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  • Jefferson Adams
    Jefferson Adams

    What Exactly is Gluten, Anyway?

      Gluten is a protein found in wheat, barley and rye. Gluten is the thing that gives makes dough stretchy and pliable, and gives bread its classic chewy, soft texture. When you eat soft, chewy bread, you can thank gluten.

    Caption: Image: CC--Jeff Kubina

    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)
       

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  • About Me

    Jefferson Adams earned his B.A. and M.F.A. at Arizona State University, and has authored more than 2,000 articles on celiac disease. His coursework includes studies in biology, anatomy, medicine, science, and advanced research, and scientific methods. He previously served as Health News Examiner for Examiner.com, and devised health and medical content for Sharecare.com. Jefferson has spoken about celiac disease to the media, including an appearance on the KQED radio show Forum, and is the editor of the book "Cereal Killers" by Scott Adams and Ron Hoggan, Ed.D.

  • Related Articles

    Jefferson Adams
    Celiac.com 10/16/2009 - A team of researchers recently set out to investigate the ability of a polymeric binder to reverse the toxic effects induced by gliadin in human intestinal cells and gliadin-sensitive HCD4-DQ8 mice. The team was made up of Maud Pinier, Elena F. Verdu, Mohamad Nasser–Eddine, Chella S. David, Anne Vézina, Nathalie Rivard, and Jean–Christophe Leroux.
    The team neutralized gliadin through complexation to a linear copolymer of hydroxyethylmethacrylate (HEMA) and sodium 4-styrene sulfonate (SS). They then examined the ability of the polymeric binder to mitigate the damaging effect of gliadin on cell-cell contact in IEC-6, Caco-2/15, and primary cultured differentiated enterocytes.
    They used gliadin-sensitive HLA-HCD4/DQ8 transgenic mice to measure the effectiveness of the polymeric binder in averting gliadin-triggered intestinal barrier dysfunction.  They found that Poly(hydroxyethylmethacrylate-co-styrene sulfonate) [P(HEMA-co-SS)] complexed with gliadin in a fairly precise manner.
    Exposing intestinal cells to gliadin caused major changes in both cell structure and cell to cell contacts. By complexing the gliadin with P(HEMA-co-SS) the researchers were able to prevent these undesirable changes. More importantly, the P(HEMA-co-SS) inhibited gliadin digestion by gastrointestinal enzymes, which minimized the development of peptides that trigger immune adverse immune reactions.
    By co-administering P(HEMA-co-SS) with gliadin to HLA-HCD4/DQ8 mice, researchers were able to eliminate gliadin-triggered changes in the gut barrier and lower intraepithelial lymphocyte and macrophage cell counts.
    From these results, the team concludes that polymeric binders can prevent in vitro gliadin-induced epithelial toxicity and intestinal barrier dysfunction in HCD4/DQ8 mice. Such polymeric binders might play a significant role in the treating people with gluten-induced disorders.
    Source:
    GASTROENTEROLOGY 2009;136:288–298


    Jefferson Adams
    Gliadin Triggers Innate Immune Reaction in Celiac and Non-celiac Individuals
    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

    Jefferson Adams
    Enzyme Shows Promise In Dissolving Gliadin Peptides in Celiac Patients
    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

    Betty Wedman-St Louis, PhD, RD
    Cannabis and Gluten
    Celiac.com 04/13/2018 - Is cannabis gluten-free? That is a frequent question I receive now that over 50%  of the United States has approved medical cannabis and some states have also included recreational cannabis. Let's begin be describing cannabis as an oral medicine that has been used since the Chinese treatise on pharmacology described Emperor Shen Nung in 2737 BCE using it. 
    In 1850 cannabis was listed in the U.S. Pharmacopoeia as a cure for many ailments. By the early 1900's Squibb Company, Eli Lilly and Park-Davis were manufacturing drugs produced from marijuana for use as antispasmodics, sedatives, and analgesics (pain medication).
    Today, hemp seed and hemp oil products are widely available. They provide CBD or cannabidiol - the non-psychoactive cannabinoid from various Cannabis sativa strains grown for high CBD levels. In order to be legal in the U.S. these products must contain less than 0.3% THC, the psychoactive cannabinoid in cannabis. CBD products can be consumed as capsules, tinctures, "gummy" chewables, lollipops, and numerous edibles like brownies, chocolates, and granola bars.
    The nutritive value of cannabis is presently described as that of hemp seed since no scientific analysis of Cannabis sativa has been done. Hemp is one of the world's most nutritious foods with high quality protein and essential fatty acids found in its seeds. Hemp contains all eight essential amino acids and can be sprouted for use in salads and shakes.
    Celiacs with protein allergies to eggs and soy need to be cautious when adding hemp and CBD products to their diet regimes. The major proteins in hemp are albumen and edestin. Hemp is a nut so those celiacs with nut sensitivities need to consider that. Others may be limiting their lectin intake and need to limit CBD products until processing evaluations can indicate levels resulting in the products.
    CBD oils contain linoleic and linolenic fatty acids which are important in reducing inflammation. They can be used in salad dressings, mashed potatoes and substituted for olive oil in recipes. Since these essential fatty acids must be obtained in the diet, using hemp or cannabis CBD products can enhance health.
    Cannabis products- particularly CBD- have been overlooked by individuals needing symptom relief from neurological (Parkinson's, ALS, Multiple Sclerosis, migraine), immune (cancer), and gastrointestinal disorders (Crohn's disease, IBS). When choosing cannabidiol-CBD products be sure to check that they have been tested for pesticides, heavy metals, and microbiological contaminants. 
    Today, more hemp is sold to pet owners as bird seed than used by humans. But as more individuals learn of the botanical benefits of cannabis, they should consider adding it to their diet and supplement regime. My book, Cannabis-A Clinician's Guide (CRC Press 2018) reviews the science and clinical uses of cannabis along with how to use it in recipes.  

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    Im the same, I never know what to eat, some food does better than others for me, I went on to make my own soup and Im glad I did, I should do it more often and at least then J know what's going in to it, it wasn't the best first try but I enjoyed it haha
    Thank you for the advice, in the end I went and made my own soup, not great for my first try but it was better than potentially making myself worse, I enjoyed it, I got some vitamains too to take, I was able to find a liquid Vitamain B Complex, the store I went to was helpfull enough to show me what was Gluten Free.   I fealt awful around then, Im feeling like I have more energy now I can actually do things and focus more, Ill keep on like I have been, Im not 100% and still have some B
    Not to mention the fact that (for those using the Nima) the Nima sensor has been known to give false positives. https://www.theverge.com/2019/4/1/18080666/nima-sensor-testing-fda-food-allergy-gluten-peanut-transparency-data https://www.celiac.ca/cca-statement-nima-gluten-sensor/ https://www.allergy-insight.com/nima-is-it-really-96-9-accurate/ https://www.glutenfreewatchdog.org/news/troubling-gluten-testing-data-released-by-nima-but-hold-the-phone/ https://www.glutenfreew
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