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Found 37 results

  1. Celiac.com 03/27/2017 - A number of researchers are looking to provide alternative or adjunct treatments to the gluten-free diet in celiac disease. Meanwhile, a number of companies are currently developing a wide variety of such options, ranging from various kinds of enzyme therapies, to treatments that eliminate celiac disease reactions, even to vaccines to inoculate celiac sufferers against their condition, perhaps allowing for full recovery and a return to non-gluten-free eating habits, as desired. At least, that's one dream. More likely will be the development of enzymes or other treatments that offer celiacs varying degrees of protection from gluten ingestion. Most likely, such treatments would be designed to augment an existing gluten-free diet, and to provide protection against moderate gluten-contamination when eating out. One particular enzyme that shows strong potential in breaking down toxic peptides in A-gliadin, the main culprit in celiac reactions, is caricain. A recent paper discusses the scientific principles behind the use of caricain for enzyme therapy. The paper is based on a recent study, in which a team of researchers set out to review the structures of the toxic peptides in A-gliadin for key sequences of amino acids or motifs related to toxicity, especially with respect to digestive difficulties, or immunogenicity. The research team included Hugh J. Cornell and Teodor Stelmasiak. They are affiliated with the RMIT University, School of Applied Sciences, Melbourne, Australia, and with Glutagen Pty Ltd, Maribyrnong, Victoria, Australia. For their study, they first evaluated structures of synthetic A-gliadin peptides shown to be toxic in the fetal chick assay, both before and after digestion with duodenal mucosa from patients in long remission. They also measured synthetic peptides corresponding to the undigested residues, and compared the key amino acid sequences, to see if they might be related to direct toxicity and immunogenicity of the peptides. They found that the smallest toxic peptides from celiac mucosal digestion were octa-peptides, which they found in greater amounts than similar products from normal digestion. One of those peptides corresponded to residues 12-19 of A-gliadin and contained the key motifs PSQQ and QQQP of De Ritis et al., while the other corresponded to residues 72-79, and contained the key motif PYPQ (extending to PYPQPQ). These key motifs have been noted by other workers, especially those investigating immunological activity over the past two decades. They are present in undigested residues from celiac mucosal digestion These motifs, along with the greater prevalence of these residues, as compared with residues from normal digestion, supports the basic notions underpinning enzyme therapy for celiac disease. This study also supports the basic scientific merits of research and development of the enzyme caricain to break down gliadin peptides with two different types of toxicity, and thus to potentially benefit people with celiac disease. Source: International Journal of Celiac Disease. Vol. 4, No. 4, 2016, pp 113-120. doi: 10.12691/ijcd-4-4-2 Previous study: NCBI
  2. Jefferson Adams

    What Exactly is Gluten, Anyway?

    Celiac.com 07/04/2018 - For the vast majority of people, gluten is nothing to worry about. However, for people with celiac disease, gluten triggers an immune reaction that can be uncomfortable and lead to damage of the intestinal lining, and, left untreated, other conditions, including certain types of deadly cancers. Actually, the real offender is a protein in gluten called gliadin. It's the gliadin that triggers the immune reaction in people with celiac disease. For our purposes today, I will talk about gluten, even though it's really gliadin that's the culprit. Still, avoiding gliadin means avoiding gluten, so let's just keep it simple, if a bit unscientific, for now. There are some people who are sensitive to gluten, but who don’t have celiac disease, a condition know as Non-Celiac Gluten Sensitivity (NCGS). When people with NCGS eat gluten, they often experience symptoms similar to those with celiac disease, yet they lack the same antibodies to gluten, as well as the intestinal damage seen in celiac disease. People with celiac disease and gluten sensitivity need to follow a gluten-free diet that excludes all products containing wheat, barley and rye ingredients. These people can still enjoy a healthy diet filled with fruits, vegetables, meats, poultry, fish, beans, legumes and most dairy products. Many delicious foods are naturally gluten-free, and safe for people with celiac disease. That said, gluten is found in a wide variety of foods, even those you wouldn’t expect, such as soy sauce and even some french fries. Foods containing wheat, barley or rye contain gluten, but the protein can also be hidden in many foods as an additive, especially processed foods. Gluten can also sometimes be found in certain medications, personal hygiene products and more. For people with celiac disease, even tiny amounts of gluten can cause damage to the small intestine and prevent nutrients from being absorbed into the bloodstream. The safest bet is to purchase naturally gluten-free grains, flours and starches labeled gluten-free and, when possible, certified gluten-free by a third party. For a more complete list, see Celiac.com’s gluten-free Safe Foods List and the non-gluten free Unsafe Foods List. What Foods and Products Contain Gluten? Gluten is found in any products with ingredients derived from wheat, barley and rye. This includes: 1) Wheat products (Triticum), including: All species of wheat contain gluten, including durum, semolina, spelt, kamut, einkorn, faro and triticale, which is a hybrid of wheat and rye. 2) Barley Products (Hordeum vulgare) 3) Rye Products (Secale) 4) Any bakery item, beer, breads, candy (not all), cereal, flour, pastas, non-dairy milk (not all), sauces (not all), soups (not all), or other product made with wheat, rye, barley, including the following ingredients: Abyssinian Hard (Wheat triticum durum) Alcohol (Spirits - Specific Types) Atta Flour Barley Grass (can contain seeds) Barley Hordeum vulgare Barley Malt Beer (most contain barley or wheat) Bleached Flour Bran Bread Flour Brewer's Yeast Brown Flour Bulgur (Bulgar Wheat/Nuts) Bulgur Wheat Cereal Binding Chilton Club Wheat (Triticum aestivum subspecies compactum) Common Wheat (Triticum aestivum) Cookie Crumbs Cookie Dough Cookie Dough Pieces Couscous Criped Rice Dinkle (Spelt) Disodium Wheatgermamido Peg-2 Sulfosuccinate Durum wheat (Triticum durum) Edible Coatings Edible Films Edible Starch Einkorn (Triticum monococcum) Emmer (Triticum dicoccon) Enriched Bleached Flour Enriched Bleached Wheat Flour Enriched Flour Farik Farina Farina Graham Farro Filler Flour (normally this is wheat) Freekeh Frikeh Fu (dried wheat gluten) Germ Graham Flour Granary Flour Groats (barley, wheat) Hard Wheat Heeng Hing Hordeum Vulgare Extract Hydroxypropyltrimonium Hydrolyzed Wheat Protein Kamut (Pasta wheat) Kecap Manis (Soy Sauce) Ketjap Manis (Soy Sauce) Kluski Pasta Maida (Indian wheat flour) Malt Malted Barley Flour Malted Milk Malt Extract Malt Syrup Malt Flavoring Malt Vinegar Macha Wheat (Triticum aestivum) Matza Matzah Matzo Matzo Semolina Meripro 711 Mir Nishasta Oriental Wheat (Triticum turanicum) Orzo Pasta Pasta Pearl Barley Persian Wheat (Triticum carthlicum) Perungayam Poulard Wheat (Triticum turgidum) Polish Wheat (Triticum polonicum) Rice Malt (if barley or Koji are used) Roux Rusk Rye Seitan Semolina Semolina Triticum Shot Wheat (Triticum aestivum) Small Spelt Spirits (Specific Types) Spelt (Triticum spelta) Sprouted Wheat or Barley Stearyldimoniumhydroxypropyl Hydrolyzed Wheat Protein Strong Flour Suet in Packets Tabbouleh Tabouli Teriyaki Sauce Timopheevi Wheat (Triticum timopheevii) Triticale X triticosecale Triticum Vulgare (Wheat) Flour Lipids Triticum Vulgare (Wheat) Germ Extract Triticum Vulgare (Wheat) Germ Oil Udon (wheat noodles) Unbleached Flour Vavilovi Wheat (Triticum aestivum) Vital Wheat Gluten Wheat, Abyssinian Hard triticum durum Wheat Amino Acids Wheat Bran Extract Wheat, Bulgur Wheat Durum Triticum Wheat Germ Extract Wheat Germ Glycerides Wheat Germ Oil Wheat Germamidopropyldimonium Hydroxypropyl Hydrolyzed Wheat Protein Wheat Grass (can contain seeds) Wheat Nuts Wheat Protein Wheat Triticum aestivum Wheat Triticum Monococcum Wheat (Triticum Vulgare) Bran Extract Whole-Meal Flour Wild Einkorn (Triticum boeotictim) Wild Emmer (Triticum dicoccoides)
  3. Celiac.com 06/26/2018 - Gliadin is an alcohol-soluble wheat protein that is toxic for people with celiac disease. Gliadin toxicity is not lowered by digestion with gastro-pancreatic enzymes. It’s been documented that an innate immunity to gliadin plays a key role in the development of celiac disease. This is mainly due to an immune response that induces epithelial stress and reprograms intraepithelial lymphocytes into natural killer (NK)-like cells, leading to enterocyte apoptosis and an increase in epithelium permeability. A team of researchers recently set out to elaborate on the role played by innate immunity to gliadin in the development of celiac disease by assessing the in vitro effects of enzymatic digested gliadin on the functionality of the process of autophagy, or natural cell destruction. The research team included Federico Manai, Alberto Azzalin, Fabio Gabriele, Carolina Martinelli, Martina Morandi, Marco Biggiogera, Mauro Bozzola, and Sergio Comincini. They are variously affiliated with the Department of Biology and Biotechnology, and with the Pediatrics and Adolescentology Unit in the Department of Internal Medicine and Therapeutics at University of Pavia, Fondazione IRCCS, Pavia, Italy. They reported recently that the administration of enzymatically digested gliadin (PT-gliadin) in in Caco-2 cells significantly reduced the expression of the autophagy-related marker LC3-II. Moreover, analysis by electron and fluorescent microscope suggests a compromised functionality of the autophagosome apparatus. The team established the rescue of the dysregulated autophagy process, along with a reduction of PT-gliadin toxicity, by using a starvation induction protocol, and by 3-methyladenine administration. Rapamycin, a well-known autophagy inducer, did not trigger significant improvement in the clearance of extra- and intra-cellular fluorescent PT-gliadin amounts. These results show the potential role of the autophagy process in the degradation and reduction of extra-cellular gliadin peptides, and provides new molecular targets for counteracting adverse gliadin reactions in celiac patients. Source: Int J Mol Sci. 2018 Feb; 19(2): 635. doi:  10.3390/ijms19020635
  4. Celiac.com 04/17/2018 - Could the holy grail of gluten-free food lie in special strains of wheat that lack “bad glutens” that trigger the celiac disease, but include the “good glutens” that make bread and other products chewy, spongey and delicious? Such products would include all of the good things about wheat, but none of the bad things that might trigger celiac disease. A team of researchers in Spain is creating strains of wheat that lack the “bad glutens” that trigger the autoimmune disorder celiac disease. The team, based at the Institute for Sustainable Agriculture in Cordoba, Spain, is making use of the new and highly effective CRISPR gene editing to eliminate the majority of the gliadins in wheat. Gliadins are the gluten proteins that trigger the majority of symptoms for people with celiac disease. As part of their efforts, the team has conducted a small study on 20 people with “gluten sensitivity.” That study showed that test subjects can tolerate bread made with this special wheat, says team member Francisco Barro. However, the team has yet to publish the results. Clearly, more comprehensive testing would be needed to determine if such a product is safely tolerated by people with celiac disease. Still, with these efforts, along with efforts to develop vaccines, enzymes, and other treatments making steady progress, we are living in exciting times for people with celiac disease. It is entirely conceivable that in the not-so-distant future we will see safe, viable treatments for celiac disease that do not require a strict gluten-free diet. Read more at Digitaltrends.com , and at Newscientist.com
  5. I was wondering if someone can help me understand my results. I got wishy washy responses from two different doctors and I am still pretty confused. I attached an image of my results, but in case you aren't able to view it, my Gliadin IgA is high, but everything else seems to be in low and in normal range. Anyone know what this means? At the time of this test, I was on a pretty low to no-gluten diet. I'd appreciate any insight you all can provide!
  6. Hey guys! Recently diagnosed officially after aoiding gluten for 12 years. It took me 3 doctors to find someone who would come at the issue with a non-biased POV. I ended up doing a gluten challenge and got a blood test and biopsy. Today I got a blood test I took last year prior to the gluten challenge and the Gliadin IGA was 78.0. I have two questions; 1) Dr who ordered the blood test told me a lot of things that were not accurate abt celiac and ruled it out totally. With a Gliadin IGA of 78, that’s just flat out wrong, isn’t it? I mean doesn’t it indicate a liklihood of celiac of like 97%? 2) Whatever diet I was eating for 14 yrs was not adequate to what I need to live with celiac based on this test, right? Just checking. I think that’s what it means and that I need to tighten up my gluten-free diet a little in light of the dx? I know a lotta you guys are serious blood test gurus so I’ll put this out there. Thanks, fam!
  7. So a couple years ago I was tested for celiac... Ttg IgG/IgA were all negative DGA IgG/IgA were all negative AGA IgG: Positive AGA IgA Negative HLADQB1*02 Negative HLADQB1*03:02 Negative HLADQA1*05 Positive Biopsies have all been negative. I suffer from Hashimoto's thyroiditis and I just feel miserable with all the body aches and brain fog. My son was born back in July and I'm just so tired of not feeling well and I really want to finally feel good and enjoy life to the fullest. I'm thinking of asking for my labs to be repeated again and see. I'm just wondering if it is possible for me to still have celiac or if I'm just looking for something that just isn't there because I'm desperate for answers... Appreciate any input!! Thank you
  8. Iron: 17 mcg/dL (Low) November 11, 2016 Ferritin: 1.8 ng/mL (Low) November 11, 2016 RBC: 4.05x10^6/uL (Low) November 11, 2016 Hemoglobin: 8.5 gm/dL (Low) November 11, 2016 Vitamin D: 25.7 ng/mL (Low) February 22, 2017 ANA Profile : February 27, 2017 FANA: Positive FANA Titer: 1:640 FANA Pattern: Homogenous Gliadin IgA: 2 units June 29, 2017 Gliadin IgG: 3 units June 29,2017 TTG Ab IgA: <1 units/mL June 29, 2017 TTG Ab IgG: <1 units/mL June 29, 2017 Immunoglobulin A: 59.1 mg/Dl (Low) July 10, 2017 Immunoglobulin M: 44.2 mg/Dl (Low) July 10,2017 Immunoglobulin G: 1010.0 mg/Dl (Normal?) July 10, 2017 Immunoglobulin E: 5 KU/L July 10,2017 My RBC and Hemoglobin have come up and are normal. My iron levels will get high (too high) when I take 65 mg elemental iron twice a day for several weeks but my ferritin has never gotten over 42 ng/mL. When I stop taking my iron supplement my iron and ferritin plummet in just a matter of weeks. My hair is falling out, I get rapid heartbeat when I get too low on iron and if I get my iron too high. My whole body hurts especially my finger joints, back , knees and really all of my joints. Going to the bathroom at least 2 times day and sometimes up to 5 times a day. Extreme fatigue, Brain fog, extremely emotional and irritable. I just went gluten free July 1, 2017 and am starting to feel better. Joints feel better, I can sleep better, my mood is better. Celiac or maybe just gluten sensitive? Any thoughts? What do my labs say about me?
  9. Hello! This is my first post. My big question is about Gliadin IgG. I was tested in 2004 and had a high positive at 64 (24 being positive). My Dr at the time told me I should cut back on gluten and diagnosed me with Sjogrens Syndrome (even though I was B12 deficient, anemic, and having such bad acid reflux that I would get sores all over the back of my throat). Recently I was diagnosed with Lupus (SLE) and asked to be tested for Celiacs. My Gliadin tests came back negative, but TtG IgG was 6 (6-9 weak positive). TtG IgA was 1.4. Tomorrow I get the endoscopy and biopsy. I'm so confused as to why I tested so high for Gliadin IgG and now it is negative. I am not gluten free. The Dr said she has no idea and they are just trying to figure it out. Ive read Celiacs does not go into remission unless you are gluten free. Does anyone know how I could have been positive 12 yrs ago and now be negative?
  10. Hi, See if any experts here can help. My test result in May 2016 was Total igA normal anti ttg igA 42 (20 is cutoff) anti gliadin igA 55 (20 cutoff) I didnt choose to have a biopsy so I just went gluten-free I took repeated test about 50 days apart and the anti ttg igA went from 42--20---36---20---17. It has become negative. Antigliadin igA went from 55--50---47---70. Anyone can explain what the hell is going on with these numbers?
  11. Celiac.com 03/09/2009 - A team of researchers based in Finland recently demonstrated for the first time that B. lactis probiotic bacteria are capable of shielding epithelial cells from cellular damage caused by gliadin exposure. The research team was made up of doctors K. Lindfors, T. Blomqvist, K. Juuti-Uusitalo, S. Stenman, J. Venäläinen, M. Mäki and K. Kaukinen. They are associated with the Paediatric Research Centre for the Medical School of the Finland’s University of Tampere, the Department of Peadiatrics, and the Department of Gastroenterology and Alimentary Tract Surgery at Tampere University Hospital, and the Department of Pharmacology and Toxicology of the Finland’s University of Kuopio. In people with celiac disease, wheat gliadin causes serious intestinal symptoms and damages the small-bowel mucosa. Untreated, this can leave the individual at risk of developing various cancers and numerous associated conditions. Most all of this can be reversed or prevented if detected and treated early enough. Currently, the only effective treatment for celiac disease is a strict life-long gluten-free diet. However, a 100% gluten-free diet is nearly impossible to maintain, with so many gluten-free products containing trace amounts of gluten. Because of this, people with celiac disease face regular gluten contamination. Also because of this, acceptable alternatives are desirable. Earlier studies have indicated that probiotic bacteria might be used in sourdough fermentation to induce the hydrolysis of celiac toxic gluten in food manufacturing, and thereby benefit people with celiac disease. Although several studies have addressed the ability of probiotic bacteria to detoxify gliadin after an extensive incubation period, the team found none that investigated whether various live probiotic bacteria can inhibit gliadin-induced toxic effects directly on epithelial cells. In this study the team set out to determine whether probiotics Lactobacillus fermentum or Bifidobacterium lactis might block the toxic effects of gliadin in intestinal cell culture conditions. To assess the degree to which live probiotics were able to block peptic-tryptic digested gliadin-induced degradation of human colon cells Caco-2, the team measured epithelial permeability by transepithelial resistance, actin cytoskeleton arrangements by the extent of membrane ruffling and expression of tight junctional protein ZO-1. B. lactis inhibited the gliadin-induced increase dose-dependently in epithelial permeability, and, at higher concentrations totally eliminated the gliadin-induced reduction in transepithelial resistance. That is, B. lactis decreased or eliminated the compromise in cell-wall resistance caused by gliadin. This means that B. lactis overcame the mechanism that gives rise to the decreased cell resistance and the increased permeability that occurs during an adverse reaction to wheat gliadin. The B. lactis strain also interfered with the creation of membrane ruffles in Caco-2 cells caused by gliadin exposure. Furthermore, it also shielded the tight junctions of Caco-2 cells from the toxic effects of gliadin, as shown by the way in which ZO-1 is expressed. The researchers concluded that live B. lactis bacteria might achieve partial to full blockage of gliadin toxicity gluten/gliadin-induced damage in the small-intestinal mucosa of people with celiac disease, and that it merits further study concerning its potential as a dietary supplement to guard against any silent damage associated with accidental gluten-contamination in celiac disease. Clinical and Experimental Immunology, 152: 552–558
  12. Celiac.com 08/20/2015 - Celiac disease is frequently mis-diagnosed. Even when patients received endoscopy, celiac disease is often missed or not detected. A team of researchers recently assessed the accuracy of finger prick-based point-of-care tests in the detection of celiac disease, and developed an algorithm for diagnosis. The research team included PD Mooney, SH Wong, AJ Johnston, M Kurien, A Avgerinos, and DS Sanders. They are variously affiliated with the Royal Hallamshire Hospital, Sheffield, United Kingdom and the University of Sheffield, Sheffield, United Kingdom. Their team conducted a prospective study of two groups of celiac disease patients evaluated at the Royal Hallamshire Hospital in Sheffield UK from March 2013 through February 2014. In group one, the team evaluated 55 patients at high risk for celiac disease, and who tested positive for endomysial antibody, using the Biocard test (BHR Pharmaceuticals, Nuneaton, UK) and the Celiac Quick Test (Biohit Healthcare UK, Ellesmere Port, UK), which measure antibodies to tissue transglutaminase (anti-tTG), and the Simtomax test (Tillotts Pharma, Rheinfelden, Switzerland), which measures deamidated gliadin peptide antibodies (DGP). Group 2 included 508 consecutive patients who received an endoscopy for any reason, received the DGP test, and also were evaluated using a diagnostic algorithm that incorporated results from the DGP test and data on symptoms. For both groups, point-of-care tests were administered at the time of endoscopy, and the results compared against results from histologic analyses of duodenal biopsy specimens from all patients. In group 1, the DGP test identified patients with celiac disease with 94.4% sensitivity, the Celiac Quick Test identified patients with 77.8% sensitivity (P = .03 vs the DGP test), while the Biocard test identified patients with 72.2% sensitivity (P = .008 vs the DGP test). In group 2, the DGP test identified patients with celiac disease with 92.7% sensitivity (95% confidence interval, 83.0-97.3), 85.2% specificity (95% confidence interval, 81.5-88.3), a positive predictive value of 49.2% (95% confidence interval, 40.3-58.2), and a negative predictive value of 98.7% (95% confidence interval, 96.8-99.5). Measurement of serum anti-tTG identified patients with celiac disease with 91.2% sensitivity (95% confidence interval, 81.1-96.4), 87.5% specificity (95% confidence interval, 84.0-90.4), a positive predictive value of 53.0% (95% confidence interval, 43.6-62.2), and a negative predictive value of 98.5% (95% confidence interval, 96.5-99.4). The algorithm identified patients with celiac disease with 98.5% sensitivity, and has the potential to reduce duodenal biopsies by 35%. In this prospective study, the test for DGP identified celiac patients with comparable sensitivity and specificity as standard serologic analysis of anti-tTG. Conducting the DGP test before endoscopy might increase the accuracy of the diagnosis of celiac disease. These results look promising, but further study is needed, in lower-prevalence populations, to more accurately determine the potential benefits of the DGP test in celiac screening. Source: Clin Gastroenterol Hepatol. 2015 Jul;13(7):1278-1284.e1. doi: 10.1016/j.cgh.2015.01.010. Epub 2015 Jan 26.
  13. Hi all, Last week I underwent extensive blood, urine, and skin testing for psychiatric purposes. I had previously been diagnosed by a psychologist with depression (dysthymia), generalized anxiety disorder, and ADHD inattentive type. When I saw a psychiatrist, he suggested that my illness may be due to food reaction. Today I got back my test results, some of which pertain to gluten intolerance. Gliadin (deamidated) IGA: 7 units <20 antibody not detected Gliadin (deamidated) IGG: 3 units <20 antibody not detected Transglutaminase IGG: 3 U/ml <6 no antibody detected Transglutaminase IGG: 1 U/ml <4 no antibody detected (To me it seems if the antibody is not detected, then gluten intolerance/sensitivity shouldn't necessarily be the issue. Am I correct, or do I have it the other way around?) I was also administered injections of diluted (not concentrated, not sure if that matters) gluten and wheat that produced no symptoms or immediate reaction, but gave a very mild delayed reaction after 24 hours. Milk and corn, by contrast, produced more noticeable reactions. Still, the psychiatrist recommended immediately cutting all gluten out of my diet (along with dairy and corn, among some other dietary changes). I plan on taking his suggestion, but I have never had any of the common symptoms of gluten intolerance/sensitivity in the past to my knowledge. I am 22 years old. Not asking for medical advice but possibly some anecdotal comparisons: do my gliadin and transglutaminase results seem to significantly suggest gluten intolerance/sensitivity? Other posters in this forum have used more stringent reference ranges, but even then, my results seem low. Even though this diagnosis is coming from a medical professional with much greater expertise on the matter than I have, it seems to rely on a reading of my results as >0 automatically equating to gluten intolerance/sensitivity. I study statistics, so I'm skeptical of using rejection ranges that liberally. Curious what you all think. Thanks, Matt
  14. Celiac.com 01/29/2015 - Testing for tissue transglutaminase antibodies (TGA) is currently a common part of attempting to diagnose celiac disease. A research team wanted to find out if determination of antibodies to synthetic deamidatedgliadin peptides (anti-DGP) might work as an alternative or complement to TGA testing. To find out, the team assessed the performance of a time-resolved immunofluorometry (TR-IFMA) based anti-DGP assay in the diagnosis of celiac disease in children, and also retrospectively analyzed the appearance of anti-DGP antibodies before TGA seroconversion. The research team included A. Lammi, P. Arikoski, S. Simell, T. Kinnunen, V. Simell, S. Paavanen-Huhtala, A. Hinkkanen, R. Veijola, M. Knip, J. Toppari, O. Vaarala, O. Simell, and J. Ilonen. They are variously affiliated with the Department of Clinical Microbiology and the A.I. Virtanen Institute for Molecular Sciences at the University of Eastern Finland in Kuopio, Finland, the Department of Pediatrics at Kuopio University Hospital and University of Eastern Finland, Kuopio, Finland, the Department of Pediatrics at the University of Oulu and Oulu University Hospital in Oulu, Finland, the Children's Hospital, and the Institute of Clinical Medicine at the University of Helsinki in Helsinki, Finland, the Folkhälsan Research Center in Helsinki, Finland, the Department of Pediatrics at Tampere University Hospital in Tampere, Finland, the Immunogenetics Laboratory, and the Department of Physiology at the University of Turku, and with the Department of Pediatrics and Adolescent Medicine at the University of Turku and Turku University Hospital in Turku, Finland. For their study, the team assessed 92 children with biopsy-confirmed celiac disease. The team took blood samples at the time of, or just prior to, clinical diagnosis. The team also assessed a control group of 82 TGA-negative children who were positive for HLA-DQ2 or -DQ8. Based on receiver operating characteristics (ROC) curves, they found that the optimal cut-off value for IgA anti-DGP positivity was 153 arbitrary units (AU) with a sensitivity of 92.4% and specificity of 97.6%, while the optimal cut-off value for IgG anti-DGP 119 AU, with a sensitivity of 97.8% and specificity of 97.6%. They found that all 92 children with celiac disease tested positive for either IgA or IgG anti-DGP at the time of diagnosis. Blood results from 48 children with celiac disease, analyzed retrospectively before the diagnosis, showed that anti-DGP antibodies preceded TGA positivity in 35 of 48 celiac disease children and appeared an average of one year earlier. From these results, the TR-IFMA test for detecting anti-DGP antibodies shows high sensitivity and specificity for celiac disease in children. For most of the patients, anti-DGP seropositivity preceded TGA positivity, which means that monitoring anti-DGP antibodies frequently in genetically susceptible children might allow doctors to spot celiac disease earlier than allowed by current tests. Source: J Pediatr Gastroenterol Nutr. 2014 Dec 16.
  15. Gastroenterology Volume 129, Issue 3, Pages 786-796 (September 2005) Celiac.com 09/14/2005 - Researchers have long thought that the resistance of gliadin prolamines to digestive enzymes is a primary contributor to celiac disease—which leads to the intestinal permeability and inflammation in those who are at risk. Taking prolyl-endopeptidase enzymes (PEP) orally has been proposed and explored as a possible treatment for celiac disease (including extensive research done at Stanford Universitys Celiac Sprue Research Foundation – CSRF). In an effort to determine the feasibility of such a treatment, researchers in France conducted both in vitro (outside a living organism) and ex vivo—using biopsy specimens of active celiac disease patients—studies on the effects of PEP on gliadin peptides. For the in vitro studies the researchers used radio-reverse-phase high-performance liquid chromatography and mass spectrometry to analyze the degradation by PEP of 3H-labeled gliadin peptides 56-88 (33-mer). In the ex vivo studies the researchers added PEP and 3H-peptides together onto the mucosal side of duodenal biopsy specimens that were mounted in Using chambers, and the peptide transport and digestion were analyzed using radio-reverse-phase high-performance liquid chromatography. The results indicate that in both in vitro and ex vivo studies the gliadin peptides were only partly degraded by 20 mu/ml of PEP. This concentration of PEP decreased the quantity of intact gliadin peptides (31-49 and 56-88) that crossed the intestinal biopsy specimens, but did not prevent the intestinal passage of toxic or immunostimulatory metabolites—for this the researchers determined that PEP concentrations of at least 500 mu/ml for at least 3 hours was required to achieve full detoxification of gliadin peptides, and thus prevent intestinal transport of active fragments—unfortunately this finding virtually eliminates PEP as a possible treatment option for those with celiac disease. The researchers conclude optimistically, however: "After prolonged exposure to high concentrations of PEP, the amount of immunostimulatory gliadin peptides reaching the local immune system in celiac patients is decreased. These results provide a basis to establish whether such conditions are achievable in vivo (in living organisms)."
  16. Celiac.com 10/24/2012 - Doctors can face challenges when attempting to diagnose celiac disease in patients who have already begun a gluten-free diet, and/or when the results of tests are inconsistent. To better understand this problem, a group of researchers set out to assess the benefits of an in vitro gliadin challenge. The research team included Raffaella Tortora, MD, Ilaria Russo, PhD, Giovanni D. De Palma, MD, Alessandro Luciani, PhD, Antonio Rispo, MD, Fabiana Zingone, MD, Paola Iovino, MD, Pietro Capone, MD and Carolina Ciacci, MD. The study cohort included 57 patients without celiac disease, 166 patients with untreated celiac disease, 55 patients with celiac disease on a gluten-free diet, and 59 patients with challenging diagnosis. The team provided all patients with endoscopy for collection of duodenal samples, which served for the diagnosis of celiac disease and for the in vitro evaluation of the gliadin-induced mucosal expression of seven inflammatory markers: PY99, ICAM-1 (intercellular cell adhesion molecule), HLA-DR, CD3, CD25, CD69, and transglutaminase 2 IgA. Diagnostic work-up for celiac disease included the search of specific serum antibodies. Researchers asked patients in the challenging diagnosis group to stop gluten-free diet to facilitate the search for these antibodies under untreated conditions. They used the area under the receptor-operated curve (ROC) for statistical analyses on accuracy. For patients with and without celiac disease (not including those on a gluten-free diet) HLA-DR offered the best accuracy for diagnosing celiac disease (area under ROC = 0.99). Combining the data from the HLA-DR with data of other markers did not increase test accuracy. The team found similar results in the 39 patients of the difficult diagnosis group undergoing the search celiac disease-speciï¬c antibodies under untreated conditions. In vitro testing of mucosal HLA-DR to gliadin is an accurate tool for the diagnosing celiac disease, and also works in patients who are hard to diagnose. Source: Am J Gastroenterol 2012; 107:111–117; doi:10.1038/ajg.2011.311; published online 27 September 2011
  17. Hello everyone!! Still on my journey to figure out what's going on with me! I've had a positive gliadin IgG test, negative gliadin IgG, Negative tissue transglutaminase IgG/IgA... Negative biopsy, it showed inflammation and lymphocytes infiltrating the epithilium but no issues with the villi... After I went gluten free for a month and felt great... Reintroduced and all my aches pains and respiratory issues came back I didn't think I had any GI issues but when I reintroduced I realized it made me constipated.... Now I had the genetic testing done and my HLA-DQB1*02 and HLA-DQB1*03:02 were negative but HLA-DQA1*05 is positive. Report says this is rarely observed in individuals with celiac and that it is only mildly supportive of a clinical diagnosis of celiac disease..... I know I should just go gluten free cause it makes me feel better... But I would have really loved a yes you have this or a no you don't
  18. Traditionally, gluten is defined as a cohesive, elastic protein that is left behind after starch is washed away from a wheat flour dough. Only wheat is considered to have true gluten. Gluten is actually made up of many different proteins. There are two main groups of proteins in gluten, called the gliadins and the glutenins. Upon digestion, the gluten proteins break down into smaller units, called peptides (also, polypeptides or peptide chains) that are made up of strings of amino acids--almost like beads on a string. The parent proteins have polypeptide chains that include hundreds of amino acids. One particular peptide has been shown to be harmful to celiac patients when instilled directly into the small intestine of several patients. This peptide includes 19 amino acids strung together in a specific sequence. Although the likelihood that this particular peptide is harmful is strong, other peptides may be harmful, as well, including some derived from the glutenin fraction. It is certain that there are polypeptide chains in rye and barley proteins that are similar to the ones found in wheat. Oat proteins have similar, but slightly different polypeptide chains and may or may not be harmful to celiac patients. There is scientific evidence supporting both possibilities. When celiac patients talk about "gluten-free" or a "gluten-free diet," they are actually talking about food or a diet free of the harmful peptides from wheat, rye, barley, and (possibly) oats. This means eliminating virtually all foods made from these grains (e. g., food starch when it is prepared from wheat, and malt when it comes from barley) regardless of whether these foods contain gluten in the very strict sense. Thus, "gluten-free" has become shorthand for "foods that dont harm celiacs." In recent years, especially among non-celiacs, the term gluten has been stretched to include corn proteins (corn gluten) and there is a glutinous rice, although in the latter case, glutinous refers to the stickiness of the rice rather than to its containing gluten. As far as we know, neither corn nor glutinous rice cause any harm to celiacs.
  19. Celiac.com 10/07/2013 - People with non-celiac gluten-sensitivity often report gut and non-gut symptoms shortly after eating gluten; symptoms disappear on gluten-free diets, although these patients have no serologic markers of celiac disease, and no intestinal damage. However, there is no evidence to suggest any changes to blood or mucosa in those individuals. To better understand non-celiac gluten sensitivity, a research team recently assessed immunologic responses of duodenal mucosa samples and peripheral blood basophils, isolated from NCGS patients, after exposure to gliadin. The research team included Cristina Bucci, Fabiana Zingone, Ilaria Russo, Ivonne Morra, Raffaella Tortora, Norberto Pogna, Giulia Scalia, Paola Iovino, and Carolina Ciacci. They are affiliated with CEINGE in Naples, Italy; the Consiglio per la Ricerca e la Sperimentazione in Agricoltura in Rome, Italy; the Gastrointestinal Unit of the Department of Medicine and Surgery at the University of Salerno in Salerno, Italy; and with the Gastrointestinal Unit at the Department of Clinical and Experimental Medicine of Federico II University of Naples. Between January 2010 and July 2011, the research team gathered mucosa samples from 34 celiac disease patients who followed gluten-free diets for at least 6 months, 35 patients with untreated celiac disease, 16 patients with non-celiac gluten sensitivity (NCGS) and 34 healthy control subjects. The team diagnosed non-celiac gluten sensitivity based on patient symptoms and current diagnositic guidelines. For each of the 119 patients, the team conducted a complete clinical evaluation to exclude celiac disease while on a gluten-containing diet, a skin prick test to exclude wheat allergy, and upper endoscopy at 2 tertiary medical centers in Italy. After incubating each biopsy sample with gliadin, the team measured inflammatory markers, including anti-phosphotyrosine-monoclonal antibody (PY99), HLA-DR, intercellular cell adhesion molecule-1 (ICAM-1), CD3, CD25 and CD69. After incubation with gliadin, mucosa samples from the 69 patients with celiac disease showed increased immunofluorescence intensity for early and delayed markers of inflammation. They also found low levels of some of these markers in three patients with non-celiac gluten sensitivity and three controls. The team found normal mucosal architecture in 56.3% of patients with non-celiac gluten sensitivity. The remaining seven patients showed increased intraepithelial infiltration, but without eosinophils. They found no villous atrophy in patients with non-celiac gluten sensitivity, and no significant increases in the levels of CD63 and CD203c. The team did find that one patient each in the NCGS and control groups, whose results indicated only weak PY99 and ICAM-1 positivity, also had Helicobacter pylori infection. Unlike mucosa from patients with celiac disease, once incubated with gliadin, mucosa from patients with NCGS does not express markers of inflammation, nor does the gliadin activate their basophils. The in vitro gliadin challenge therefore should not be used to diagnose NCGS. This study does suggest that wheat components, other than proteins, might be associated with GI symptoms in patients with IBS, and should be assessed for a possible role in the pathogenesis of NCGS. Source: Clinical Gastroenterology and Hepatology. Volume 11, Issue 10 , Pages 1294-1299.e1, October 2013
  20. Celiac.com 06/10/2013 - Researchers have known for some time that immunoglobulin G antibodies against deamidated gliadin peptides are about as accurate as tissue transglutaminase and endomysium autoantibodies in diagnosing celiac disease in adults. However, not much is known about their predictive value in infants with a suspected gluten enteropathy. A team of researchers recently set out to determine if antibodies to deamidated gliadin peptides could be an accurate predictor of celiac disease in infants. The research team included S. Amarri, P. Alvisi, R. De Giorgio, M.C. Gelli, R. Cicola, F. Tovoli, R. Sassatelli, G. Caio, and U. Volta. They are affiliated with the Pediatric Unit, IRCCS - Arcispedale Santa Maria Nuova, Reggio Emilia, Italy. To test whether deamidated gliadin immunoglobulin G antibodies are more reliable than traditional tests for screening celiac disease in infants, the researchers tested 65 children under 2 years of age for deamidated gliadin immunoglobulin G, tissue transglutaminase and endomysium immunoglobulin A, and gliadin immunoglobulins A and G. The group included 42 infants with malabsorption, along with 23 infants as control subjects. Thirty-seven of the 42 children with malabsorption had deamidated gliadin antibodies, associated with tissue transglutaminase and endomysial antibodies in 33, and with gliadin immunoglobulins A and G in 21 and 29, respectively. The team conducted intestinal biopsy in 34 of the 37 children who tested positive for deamidated gliadin antibodies. Thirty-two of the 34 showed villous atrophy consistent with celiac disease, while one of the remaining two had a Marsh 1 and the other showed normal mucosa. The control group showed only gliadin immunoglobulins A (4.3 %) and G (39.1 %). The results showed that deamidated gliadin, tissue transglutaminase and endomysial antibodies were significantly more sensitive for celiac disease than gliadin immunoglobulins G and A. High levels of deamidated gliadin antibodies correlated with severe intestinal damage. For infants, deamidated gliadin antibodies showed a higher diagnostic accuracy for celiac disease than gliadin antibodies. High levels of deamidated gliadin antibodies are good predictors of severe gluten-dependent duodenal damage. Source: J Clin Immunol. 2013 Apr 5.
  21. Hi My blood values are coming down, but while the anti-deaminated gliadin IGG has come down to normal values, the TTG IGA is still lagging behind at 12 (should be <7). TTG IGA was 15 in January. Why is it that the anti-deaminated gliadin comes down before the TTG?
  22. I've been reading all about these test results and I don't understand what I have. There seems to be different wording for some of the tests and I don't understand my results. I know one is high, but does that mean I've got Celiac Disease, or just a gluten intolerance Do I need to get the biopsy done? I've been gluten-free for 3 months now, would I need to go back to eating gluten before I get the biopsy done? Here are my test results: Immunoglobulin A: 427 (normal range 68-378) Tissue Transglutaminase Antibody, lgA: 5 (normal range 0-19) Gliadin lgA Antibodies: 5 (normal range 0-19) thanks in advance for any assistance!
  23. Celiac.com 10/20/2010 - U.S. doctors and patients looking for accurate early diagnosis of celiac disease now have a state of the art celiac disease assay with a high level of sensitivity and specificity. The US Food and Drug Administration (FDA) has given 510(k) clearance for the first two fully automated gliadin tests featuring deamidated peptides for celiac disease. Manufactured by Phadia US, the tests, EliA GliadinDP IgA and EliA GliadinDP IgG, are designed to be used in conjunct with other laboratory and clinical findings in the early diagnosis of celiac disease. According to Gabi Gross, autoimmune franchise leader for Phadia US, "EliA GliadinDP IgA and EliA GliadinDP IgG will offer physicians who suspect a possible case of celiac disease, antibody tests with the lowest number of false positive results." This means less "unnecessary endoscopies and biopsies," she adds. EliA GliadinDP IgA and EliA GliadinDP IgG will offer antibody tests with the lowest number of false positive results for doctors who suspect a patient has celiac disease. The assays are optional on Laboratory Systems Phadia 100Є and Phadia 250 instruments with features like quick turnaround, monthly calibration, onboard instrument dilution, and a discrete single-well, random-access, nonmicrotiter plate format. Phadia also manufactures other approved CLIA moderately complex assays in the EliA autoimmune product line, including anticardiolipin IgG/IgM, anti-B2-glycoprotein 1 IgG/IgM, cyclic citrullinated peptide, tissue transglutaminase IgA/ IgG, gliadin IgA/IgG, dsDNA, antinuclear antibody screen, and ENA antibodies to the following antigens: Sm, U1RNP, RNP70, Ro, La, Scl-70, CENP, and Jo-1. Source: Medscape
  24. Celiac.com 12/31/2012 - In people with celiac disease, eating wheat, barley, or rye triggers inflammation in the small intestine. Left unchecked, this inflammation causes the gut damage that is associated with untreated celiac disease. Specifically, the storage proteins in these grains (gluten) trigger an adaptive Th1-mediated immune response in individuals carrying HLA-DQ2 or HLA-DQ8 as major genetic predisposition. Researchers actually have a pretty good understanding of this aspect of celiac disease, part of a process called adaptive immunity. However, there has been some research that suggests that gluten proteins might trigger an immune response in people who do not have celiac disease, and who do not carry the HLA-DQ2 or HLA-DQ8 genetic markers that predispose them to developing celiac disease. Such a response is part of a process called innate immunity, and is far less understood than the adaptive immunity process. The innate immune system provides an early response to many microbial and chemical stimuli and is critical for successful priming of adaptive immunity. To better understand the relationship between adaptive immunity and innate immunity in celiac disease, a research team recently set out to determine if gliadin digests might induce innate immune responses in celiac and non-celiac individuals. Specifically, they wanted to know if wheat amylase trypsin inhibitors drive intestinal inflammation, and if so, by what receptor mechanism. The research team included Yvonne Junker, Sebastian Zeissig, Seong-Jun Kim, Donatella Barisani, Herbert Wieser, Daniel A. Leffler, Victor Zevallos, Towia A. Libermann, Simon Dillon, Tobias L. Freitag, Ciaran P. Kelly, and Detlef Schuppan. They are affiliated variously with the Division of Gastroenterology and the Proteomics and Genomics Center at Beth Israel Deaconess Medical Center at Harvard Medical School in Boston, with the Department of General Pediatrics and the Department of Internal Medicine I at the University Medical Center Schleswig-Holstein Kiel in Kiel, Germany, the Department of Experimental Medicine at the University of Milano-Bicocca in Milan, Italy, the German Research Center for Food Chemistry in Garching, Germany, the Hans-Dieter-Belitz-Institute for Cereal Grain Research in Freising, Germany, the Division of Molecular and Translational Medicine in the Department of Medicine I at Johannes Gutenberg University in Mainz, Germany, and with the Department of Bacteriology and Immunology at the Haartman Institute at the University of Helsinki in Finland. A number of earlier studies (Molberg et al., 1998; Anderson et al., 2000; Shan et al., 2002) have found HLA-DQ2– and HLA-DQ8–restricted gluten peptides that trigger the adaptive immune response in people with celiac disease. However, only 2–5% of individuals who show these HLAs develop celiac disease, which means that other factors, especially innate immune activation, are at play in the generation of celiac disease. Responsive innate cells are primarily macrophages, monocytes, DCs, and polymorphonuclear leukocytes that by means of their pattern-recognition receptors, such as TLRs, trigger the release of proinflammatory cytokines and chemokines, resulting in recruitment and activation of additional inflammatory cells (Medzhitov, 2007). Earlier studies (Maiuri et al., 2003) showed that peptides p31-43 or p31-49 from α-gliadin, that lack adaptive stimulatory capacity, triggered innate immune reactions by inducing IL-15 and Cox-2 expression in patient biopsies, and MHC class I polypeptide–related sequence A (MICA) on intestinal epithelial cells (Hüe et al., 2004). However, these studies have proven difficult to reproduce in cell culture, and researchers could not identify any specific receptor responsible for the observed effects. In a subsequent study, gliadin, in cell culture, reportedly triggered increased expression of co-stimulatory molecules and the production of proinflammatory cytokines in monocytes and DCs (Nikulina et al., 2004; Cinova et al., 2007). Two other studies (Thomas et al., 2006; Lammers et al., 2008) implicated the chemokine receptor CXCR3 in increased intestinal epithelial permeability upon gliadin challenge in a MyD88-dependent manner. However, those studies failed to reproducibly identify a specific gliadin peptide as the trigger. So far, no clear picture of the role of the innate immune system in celiac disease has emerged. In this study, the researchers show that members of the non-gluten α-amylase/trypsin inhibitors (ATIs), CM3 and 0.19, pest resistance molecules in wheat and related cereals, are strong triggers of innate immune responses in human and murine macrophages, monocytes, and dendritic cells. Their results show that ATIs activate the TLR4–MD2–CD14 complex and lead to up-regulation of maturation markers and elicit release of proinflammatory cytokines in cells from celiac and nonceliac patients and in celiac patients’ biopsies. They also show that mice deficient in TLR4 or TLR4 signaling are protected from intestinal and systemic immune responses upon oral challenge with ATIs. These findings define cereal ATIs as novel contributors to celiac disease. Moreover, ATIs may fuel inflammation and immune reactions in other intestinal and nonintestinal immune disorders. The findings of this study mean that the proteins in wheat may trigger immune reactions not just in people with celiac disease, but in people without celiac disease, and that these reactions may be actively contributing to the development of numerous other intestinal and non-intestinal immune disorders. That's a pretty big deal. Stay tuned to see how future studies elaborate these findings. Read the entire study in the Journal of Experimental Medicine. Source: J Exp Med. 2012 Dec 17;209(13):2395-408. doi: 10.1084/jem.20102660
  25. Celiac.com 12/12/2012 - In duodenal biopsy samples from people with active celiac disease, the transferrin receptor, CD71, is up-regulated, and promotes retro-transport of secretory immunoglobulin A (SIgA)-gliadin complexes. To better understand how interactions between SIgA and CD71 promote transepithelial transport of gliadin peptides, a team of researchers set out to determine if interactions among secretory immunoglobulin A, CD71, and transglutaminase-2 affect permeability of intestinal epithelial cells to gliadin peptides. The research team included C. Lebreton, S. Ménard, J. Abed, I.C. Moura, R. Coppo, C. Dugave, R.C. Monteiro, A. Fricot, M.G. Traore, M. Griffin, C. Cellier, G. Malamut, N. Cerf-Bensussan, and M. Heyman. They are affiliated with the Mixed Research Unit 989 of the National Institute of Health and Medical Research (INSERM UMR989) in Paris, France. For their study, the team evaluated duodenal biopsy specimens from 8 adults and 1 child with active celiac disease. The team used fluorescence-labeled small interfering RNAs against CD71 to transfect Caco-2 and HT29-19A epithelial cell lines. They used flow cytometry, immunoprecipitation, and confocal microscopy to assess interactions among IgA, CD71, and transglutaminase 2 (Tgase2). They then assessed transcytosis of SIgA-CD71 complexes and intestinal permeability to the gliadin 3H-p31-49 peptide in polarized monolayers of Caco-2 cells. To assess physical interplay between SIgA and CD71 or CD71 and Tgase2 at the apical surface of enterocytes in biopsy samples and monolayers of Caco-2 cells, the team used fluorescence resonance energy transfer and in situ proximity ligation assays. They co-precipitated CD71 and Tgase2 with SIgA, bound to the surface of Caco-2 cells. They found that SIgA-CD71 complexes were internalized and localized in early endosomes and recycling compartments, but not in lysosomes. In the presence of celiac IgA or SIgA against p31-49, transport of intact 3H-p31-49 increased significantly across Caco-2 monolayers, while soluble CD71 or Tgase2 inhibitors interfered with transport. Once it binds to apical CD71, SIgA (with or without gliadin peptides) enters a recycling pathway and avoids lysosomal degradation; this process allows apical-basal transcytosis of bound peptides. This mechanism is assisted by Tgase2 and might be involved in the pathogenesis of celiac disease. Source: Gastroenterology. 2012 Sep;143(3):698-707.e1-4. doi: 10.1053/j.gastro.2012.05.051.
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