbe, 21(4), 455–466.e4.
  28. Additional Resources and References (not cited)
  29. Freed DJ. British Medical Journal, 1999 Apr 17;318(7190):1023-4.
  30. Pusztai A. Dietary lectins are metabolic signals for the gut and modulate immune and hormone functions. Eur J Clin Nutr 1993 Oct;47(10):691-9
  31. Irache JM, Durrer C, Duchene D, Ponchel Bioadhesion of lectin-latex conjugates to rat intestinal mucosa. Pharm Res 1996 Nov;13(11):1716-9
  32. Acarin L, Vela JM, Gonzalez B, Castellano B Demonstration of poly-N-acetyl lactosamine residues in ameboid and ramified microglial cells in rat brain by tomato lectin binding. J Histochem Cytochem 1994 Aug;42(8):1033-41
  33. Hussain N, Jani PU, Florence AT Enhanced oral uptake of tomato lectin conjugated nanoparticles in the rat. Pharm Res 1997 May;14(5):613-8
  34. Chuang JS, Callaghan JM, Gleeson PA, Toh BH Diagnostic ELISA for parietal cell autoantibody using tomato lectin-purified gastric H+/K(+)-ATPase (proton pump). Autoimmunity 1992;12(1):1-7
  35. Tariq SM, Stevens M, Matthews S, Ridout S, Twiselton R, Hide DW Cohort study of peanut and tree nut sensitisation by age of 4 years. BMJ 1996 Aug 31;313(7056):514-7
  36. Gan RL[Peanut lectin-binding sites in gastric carcinoma and the adjacent mucosa]. Chung-hua Ping Li Hsueh Tsa Chih 1990 Jun;19(2):109-11
  37. Lin M, et al Peanut lectin-binding sites and mucins in benign and malignant colorectal tissues associated with schistomatosis. Histol Histopathol. 1998 Oct;13(4):961-6.
  38. Melato M, et al The lectin-binding sites for peanut agglutinin in invasive breast ductal carcinomas and their metastasis. Pathol Res Pract. 1998;194(9):603-8.
  39. Jordinson M, Playford RJ, Calam Effects of a panel of dietary lectins on cholecystokinin release in rats. Am J Physiol 1997 Oct;273(4 Pt 1):G946-50
  40. Jordinson M, et al Soybean lectin stimulates pancreatic exocrine secretion via CCK-A receptors in rats Am J Physiol. 1996 Apr;270(4 Pt 1):G653-9.
  41. Mikkat U, Damm I, Schroder G, Schmidt K, Wirth C, Weber H, Jonas L Effect of the lectins wheat germ agglutinin (WGA) and Ulex europaeus agglutinin
  42. (UEA-I) on the alpha-amylase secretion of rat pancreas in vitro and in vivo. Pancreas 1998 May;16(4):529-38
  43. Burks AW, et al Identification of peanut agglutinin and soybean trypsin inhibitor as minor legume allergens. Int Arch Allergy Immunol. 1994 Oct;105(2):143-9.
  44. Buchanan and Higley : The relationship of blood groups to disease. Br. J. Exp. Path. (1921) 2;227
  45. Springer GF. Relation of blood group active plant substances to human blood groups. Acta Haem. 20 (1958) 147-55
  46. Alderman S, Kailas S, Goldfarb S, Cholestatic hepatitis after ingestion of chaparral leaf: confirmation by endoscopic retrograde cholangiopancreatography and liver biopsy. Clin Gastroenterol 1994 Oct;19(3):242-7
  47. Okada Y, Jinno K, Moriwaki S, Shimoe T, Tsuji T, Murakami M, Thurin J, Koprowski H Blood group antigens in the intrahe- patic biliary tree. I. Distribution in the normal liver. J Hepatol 1988 Feb;6(1):63-7
  48. Jordinson M, Playford RJ, Cala Am J Physiol Effects of a panel of dietary lectins on cholecystokinin release in rats 1997 Oct;273(4 Pt 1):G946-50
  49. Pusztai A Dietary lectins are metabolic signals for the gut and modulate immune and hormone functions. Eur J Clin Nutr. 1993 Oct;47(10):691-9. Review
  50. Ruhlmann J, Sinha P, Hansen G, Tauber R, Kottgen E Studies on the aetiology of coeliac disease: no evidence for lectin-like componentsn wheat gluten. Biochim Biophys Acta 1993 Jun 19;1181(3):249-56
  51. Freed DJ Dietary Lectins in Food Allergy and Intolerance Brostoff and Callacombe Editors Bailliere Tindall Publishers, London
  52. Gendel, Steven M. (1998) Sequence Databases for Assessing the Potential Allergenicity of Proteins Used in Transgenic Foods. Advances in Food and Nutrition Research 42; 63-92.
  53. Forssell F, Wieser H [Spelt wheat and celiac disease]. Z Lebensm Unters Forsch 1995 Jul;201(1):35-9
  54. 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. 1995 May;6 (2):98-102.
  55. Brady PG, Vannier AM, Banwell JG Identification of the dietary lectin, wheat germ agglutinin, in human intestinal contents. Gastroenterology 1978 Aug;75(2):236-9
  56. Pusztai A, Ewen SW, Grant G, Brown DS, Stewart JC, Peumans WJ, Van Damme EJ, Bardocz S Antinutritive effects of wheat- germ agglutinin and other N-acetylglucosamine-specific lectins. Br J Nutr 1993 Jul;70(1):313-21
  57. Deschodt-Lanckman M, Robberecht P, Camus JC, Christophe J Wheat germ agglutinin inhibits basal- and stimulated-adenyl- ate cyclase activity as well as the binding of [3H] caerulein to rat pancreatic plasma membranes J Cyclic Nucleotide Res 1977 Jun;3(3):177-87
  58. Ponzio G, Debant A, Contreres JO, Rossi B Wheat-germ agglutinin mimics metabolic effects of insulin without increasing receptor autophosphorylation Cell Signal 1990;2(4):377-86
  59. Wu AM, Wu JH, Song SC, Tsai MS, Herp A. Studies on the binding of wheat germ agglutinin (Triticum vulgaris) to O-glycans. FEBS Lett 1998 Dec 4;440(3):315-9
  60. Kitano N, Taminato T, Ida T, Seno M, Seino Y, Matsukura S, Kuno S, Imura H Detection of antibodies against wheat germ agglutinin bound glycoproteins on the islet-cell membrane. Diabet Med 1988 Mar;5(2):139-44 Intern Med 1986 Dec;105(6):883-
  61. Hollander D, Vadheim CM, Brettholz E, Petersen GM, Delahunty T, Rotter JI Increased intestinal permeability in patients with Crohn’s disease and their relatives. A possible etiologic factor. Ann Intern Med 1986 Dec;105(6):883-5
  62. Nachbar MS, Oppenheim JD Lectins in the United States diet: a survey of lectins in commonly consumed foods and a review of the literature. (SV)Am J Clin Nutr 1980 Nov;33(11):2338-45 Prog Food Nutr Sci 1989;13(3-4):317-48
  63. Erickson RH, Kim J, Sleisenger MH, Kim YS Effect of lectins on the activity of brush border membrane-bound enzymes of rat small intestine. J Pediatr Gastroenterol Nutr 1985 Dec;4(6):984-91
  64. Weinman MD, Allan CH, Trier JS, Hagen SJ Repair of microvilli in the rat small intestine after damage with lectins contained in the red kidney bean. Gastroenterology 1989 Nov;97(5):1193-204
  65. Greer F, Pusztai A Toxicity of kidney bean (Phaseolus vulgaris) in rats: changes in intestinal permeability. Digestion 1985;32(1):42-6
  66. Grant G Anti-nutritional effects of soyabean: a review. J Anim Sci 1982 Nov;55(5):1087-98
  67. Aletor VA Effect of dietary sub-lethal doses of lima bean lectin on relative organ weights, pancreatic and intestinal trypsin (EC 3.4.21.4) and chymotrypsin (EC 3.4.21.1) in the rat. Nahrung 1989;33(4):355-60
  68. Toro F, Benshimol AL, Gonzalez Elorriaga M, Soyano A Spleen and thymus histology and proliferative response of splenic cells in rats fed raw and cooked Phaseolus vulgaris beans. (SJ)Arch Latinoam Nutr 1992 Dec;42(4):395-402
  69. Henney L, Ahmed EM, George DE, Kao KJ, Sitren HS Tolerance to long-term feeding of isolated peanut lectin in the rat: evidence for a trophic effect on the small intestines J Nutr Sci Vitaminol (Tokyo) 1990 Dec;36(6):599-607
  70. Myer RO, Froseth JA, Coon CN Protein utilization and toxic effects of raw beans (Phaseolus vulgaris) for young pigs. J Anim Sci. 1982 Nov;55(5):1087-98.
  71. Grant G, More LJ, McKenzie NH, Stewart JC, Pusztai A A survey of the nutritional and haemagglutination properties of legume seeds generally available in the UK. Br J Nutr 1983 Sep;50(2):207-14
  72. Chiba M, et al Anti-erythrocyte antibodies in ulcerative colitis: case report and discussion on the pathophysiology of anti-eryth- rocyte antibody. Gastroenterol Jpn. 1988 Oct;23(5):564-9.
  73. Vesely KT. Frequency of blood groups of the ABC and Rho(D) system in patients with viral hepatitis,
  74. Springer GF Importance of blood-group substances in interactions between man and microbes. Ann NY Acad Sci. 1970 Feb 13;169(1):134-52.
  75. Variyam EP, Hoskins LC Mucin degradation in human colon ecosystems. Degradation of hog gastric mucin by fecal extracts and fecal cultures. Gastroenterology 1981 Oct;81(4):751-8
  76. Springer GF. Role of human cell surface structures in interactions between man and microbes. Naturwissenschaften. 1970 Apr;57(4):162-71.
  77. Yang N, Boettcher B Development of human ABO blood group A antigen on Escherichia coli Y1089 and Y1090. Immunol Cell Biol 1992 Dec;70 ( Pt 6):411-6
  78. Lindstedt R, Larson G, Falk P, Jodal U, Leffler H, Svanborg C The receptor repertoire defines the host range for attaching Esch- erichia coli strains that recognize globo-A. Infect Immun 1991 Mar;59(3):1086-92
  79. Essery SD, et al Detection of microbial surface antigens that bind Lewis(a) antigen. FEMS Immunol Med Microbiol. 1994 Jun;9(1):15-21.
  80. Tosh FD, et al Characterization of a fucoside-binding adhesin of Candida albicans. Infect Immun. 1992 nov;60(11):4734-9.
  81. Osipova SO, et al [The ABO system and Lamblia infection. 2. The secretion of ABO system antigens and level of the specific humoral response in persons with Lamblia infection and the presence of group-specific antigens in Lamblia].
  82. Med Parazitol (Mosk). 1985 Nov-Dec;(6):16-9. Russian.
  83. Jordinson M, et al Vicia faba agglutinin, the lectin present in broad beans, stimulates differentiation of undifferentiated colon cancer cells. Gut. 1999 May;44(5):709-714.
  84. Itzkowitz SH Blood group-related carbohydrate antigen expression in malignant and premalignant colonic neoplasms. J Cell Biochem Suppl 1992;16G:97-101
  85. Denk H, Holzner JH, Obiditsch-MayrEpithelial blood group antigens in colon polyps. I. Morphologic distribution and rela- tionship to differentiation. J Natl Cancer Inst 1975 Jun;54(6):1313-7
  86. Li R, et al [Subcellular localization of blood group substances ABH in human gastrointestinal tracts]. Chung KuoHsueh Ko Hsueh Yuan Hsueh Pao. 1996 Feb;18(1):49-53. Chinese.
  87. Itzkowitz SH, Dahiya R, Byrd JC, Kim YS Blood group antigen synthesis and degradation in normal and cancerous colonic tissues. Gastroenterology 1990 Aug;99(2):431-42
  88. Vowden P, Lowe AD, Lennox ES, Bleehen NM Thyroid blood group isoantigen expression: a parallel with ABH isoantigen expression in the distal colon. Br J Cancer 1986 Jun;53(6):721-5
  89. Schumacher U, Higgs D, Loizidou M, Pickering R, Leathem A, TaylorCancer 1994 Dec 15;74(12):3104-3107 Helix pomatia agglutinin binding is a useful prognostic indicator in colorectal carcinoma.
  90. Campbell BJ, et al Direct demonstration of increased expression of Thomsen-Friedenreich (TF antigen in colonic adenocarci- noma and ulcerative colitis mucin and its concealment in normal mucin. J Clin Invest. 1995 Feb;95(2):571-6.
  91. Datta PK, et al Enhancement of lectin-erythrocyte agglutination by gums. Biochim Biophys Acta. 1988 Nov 2;957(1):164-7.
  92. Melito C, et al Vegetable gums modify lectin hemagglutinability. Acta Cient Venez. 1992;43(5):312-4.
  93. Clausen H, et al . Monoclonal antibodies directed to the blood group A associated structure, galactosyl-A: specificity and rela- tion to the Thomsen- Friedenreich antigen. Mol Immunol. 1988 Feb;25(2):199-204.
  94. Wu AM, et al Binding studies on the combining site of a GalNAc alpha 1-->-specific lectin with Thomsen-Friedenreich activity prepared from green marine algae Codium fragile subspecies tomentosoides.
  95. Murayama T, et al. Colon carcinoma glycoproteins carrying alpha 2,6-linked sialic acid reactive with Sambucus nigra agglutinin are not constitutively expressed in normal human colon mucosa and are distinct from sialyl-Tn antigen. Int J Cancer. 1997 Mar 4;70(5):575-81.
  96. Boland CR, et al Use of the lectin from Amaranthus caudatus as a histochemical probe of proliferating colonic epithelial cells Cancer Res. 1991 Jan 15;51(2):657-65.
  97. Poola I, et al. Purification and saccharide-binding charcteristics of a rice lectin. Carbohydr Re. 1986 Feb 1;146(2):205-217
  98. Springer GF. Relation of blood group active plant substances to human blood groups. Acta Haem. 20 (1958) 147-55
  99. Freed DL, et al Letter: Do dietary lectins protect against colonic cancer? Lancet. 1975 Dec 20;2(7947):1261-2.
  100. Bardocz S, et al. Reversible effect of phytohaemagglutinin on the growth and metabolism of rat gastrointestinal tract. Gut. 1995 Sep;37(3):353-60.
  101. Pusztai, A. (1995) Proc. Int. Symp. Control. Rel. Bioact. Mater. 22, 161-162
  102. Tchernychev B, et al Natural human antibodies to dietary lectins. FEBS Lett. 1996 Nov 18;397(2-3):139-42.
  103. Seaweeds and Their Uses (Levring, Hoppe and Schmid, 1969) by V.J. Chapman (Professor of Botany, Auckland University) 1970.
  104. Fasano A. Zonulin, regulation of tight junctions, and autoimmune diseases. Ann N Y Acad Sci. 2012;1258(1):25-33.
  105. Hamid R, Masood A. Dietary Lectins as Disease Causing Toxicants. Pakistan J Nutr. 2009;8(3):293-303.
  106. Miyake K, Tanaka T, McNeil PL. Lectin-based food poisoning: a new mechanism of protein toxicity. PLoS One. 2007;2(8):e687.
  107. Pérez-Maceda B, López-Bote JP, Langa C, Bernabeu C. Antibodies to dietary antigens in rheumatoid arthritis--possible molecular mimicry mechanism. Clin Chim Acta. 1991;203(2-3):153-165.
  108. Cordain L, Toohey L, Smith MJ, Hickey MS. Modulation of immune function by dietary lectins in rheumatoid arthritis. Br J Nutr. 2000;83(3):207-217.



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