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      Frequently Asked Questions About Celiac Disease   04/07/2018

      This Celiac.com FAQ on celiac disease will guide you to all of the basic information you will need to know about the disease, its diagnosis, testing methods, a gluten-free diet, etc.   Subscribe to Celiac.com's FREE weekly eNewsletter   What are the major symptoms of celiac disease? Celiac Disease Symptoms What testing is available for celiac disease?  Celiac Disease Screening Interpretation of Celiac Disease Blood Test Results Can I be tested even though I am eating gluten free? How long must gluten be taken for the serological tests to be meaningful? The Gluten-Free Diet 101 - A Beginner's Guide to Going Gluten-Free Is celiac inherited? Should my children be tested? Ten Facts About Celiac Disease Genetic Testing Is there a link between celiac and other autoimmune diseases? Celiac Disease Research: Associated Diseases and Disorders Is there a list of gluten foods to avoid? Unsafe Gluten-Free Food List (Unsafe Ingredients) Is there a list of gluten free foods? Safe Gluten-Free Food List (Safe Ingredients) Gluten-Free Alcoholic Beverages Distilled Spirits (Grain Alcohols) and Vinegar: Are they Gluten-Free? Where does gluten hide? Additional Things to Beware of to Maintain a 100% Gluten-Free Diet What if my doctor won't listen to me? An Open Letter to Skeptical Health Care Practitioners Gluten-Free recipes: Gluten-Free Recipes
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    Betty Wedman-St Louis, PhD, RD

    • Journal of Gluten Sensitivity Winter 2015 Issue

    Celiac.com 06/16/2016 - Do you realize that metabolic and emotional stress, hormonal imbalance and food sensitivities all impact digestion? Many individuals believe that once they stop eating gluten, digestive disorders will disappear. Nothing could be further from the truth as we take a closer look at gastroenterology and the link between the gut and brain.

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    The adult gut has between 10 trillion and 100 trillion bacteria that make up the microbiome or surface of the intestines. The goal for digestive wellness is to be sure that there are more GOOD bacteria than BAD bacteria in the microbiome. Food choices, antibiotic use and lifestyle play an important part in creating that balance. Endocrine disrupting chemicals in plastics, along with artificial sweeteners all influence the bacteria or microbiome levels.

    The bacteria content of the gut begins at birth. A vaginal delivery results in a microbiome from the mother while a cesarean section produces a microbiome from everyone who handles the infant. Gut bacteria levels are also influenced by breast feeding versus the use of infant formula.

    Diets deficient in fruits and vegetables mean less antioxidants are consumed so free radicals can destroy digestive and immune function. In addition, fruits and vegetables provide fiber for bacteria to grow on. Current research from the Journal of Clinical Nutrition indicates high fiber diets yield more bacteroides bacteria growth that helps control body weight. Low fiber diets result in more firmicute bacteria which produces weight gain and can lead to obesity.

    Microbiological safety in fresh produce continues to gain prominence in the media. Fresh cut, RTE (ready to eat) produce in convenient packages leads the way in food safety recalls. Fruits and vegetables are prone to microbial contamination from irrigation water, soil, fertilizers, insects, animal feces and field workers during pre-harvest processing. After harvest, the washing and sanitation procedures lack oversight. Remember to wash all raw fruits and vegetables to minimize food poisoning potential.

    Listeria monocytogenes is one of the leading causes of death from food borne illness. It is found in raw milk, cheese, and packaged deli meats. Flu-like symptoms can last days to weeks, and in pregnant women listeria infection can lead to miscarriage.

    Noroviruses make the news regularly, especially on cruise ships. Common food sources include raw produce and shellfish such as clams, mussels, scallops and oysters. Symptoms begin as early s 12 hours after ingestion and the malaise disappears 3 to 4 days later.

    Salmonella continues to plague many with chills, nausea, joint pain and headaches beginning 12 hours post ingestion. Eggs, poultry and raw produce are major sources of salmonella.

    Probiotics are an important addition to the celiac diet for balancing the bacteria levels in the GI tract. They should be taken WITH food to reduce the degradation in an acid stomach. Research has shown that urinary tract and vaginal infections have an improved management rate when lactobacillus and bifidobacterium multi-species probiotics are used.

    Probiotics are live bacteria which have been shown to reduce inflammation in the gastrointestinal tract. They also reduce intestinal permeability and influence serotonin and melatonin production in the gut.

    So since the human gut contains 10 times more bacteria than all the human cells in our body, keeping a healthy balance of bacteria in the gut is critical for digestive wellness.

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    Guest Pete Dixon


    Can you offer any articles relating to gut health after a celiac has stopped ingesting gluten?

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    Maria Lerario
    Celiac.com 11/17/2015 - For most people, when they think of gluten, the first thing that comes to mind is bread. And for most people with celiac or a gluten sensitivity, that is what we miss most.
    While people with celiac or gluten sensitivity may never be able to experience the wide selection or soft texture that "glutenous" bread offers, there are still some tasty gluten-free bread options available at most grocery stores. In order to find the best gluten-free bread options, I went to my local Giant Eagle and tried all of the gluten-free bread available and explored four main aspects: taste, texture, price, and variety.
    The three brands of gluten-free bread offered at Giant Eagle were Schar, Udi's, and Goodbye Gluten.
    In the variety category, Udi's offered the largest selection of bread with the choice of white bread, multigrain bread, cinnamon raisin bread, and millet-chia bread and omega flax and fiber bread. Udi's also offers a large variety of other products ranging from muffins and cookies, to pizza crusts and tortillas.
    While Udi's may have the largest variety of the three brands, Schar offered a few different kinds of bread as well, with a cinnamon raisin and multigrain option along with an assortment of rolls.
    In the category of price, Goodbye Gluten came in as the most inexpensive per ounce at $0.27 per ounce. Udi's was in the middle $0.37 per oz. and Schar was the most expensive of the three, coming in at $0.40 per oz.
    Now let's get down to business. Taste and texture—the two aspects that are hardest to get right when making gluten-free bread. In my opinion, Udi's won both categories with the tastiness, most normal textured bread. My only critique was the slices of bread weren't big enough! All three brands seemed to have their slices of bread on the smaller side, but Udi's bread seemed to be especially small.
    Although Udi's took the first prize in three of the four categories, that is not to say the other two brands were not good. I was impressed with all three brands, but my main critique covers the texture category.
    The Goodbye Gluten bread seemed to be very dense, and while most gluten-free bread crumbles more than normal, I felt that the Goodbye Gluten loaf broke easier than the other two. However, it was very moist, something that is hard to come by in gluten-free bread.
    With the Schar bread, I felt that it was a little dry and grainy rather than moist and chewy like normal gluten filled bread. However, I found that when I toasted the bread, it had a texture more consistent with normal toast.
    Overall, I was satisfied with all three brands, but Udi's was the favorite. With the texture and taste being spot on, I did not need much else to convince me, but the added bonus of the reasonable price and large variety made it the most desirable gluten-free bread available.

    Betty Wedman-St Louis, PhD, RD
    Celiac.com 12/01/2015 - Lectins are carbohydrate binding proteins which promote inflammatory responses like Crohn's disease, systemic lupus, asthma, and rheumatoid arthritis. They were discovered over 100 years ago and cause leaky gut and gastrointestinal dysbiosis yet the push for a plant-based diet focusing on legumes as meat alternatives has overlooked the damage lectins cause to the gut. Legumes offer inferior nutrition compared to animal proteins so toxicity needs to be considered when recommending food choices.
    As carbohydrate binding proteins, lectins are difficult to digest and irritate the brush border of the small intestine. Consequently, the tight junctions of the microvilli are damaged by prolamin and agglutinins which can lead to numerous disorders of the gastrointestinal tract and autoimmune diseases. Lectins are also a major contributor to leptin resistance which contributes to obesity.
    As described in The Handbook of Plant Lectins: Properties and Biomedical Applications (John Wiley, 1998), foods that contain these toxic lectins are members of the pea family and include peanuts, pigeon peas, soybeans, kidney beans, mung beans, lima beans, lentils, fava beans, chickpeas, carob, green and yellow peas. Green beans, snow peas and snap peas are usually well tolerated once the gut has been healed since they are immature protein sources with minor amounts of lectins.
    Lectins are found in other foods including grains and pseudo-grains. Grains are seeds from grasses—barley, oats, rice, rye, millet, wheat, teff, corn, kamut, spelt and possibly wild rice. Many gastroenterologists believe that the detrimental affects of lectins in grains are a factor in the development of celiac disease. Genetics and frequent consumption possibly play a critical role in the severity of sensitivities to these foods.
    Pseudo-grains are seeds from broadleafed plants—amaranth, buckwheat, chia, and quinoa. These seed products were geographically limited to specific populations and only available on a limited basis seasonally. But modern agriculture has greatly increased the consumption of these pseudo-grains because they can be labeled “gluten-free” because US standards allow any grain with less than 20 ppm gluten to be called gluten-free.
    Omitting toxic lectins—prolamins and agglutinins—from the diet is critical for gut health. Prolamins are predominately found in the seeds of plants. Gluten is the most widely known source of prolamins. They get their name from the high content of the amino acid proline. Research studies have shown that the prolamins in quinoa, corn and oats can cause damage to the digestive tract in people with celiac disease, yet these grains are frequently included in a gluten-free diet.
    Aggltinins are named for their ability to cause clumping of red blood cells. The most recent example of how this toxic lectin works is the bioterrorism threat caused from ricin. Ricin is the compound in castor beans that is so toxic that only tiny amounts are needed to cause death. Agglutinins are found on the seed coatings of grains and pseudo-grains and serve to protect the seed from fungus growth. Genetically modified crops—wheat, corn, soybeans—have higher amounts of agglutinins to insure higher yields.
    A leaky gut is harmful to the innate and adaptive immune systems. Toxic lectins cause inflammation and induce cytokine production. As few as five soaked, uncooked kidney beans can lead to gut distress for the raw foodies while 1 tablespoon of peanut butter leads to peanut agglutinins entering the bloodstream soon after consumption.
    Paolo Zatto and Pamela Zambenedetti from Padova, Italy studied lectins, microglia and Alzheimer's Disease (AD) as reported in Lectins and Pathology, 2000. The microglia of 10 AD brains stained intensely for agglutinins. Their research concluded that the glycation reaction seen in AD from lectins may serve as a significant factor in amyloid plaque development and disease progression.
    Bacteria overgrowth in the gut is associated with a wide variety of diseases- septicemia, pulmonary infections, enteropathies. Adhesion of pathogenic bacteria to epithelial cells in the gut can be a critical first stage in the infectious disease process. Michele Mouricout and Bruno Vedrine of Limoges, France described how lectins cause adhesion of numerous bacterial strains to intestines, brain tissues, urinary tract, lung and corneal cells. Their research is reported in Lectins and Pathology, 2000 illustrates the mosiac effect of how agglutinins cause tissue damage.
    Even though lectins have been identified for decades, little interest has been shown by biological and medical science. Since they are so widely distributed in foods consumed daily, lectins may finally become recognized as partners in the pathogenesis of diseases like cancer. Galectin-3 (gal 3) galactoside-binding lectin is found on the surface of most cancer cells and has been reported to promote angiogenesis. Lectins are not oncogenes but they help in cancer progression once initiated. Some are implicated in adhesion while others cause metatasis.
    Isn't it about time that nutrition science took a closer look at the lectin levels in foods consumed daily and customize the diet for lectin sensitivity to better manage inflammation and auto immune diseases? The higher intact of GMO food in the diet, the more lectins are consumed. Without food labeling of GMOs, consumers will continue to be misled and many will remain sick.

    Dr. Ron Hoggan, Ed.D.
    Celiac.com 12/08/2015 - Is the rate of food sensitivity and allergy growing? Or are we just more concerned about it because children experience anaphylactic crisis, sometimes even dying from exposure to peanuts, strawberries, and all the other foods that most of us think of as harmless? Even if the rates are growing, what is the cause? And should we, in the gluten sensitive community, be concerned about developing such allergies? After all, celiac patients were often told that there was no greater risk of developing IgE food allergies among those with celiac disease than is experienced by the general population (1, 2). I was certainly told this, on more than one occasion, by apparently well qualified medical practitioners. Yet, more recent research is showing that those with any autoimmune disease, including celiac disease, have a much greater risk of developing such allergies (3). Unfortunately, we still have more questions than answers. Nonetheless, the issue really does warrant exploration, especially among those who are gluten sensitive. Further, since the numbers of those with non-celiac gluten sensitivity remain controversial, we can also look at the issue from another perspective.
    For instance, a study of childhood IgE allergy frequency, at a center in Texas devoted to treating allergies and similar ailments, the investigators looked at antibody reactions to cow's milk, eggs, fish, peanuts, sesame, shellfish, soy, tree nuts, and wheat. They reported that the rate of all of these allergies combined had almost tripled (from 3% to 8%) in only five years (4). That is a startling rate of increase. If this finding can be applied more broadly, it should be alarming.
    However, another research group at Cornell University in Ithaca, New York, reported that childhood emergency department visits for food allergy reactions remained stable over a nine year period, while adult visits for food allergy reactions declined over this same time period (5). The central thrust of their report appears to be that we have an improving understanding of how to manage our own and our children's allergic reactions, so emergency room visits are becoming, relatively less frequent. This may simply signal that allergies are becoming so common that, as a culture, we are becoming better versed in how to avoid or manage mild allergic manifestations.
    Yet another group of investigators in Australia state that there has been a "dramatic rise in the prevalence of IgE-mediated food allergy over recent decades, particularly among infants and young children " (6). They go on to suggest that this increase may be due to "the composition, richness and balance of the microbiota that colonize the human gut during early infancy" (6). They further assert that IgE food allergies are connected to an impaired barrier function of epithelial cells that line the intestinal wall, in combination with immune dysregulation (6).
    Still others assert that the increase in allergies may be tied to climate change via several factors including "variability of aeroallergens, food allergens and insect-based allergic venoms" (7).
    Martin Blazer, M.D., in his book titled Missing Microbes argues that overuse of antibiotics may be at the root of both the increase in food allergies, as well as the increasing prevalence of celiac disease, through disrupting the gut microbiome and selection for antibiotic-resistant strains of microbes (8).
    Some or all of the foregoing theories may well have a legitimate influence on our growing rates of allergies. As I see it, however, the various theories postulated to explain these increasing rates have left out one powerful dietary trend that has also accompanied these increases in IgE food allergy prevalence. For instance, compromised intestinal barrier function is a well documented feature of gluten grain consumption, although it is greatest in the context of celiac disease. The increased release of zonulin, triggered by eating gluten grains, may also be a critical factor in the development and persistence of the disease process, especially in cases of celiac disease, type 1 diabetes, rheumatoid arthritis, ankylosing spondylitis, Crohn's disease, systemic lupus erythematosus, and about one quarter of cases of multiple sclerosis (9, 10).
    In the gut, gluten triggers increased release of zonulin, which weakens the junction between the epithelial cells that form the intestinal walls, and usually provide a protective barrier where these cells connect (11). The "gap" between these cells, caused by increased zonulin release, allows undigested proteins and peptides to bypass the cells that usually transport digested particles from the intestine to the bloodstream. Partly digested proteins, small peptides, also move through these epithelial cells, following the same path that fully digested food particles follow. However, according to Dr. Fasano, those are usually so degraded that they don't trigger antibody production (9). Thus, the leaky gut that has long been associated with celiac disease, and is often seen as a characteristic of, but not restricted to this ailment, is a critical stage in the development of this illness. This leakiness is, as most readers will know, reversed by a gluten-free diet.
    We are now seeing, in the peer reviewed medical literature, a wide range of ailments being identified as manifestations of undigested food proteins being "leaked" into the circulatory system. Further, there is a dose-dependent relationship between increasing gut permeability and increased gluten consumption, both in celiac disease and in other forms of autoimmunity (12). If this dose-dependent relationship also applies to many of those with other sensitivities, at admittedly lower levels of permeability (13), and if that is the dynamic that underlies much of the increasing trend of IgE food allergies, we should be seeing the rates of these allergies continue to rise in the general population. And, if we continue with our gluten gluttony, who can say how many ailments are associated with gluten consumption and increased zonulin release?
    It is also possible, perhaps even probable, that some of us experience increased zonulin release into the bloodstream, rather than into the intestinal lumen. If so, those peoples' epithelial linings of lungs, nasal passages, and blood brain barriers, may be more compromised than those individuals who primarily experience a leaky gut. By weakening these other barriers, they may invite other ailments that are less obviously triggered by gluten and other food proteins.
    Dr. Alessio Fasano has stated that new understandings of zonulin's role in autoimmunity, inflammation, and some cancers, "suggests that the autoimmune process can be arrested if the interplay between genes and environmental triggers is prevented by reestablishing [sic] the intestinal barrier function" (9). An animal study showed that AT1001, an experimental drug that blocks the action of zonulin, protected against autoimmune attack on pancreatic islet cells (9) which produce insulin. A human study of twenty-one subjects, reported similar findings (14).
    While it is true that intestinal infections have also been shown to induce zonulin release in the gut, the issue of microbes may not be as large a factor as it at first appears. When bacteria colonize our intestines, there are three possible outcomes: First, the infection may run rampant and kill us, thus solving the problem in a most undesirable manner. Second, and much more likely, we may take antibiotics and deplete or eliminate these infectious agents in our intestines. Third, and most likely, a combination of our immune systems, other microbes resident in our gut, antibiotics, and other, possibly unknown factors, may quickly or slowly bring the infectious agent under control. By reducing its numbers sufficiently that it won't pose a serious threat to our well being, and the harmful impact of these microbes has been muted.
    The second and third possibilities will be both the most common and most desirable. Also, as soon as the microbe in question is under control, zonulin release should be diminished to a point where it is either a minor factor in triggering continued zonulin release or, because it has been eradicated, the microbe will become irrelevant to zonulin release. On the other hand, for as long as we consume gluten, zonulin continues to be released, thus disrupting tight junctions in the intestinal, pulmonary, sinus, and other mucosal membranes, permitting allergens to reach our circulatory systems, ultimately giving rise to the growing prevalence of dangerous allergies that may sometimes manifest in anaphylactic reactions.
    The most important issue here seems to be the impact of gluten consumption on zonulin release, along with its impact on several protective barriers in the body, weakening them at the previously tight junctions between their cells. These include the blood brain barrier, which usually protects the brain from impurities and antibodies in the blood. It also includes the mucosa that line the lungs and nasal passages that protect us from airborne toxins and microbes. When that barrier is compromised, small particles from the air that we breathe will reach our circulation and trigger immune reactions...also known as allergies.
    Perhaps the most important barrier is in the digestive tract. It is made up of several variants of mucosa that protect the tissues of the gastrointestinal tract from toxins and the unwanted particles in our foods and beverages (well, most of them anyway). This, it seems to me, is the crux of our growing crisis with environmental allergies and the elevated zonulin levels that sometimes accompany them. And we can't even begin to combat this dynamic without first understanding it better.
    In the meantime, adding AT1001 to gluten-containing flours might be useful. Conversely, the media voices that are selling the idea that a gluten-free diet is an expensive fad might soon see research that reveals the gluten-free diet as an excellent prophylactic against developing IgE allergies, a variety of cancers, autoimmunity, some psychiatric illnesses, and many neurological diseases. In the interim, we can only use our own best judgement and decide for ourselves. Would the dietary products of gluten grains really be that great a loss to the palate? Is it a reasonable trade-off to risk falling prey to all of the potential consequences that come to us through elevated release of zonulin?
    More compellingly, perhaps, Professor Loren Cordain's assertion that humans have not had enough time to become fully adapted to eating cereal grains, especially as a dominant portion of our diet (15), appears to gain considerable support from the discovery and characterization of zonulin. Further, although some European, Asian, and northern African genes may have had as much as 15,000 years to adapt to this food source, most of the world's inhabitants have had a much shorter time to adapt. These are periods that are most appropriately measured in centuries and decades. The assumption that gluten grains can be safely consumed by all humans, because we have been eating them for "thousands of years" is unlikely to be true for most of the world's current population, and may represent a Eurocentric perspective.
    Csorba S, Jezerniczky J, Ilyés I, Nagy B, Dvorácsek E, Szabó B. Immunoglobulin E in the sera of infants and children. Acta Paediatr Acad Sci Hung. 1976;17(3):207-14. Greco L, De Seta L, D'Adamo G, Baldassarre C, Mayer M, Siani P, Lojodice D. Atopy and coeliac disease: bias or true relation? Acta Paediatr Scand. 1990 Jun-Jul;79(6-7):670-4. Fraser K, Robertson L. Chronic urticaria and autoimmunity. Skin Therapy Lett. 2013 Nov-Dec;18(7):5-9. Amin AJ, Davis CM. Changes in prevalence and characteristics of IgE-mediated food allergies in children referred to a tertiary care center in 2003 and 2008. Allergy Asthma Proc. 2012 Jan-Feb;33(1):95-101. Clark S, Espinola JA, Rudders SA, Banerji A, Camargo CA. Favorable trends in the frequency of U.S. emergency department visits for food allergy, 2001-2009. Allergy Asthma Proc. 2013 Sep-Oct;34(5):439-45. Molloy J, Allen K, Collier F, Tang ML, Ward AC, Vuillermin P. The potential link between gut microbiota and IgE-mediated food allergy in early life. Int J Environ Res Public Health. 2013 Dec 16;10(12):7235-56. Bielory L(1), Lyons K, Goldberg R. Climate change and allergic disease. Curr Allergy Asthma Rep. 2012 Dec;12(6):485-94. Blazer M. Missing Microbes. Harper Collins, Toronto, Canada, 2014. Fasano A. Zonulin and its regulation of intestinal barrier function: the biological door to inflammation, autoimmunity, and cancer. Physiol Rev. 2011 Jan;91(1):151-75. Yacyshyn B, Meddings J, Sadowski D, Bowen-Yacyshyn MB. Multiple sclerosis patients have peripheral blood CD45RO+ B cells and increased intestinal permeability. Dig Dis Sci. 1996 Dec;41(12):2493-8. Tripathi A, Lammers KM, Goldblum S, Shea-Donohue T, Netzel-Arnett S, Buzza MS, Antalis TM, Vogel SN, Zhao A, Yang S, Arrietta MC, Meddings JB, Fasano A. Identification of human zonulin, a physiological modulator of tight junctions, as prehaptoglobin-2. Proc Natl Acad Sci U S A. 2009 Sep 29;106(39):16799-804. Fasano A. Leaky gut and autoimmune diseases. Clin Rev Allergy Immunol. 2012 Feb;42(1):71-8. Drago S, El Asmar R, Di Pierro M, Grazia Clemente M, Tripathi A, Sapone A,Thakar M, Iacono G, Carroccio A, D'Agate C, Not T, Zampini L, Catassi C, Fasano A. Gliadin, zonulin and gut permeability: Effects on celiac and non-celiac intestinal mucosa and intestinal cell lines. Scand J Gastroenterol. 2006 Apr;41(4):408-19. Paterson BM, Lammers KM, Arrieta MC, Fasano A, Meddings JB. The safety, tolerance, pharmacokinetic and pharmacodynamic effects of single doses of AT-1001 in coeliac disease subjects: a proof of concept study. Aliment Pharmacol Ther. 2007 Sep 1;26(5):757-66. Cordain L. Cereal Grains: Humanity's Double-Edged Sword. in Simopoulos AP (ed): Evolutionary Aspects of Nutrition and Health. Diet, Exercise, Genetics and Chronic Disease. World Rev Nutr Diet. Basel, Karger, 1999, vol 84, pp 19–73

    Yvonne Vissing Ph.D.
    Celiac.com 02/02/2016 - Thanksgiving dinner is one of the culinary highlights of the year. Family and friends join together to share a blessed moment when they give thanks for each other and for homes, jobs, and the opportunity to live comfortable lives. We may give thanks for peace, decent weather, surviving illness, or just making it through another day.
    This is all done around the celebration of a food feast. Food is of central importance to social bonding and sharing a sense of community. As we all eat from the same platters and serve from the same bowls, there is a one-ness, a unity between us. But for folks who have celiac or who can't eat gluten, there is a sense of exclusion when relegated to a "separate but equal" dining system.
    People who have no problem eating anything and everything often fail to consider how hard it is for people who need to be super-careful about what they consume. When they have gone to great expense to buy festive foods, and after they've expended significant time planning the perfect plates, it is understandable that they get frustrated when others won't eat what they've prepared. What they may not remember is that there is a big difference between "won't" and "can't". Will-not implies a preference—and in food-terms it means wrinkling up your nose over something that doesn't strike your fancy. Can-not implies the hard truth that if one eats something, they could get sick. Won't is a choice—can't occurs when there is no choice. So when people do not eat a festive food, is it because they can't or won't? The usual default is to assume won't. But for people who are gluten-free, the answer is can't.
    Going gluten-free at Thanksgiving can be tough because it's so keenly associated with memories. Some of them are sensory, like remembering the smells of fresh-baked pumpkin pie or roasted turkey wafting out of the oven. Others are emotional, such as laughing with grandma while kneading bread that they family will soon lunge to smother with melting butter, or chopping up onions, celery, and chestnuts for dressing with Aunt Molly. For folks who once weren't gluten-free, certain foods evoke desire. We all have emotional trigger-foods. What's yours? One year we were invited to a colleague's Thanksgiving dinner and the hostess asked everyone, "What is the one food that if you don't have it for Thanksgiving, you would feel sad about?" It was a thoughtful question. After we all confessed she then told us that was the item we were to bring.
    When you're going to a pot-luck type of Thanksgiving dinner where everyone is bringing something, it's dietary roulette for someone with celiac. It's gambling at its finest. What are the chances that you can eat a dish? Does the cook appear conscientious and trustworthy or make you ask "am I feeling lucky?" enough to try that dish? Eating in collective settings lowers the risk of getting glutened when everyone knows you've got dietary issues and they're openly attentive to them. The risk is greater when you're with people you don't know well, or those who aren't as careful as they seem. Culinary posers prevail during the holidays. Some stop at the deli and put the food into their own bowls and cover them with aluminum foil to make it appear they made it themselves (I know—I have in fact done this). We have no idea what's really in the food because we didn't make it ourselves. Others lie about the dish's ingredients. They may innocently fib because they don't know what's safe and what's not for someone who has to go gluten-free—or they could tell only partial truth, like I did long ago about whether I put cream in a pumpkin soup when someone was lactose intolerant. Back then, I wrongly assumed that if they didn't know, they couldn't tell, so they wouldn't put up a fuss and then I wouldn't get embarrassed. I didn't know then what I know now. Even well-intended people may screw up when it comes to telling the truth, the whole truth, and nothing but the truth about what's in food or how it was prepared.
    Preparing a gluten-free Thanksgiving dinner that is absolutely safe and delicious for everyone to eat is easy. Here's a menu and recipes that will help you to create a meal that everyone is thankful for! It focuses on foods of the season, especially apples and the family of squashes. It is inclusive and delicious, and will give everyone one less thing to worry about as we instead focus on gratitude.
    A Gluten-Free Thanksgiving Dinner Menu
    When folks are milling around before a meal, it's nice to put out appetizers that they can nibble on. Usually these are very sharable, so making sure they are safe for someone with celiac is essential. So don't put out anything that could lead to cross-contamination. Here is our favorite tried-and-true appy:
    Artichoke Dip
    This is so easy and delicious as not to be believed!
    2 -3 cans of artichokes, cut into small pieces
    1 red pepper, diced
    Swiss, Cheddar, Parmesan, Muenster, and other cheeses of your liking
    Salt, pepper, onion flakes
    gluten-free crackers
    Spray a low casserole dish. In a bowl, mix in the cut artichokes, pepper, and pieces of cheeses. Add in the spices; only a little salt and more pepper, as the cheeses are usually salty and the artichokes could have been processed with some. Probably there will be salt on the crackers, so you don't want to kill this dish with it. Pour in the mixture into the casserole and heat until bubbly. Serve with only gluten free crackers or veggie sticks. . Part of the fun is dipping in a bowl together, so make sure if people double-dip that everyone is safe!
    Option: some people like to add spinach or cream cheese to their dip. It's not my way, but the popularity of spinach-artichoke dips conveys that it may be right for you!
    Soup is warm, comforting, and sets the stage for what's to come. Here are two recipes from which you can choose that are sure to whet the whistle of people for dishes to come!
    Apple Kale Soup
    Apples are abundant in autumn, and I created this dish in desperation to use foods that I had in the fridge on a day when the chill started to go through my bones. As a child I didn't understand kale, but now know it's a flexible, healthy and friendly vegetable.
    2-3 apples, peeled and sliced and diced 2/3 bag of fresh kale, or a hearty bunch cut into small pieces 1 purple onion, diced 1/3 pound of bacon (maple bacon is an especially good choice) 16 oz chicken broth (have another can handy if you want it) Salt, pepper Olive oil Plain nonfat yogurt Directions:
    Saute the onion and bacon in a little olive oil until they are brown and crispy. Add in a little broth, then the kale, which will shrink up immediately. Then add the apples in, along with the rest of the broth. Season with salt and pepper and let it simmer awhile on medium-low heat. I think a creamy looking soup is elegant, so I recommend spooning out the mixture into a food processor to make it smooth. Then return to the pan, adding more broth if you want. When that is done, add in the secret ingredient—plain yogurt. It will give it a creamy consistency and a little zing. You have to play with the amount of broth, yogurt and mixture to create a soup the consistency you like. It is an unusual soup that is tasty and sure to garner compliments.
    Gluten-Free Pumpkin Squash Soup
    In contrast to the previous soup recipe with is savory, this is a sweet soup recipe.
    2 cans pumpkin 1 small diced onion 1 medium butternut squash, cubed 3 cups chicken broth 1 teaspoon butter 2 tablespoons gluten-free flour or cornstarch 2 Tablespoon brown sugar 1 cup + half-and-half Salt, pepper, ginger, cinnamon to taste Directions:
    Saute the onions and squash in butter. Mash the squash when it is soft. Add to the chicken broth and simmer. Stir in the canned pumpkin. Mix gluten-free flour/cornstarch, butter, sugar, and spices. Fold in cream last. Heat but do not boil. You can garnish with a few slivered almonds if you want.
    While my mama had many culinary talents, the salads she made weren't her specialty, to say the least. Her "green" salad consisted of iceberg lettuce with tomatoes thrown on top, or we might enjoy a Waldorf salad that had red-delicious apples cut up, some celery and pecans that she mixed with Miracle Whip. It took me years to understand that salads could be the best part of a meal. Here are substitutions for what mama didn't know about!
    Diversity Salad
    Salads are most enjoyable with they contain a mixture of ingredients. You are the artist in the kitchen and get to decide what ingredients in what proportions. Here are our suggestions of items to consider: Baby spinach, romaine lettuce, and spring greens are the base of the salad, but don't rely on this to be the biggest ingredient. Using plenty of other vegetables will make every bite an experience, each mouthful different than the bite before. Add liberal amounts of carrots, tomatoes, onions, cucumber, and peppers, cut in various shapes and types. We love radishes, celery, sprouts, broccoli, cauliflower, and fresh mushrooms, but not everyone agrees. Avocado, beets and asparagus are other vegetables that may be questionable; while we like them, not everyone does. We are sensitive to the palate of our guests and modify the salad ingredients to please them. Leafy vegetables like kale, arugula, cabbage, chicory, watercress can make a salad interesting. Likewise, using fresh basil, cilantro, parsley and other herbs create tastes that give each salad a different flavor. Do you like roasted red peppers? Artichoke hearts? Banana pepper slices tossed into a salad can be delightful if you like that kind of spiciness. Olive varieties are endless. We recommend putting out different types of dressings so people have choice. For examples of easy and delicious dressings, there is a list for you to consider in our book Going Gluten Free.
    Waldorf Salad
    This salad can be anything but boring!
    The base:
    Toasted walnuts or pecans – toasting gives them a nice crunch that adds to the texture of the dish. Apples—I like flavorful crispy kinds, unpeeled so the color shines out. Red? Green? Combination? You choose! You also get to choose how to slice them. Hunks, thin slivers, slices—you're in charge. I rather like them slivered—they seem more delicate for an elegant meal. Directions:
    Celery—Cut it in slender shreds.
    Seedless Grapes or Dried Cranberries—Historically, grapes were the ingredient selected in the original Waldorf Astoria recipe. You can certainly keep tradition and use them. I like grapes to eat but not as fond of them in salads, so I prefer dried cranberries. I live in New England and using them at this time of year seems right. The dried berries add another texture and bright color to the dish.
    Optional: Some folks like to add thin sliced red or green peppers or even a few scallions.
    This is the make-or-break part of this salad. Mayonnaise is traditional, but today has been sidelined by the use plain yogurt or sour cream. Many people use a combination. I veer away from mayo in preference is a thinner, lighter dressing. Others add a tablespoon of fresh lemon juice mixed with a little honey. If you're into mustard, you may want to add a teaspoon, but no more or you will kill the dressing. It will need a little salt and pepper. Have handy some fresh mint leaves or parsley for garnish. Don't forget to serve it on some leafy lettuce. The lettuce bottom helps make the rest of the salad work even better!
    Main Dishes
    Turkey is by far the main dish at most Thanksgiving dinners. Every year, recipes seem to get more complex, like Turduckins or deep fried turkeys. Here is our recipe—it's simple, delicious, and healthy.
    Roasted Turkey
    Turkey Salt, pepper, paprika Butter Can of turkey/chicken broth Directions:
    Choose your turkey to your liking—some people like 20 pound birds with legs attached, others prefer a turkey breast and forgo the dark meat. Whatever you pick, you must decide whether to live the skin on or off. I always pull it off. It's an emotionally wrenching thing to do, but it's much healthier and makes for a tastier and prettier dish (in my opinion). I put the bird in a roasting pan that has some broth on the bottom. This keeps the bird moist as it cooks and it catches the natural juices and becomes the base for awesome gravy later on.
    Then I butter the bird a bit to enhance flavor and to help the spices stick. Heavily salt, pepper and add paprika to the exterior of the bird. There are many different types of paprika and some are quite spicy, so judge accordingly. Paprika makes the bird brown beautifully. Put a lid or aluminum foil over the bird and bake at 425F degrees for an hour or several more, depending on the size of the bird. This will enable the bird to cook through (nothing worse than raw poultry!) and not over-brown on top. After it appears that the bird is done on the inside, then remove the foil/lid and let it brown on top. You can baste it with some of the broth to keep it moist. When the bird is golden brown, you can take it out and eat it steaming hot. Add some corn starch, salt and pepper to the broth, whisk over medium heat, and make gravy to go on mashed potatoes if you like. This is a simple recipe that is sure to please!
    I was a vegetarian for two decades and know how awesome non-meat holiday dishes can be. Tofurky never quite worked for me. Here is one of our favorite dishes - but it's not safe for vegans because it contains both eggs and cheese. Sorry about that! We can't be all things to all people—but at least we are honestly transparent.
    Holiday Cheesy-Nut Delight
    30 oz. cottage cheese 1 purple onion, diced 5 eggs 1 cup grated cheddar cheese 1 cup chopped walnuts 3-4 cups gluten-free corn flakes or rice krispies Butter Directions:
    Salt, pepper, A-1 sauce, optional dried minced onions or dried parsley
    Saute the onion in butter until transparent and lovely. In a bowl, add cottage cheese, eggs, cheddar, walnuts, a tablespoon of A-1 sauce, and spices to your liking. Then stir in the cooked onions. Finally, add in the cereal. The mixture should be moist but not runny. Poor it into a greased pan—you can make them into a loaf, muffins, or cook in a casserole pan. The size of the pan you use determine how long you will cook this dish. It should take around a half-hour for most size pans. The dish will be firm and browned, but don't overcook it or it will be dry. It cuts nicely when cool. If you want to make it look even fancier, you can drizzle a bechemal sauce over it with parsley garnish. This is a family favorite, and we hope you will enjoy it too.
    Chop 1 onion sauted in butter, add to mixture of eggs, cottage cheese, cheddar cheese, walnuts, salt, pepper, a T of A-1 and mix in 4 cups of gluten-free Corn Flakes. Baked in a greased pan at 350F degrees for an hour. Let sit 10 minutes uncovered before cutting.
    What's Thanksgiving dinner without stuffing? Here's our version—tweak to your heart's content!
    Gluten-Free Thanksgiving Stuffing
    Leftover gluten free bread, any type, torn into small pieces Olive Oil Celery and Onion, cut into small pieces Chicken/turkey broth Salt, Pepper, Sage, Rosemary, Thyme, Parsley Butter Optional: Nuts (your choice), dried fruit (apricots, apples), sausage, or vegetables Directions:
    I gave up cooking the stuffing in the turkey ages ago. It turns out much better if you bake it in pan of its own. Saute until soft onion and celery in butter. Spray a cooking dish. In a bowl, mix the bread pieces, pour in the celery/onion mixture, add spices, and enough chicken broth to make it very moist. Add in whatever other ingredients you want. Personally, the simpler the better. Sometimes too much is overkill. Bake at 350 until it is firm with a light crust on top – then enjoy!
    Let's face it—the sky's the limit when it comes to making amazing gluten-free vegetable dishes. I learned that color was important for a festive meal, so ours is white (potatoes), yellow (corn), orange (pumpkin), and red (cranberries or tomatoes in the salads). Instead doing green beans, broccoli, or asparagus—all that are awesome—we've given you a less familiar Brussel sprout recipe.
    Mashed Potatoes
    What could be easier? Scrape clean potatoes, cut them into hunks and toss them into boiling water until soft. Then mash. Add butter, milk, salt and pepper. Make more than you think you're going to need—they are going to disappear.
    Baked Corn
    Take 2 cans of gluten-free creamed corn, a can of whole kernel corn, drained, and mix them together in a bowl with 2-3 eggs, 1/3 cup corn starch, dried minced onion, salt and pepper and a smidge of butter. Pour into a greased casserole and bake until it is bubbly.
    Bacony-Delicious Brussel Sprouts
    Bacon Brussel sprouts Olive oil Salt/pepper Balsamic vinegar Parmesan cheese Directions:
    Cut the bacon into little pieces and fry them in olive oil. When brown, toss in the sprouts—slice the bigger ones. They will brown beautifully—you may want to put a lid on them for a few minutes to make sure they cook through and become soft. Then add salt, pepper, a tablespoon of balsamic vinegar and sprinkle with parm cheese. These are bound to be a hit!
    I'll be honest with you—as a child I learned to bake some of the most fantastic yeast wheat bread imaginable. gluten-free bread has, by far, been the hardest thing for me to recreate with satisfaction. My solution? Don't try to do it in a way that recreates child memories. Find a new way. You may be pleased with the result.
    Pumpkin Muffins
    This is my own concoction. As you may recall from our cooking model described in our book, Going Gluten Free, I don't measure ingredients. I work with them in a zen method until they seem to be right. So I'll give you my recipe, with the recommendation that you tweak it as your intuition dictates!
    1 can pumpkin 1 1/2 c. gluten-free flour 1 c sugar ½ c. canola oil 2-3 eggs 1 tsp baking powder and 1 tsp baking soda Cinnamon Chocolate chips Directions:
    Mix all of the ingredients together in a bowl, then pour into greased muffin tins. Make sure the tins are gluten-free safe. We have a special pan that nothing else goes in, and recommend you do the same. It's better to spray the muffin cups instead of using papers—the muffins actually come out much prettier. They rise high and are beautiful and tasty. These are our autumn delights!
    3 c. gluten-free flour ½ c. canola oil + oil for cooking 1-2 eggs 1 tsp baking powder Salt Optional ingredients: sliced scallions, cheese, herbs, or whatever pleases you! Directions:
    Mix the ingredients together in a bowl while the oil heats in a skillet. Drop a large spoonful of the batter into the oil, and flip when it browns. When both sides are golden, remove and add more fritter batter into the pan. Serve hot with butter. They satisfy the need for bread without having to feel dissatisfied with trying to make a loaf and expect it to be like traditional wheat bread. Maybe one day the recipes and products will be there for that, but not today. This is a satisfactory substitute, to be sure!
    Every meal needs to end with a food that ritually signifies the meal is over. By this time, bellies are usually full and dessert needs to be symbolic more than substantive. It should look pretty and taste sweet. Here is the quintessential Thanksgiving dessert.
    Pumpkin Pie
    This is the traditional dessert and so easy to make.
    Gluten-Free Pie Crust:
    1 can pumpkin 2/3 c. sugar 3 eggs 1 can evaporated milk Cinnamon, nutmeg Butter A tsp of corn starch Directions:
    The nice thing about making a gluten-free pumpkin pie for Thanksgiving dinner is that all the ingredients in the pie are naturally gluten-free, except for the pie crust. So follow the directions on the can for pie, or use the directions here. Mix all the ingredients in a bowl and then put into a gluten-free crust (your choice of frozen or homemade) and bake until it is firm and beautiful. Don't burn it! It will firm up as it sits for a few minutes. Top with ice cream or whip cream, and maybe a garnish of chocolate or glazed nuts. Serve with coffee or tea, and enjoy the closing conversation.
    This meal should leave everyone feeling satiated and satisfied. What most people are grateful for at Thanksgiving is to just sit together with loved ones and share good conversation, laughter, and connection. What they eat isn't nearly as important as eating together. But with a menu like this, everyone can eat together and feel treated to a gourmet meal fit for a king. And it's fun to show nonbelievers how scrumptious Going Gluten Free can be!

  • Recent Articles

    Jefferson Adams
    Celiac.com 04/20/2018 - A digital media company and a label data company are teaming up to help major manufacturers target, reach and convert their desired shoppers based on dietary needs, such as gluten-free diet. The deal could bring synergy in emerging markets such as the gluten-free and allergen-free markets, which represent major growth sectors in the global food industry. 
    Under the deal, personalized digital media company Catalina will be joining forces with Label Insight. Catalina uses consumer purchases data to target shoppers on a personal base, while Label Insight works with major companies like Kellogg, Betty Crocker, and Pepsi to provide insight on food label data to government, retailers, manufacturers and app developers.
    "Brands with very specific product benefits, gluten-free for example, require precise targeting to efficiently reach and convert their desired shoppers,” says Todd Morris, President of Catalina's Go-to-Market organization, adding that “Catalina offers the only purchase-based targeting solution with this capability.” 
    Label Insight’s clients include food and beverage giants such as Unilever, Ben & Jerry's, Lipton and Hellman’s. Label Insight technology has helped the Food and Drug Administration (FDA) build the sector’s very first scientifically accurate database of food ingredients, health attributes and claims.
    Morris says the joint partnership will allow Catalina to “enhance our dataset and further increase our ability to target shoppers who are currently buying - or have shown intent to buy - in these emerging categories,” including gluten-free, allergen-free, and other free-from foods.
    The deal will likely make for easier, more precise targeting of goods to consumers, and thus provide benefits for manufacturers and retailers looking to better serve their retail food customers, especially in specialty areas like gluten-free and allergen-free foods.

    Jefferson Adams
    Celiac.com 04/19/2018 - Previous genome and linkage studies indicate the existence of a new disease triggering mechanism that involves amino acid metabolism and nutrient sensing signaling pathways. In an effort to determine if amino acids might play a role in the development of celiac disease, a team of researchers recently set out to investigate if plasma amino acid levels differed among children with celiac disease compared with a control group.
    The research team included Åsa Torinsson Naluai, Ladan Saadat Vafa, Audur H. Gudjonsdottir, Henrik Arnell, Lars Browaldh, and Daniel Agardh. They are variously affiliated with the Institute of Biomedicine, Department of Microbiology & Immunology, Sahlgrenska Academy, University of Gothenburg, Gothenburg, Sweden; the Institute of Clinical Sciences, Sahlgrenska Academy at the University of Gothenburg, Gothenburg, Sweden; the Department of Pediatric Gastroenterology, Hepatology and Nutrition, Karolinska University Hospital and Division of Pediatrics, CLINTEC, Karolinska Institute, Stockholm, Sweden; the Department of Clinical Science and Education, Karolinska Institute, Sodersjukhuset, Stockholm, Sweden; the Department of Mathematical Sciences, Chalmers University of Technology, Gothenburg, Sweden; the Diabetes & Celiac Disease Unit, Department of Clinical Sciences, Lund University, Malmö, Sweden; and with the Nathan S Kline Institute in the U.S.A.
    First, the team used liquid chromatography-tandem mass spectrometry (LC/MS) to analyze amino acid levels in fasting plasma samples from 141 children with celiac disease and 129 non-celiac disease controls. They then crafted a general linear model using age and experimental effects as covariates to compare amino acid levels between children with celiac disease and non-celiac control subjects.
    Compared with the control group, seven out of twenty-three children with celiac disease showed elevated levels of the the following amino acids: tryptophan; taurine; glutamic acid; proline; ornithine; alanine; and methionine.
    The significance of the individual amino acids do not survive multiple correction, however, multivariate analyses of the amino acid profile showed significantly altered amino acid levels in children with celiac disease overall and after correction for age, sex and experimental effects.
    This study shows that amino acids can influence inflammation and may play a role in the development of celiac disease.
    PLoS One. 2018; 13(3): e0193764. doi: & 10.1371/journal.pone.0193764

    Jefferson Adams
    Celiac.com 04/18/2018 - To the relief of many bewildered passengers and crew, no more comfort turkeys, geese, possums or other questionable pets will be flying on Delta or United without meeting the airlines' strict new requirements for service animals.
    If you’ve flown anywhere lately, you may have seen them. People flying with their designated “emotional support” animals. We’re not talking genuine service animals, like seeing eye dogs, or hearing ear dogs, or even the Belgian Malinois that alerts its owner when there is gluten in food that may trigger her celiac disease.
    Now, to be honest, some of those animals in question do perform a genuine service for those who need emotional support dogs, like veterans with PTSD.
    However, many of these animals are not service animals at all. Many of these animals perform no actual service to their owners, and are nothing more than thinly disguised pets. Many lack proper training, and some have caused serious problems for the airlines and for other passengers.
    Now the major airlines are taking note and introducing stringent requirements for service animals.
    Delta was the first to strike. As reported by the New York Times on January 19: “Effective March 1, Delta, the second largest US airline by passenger traffic, said it will require passengers seeking to fly with pets to present additional documents outlining the passenger’s need for the animal and proof of its training and vaccinations, 48 hours prior to the flight.… This comes in response to what the carrier said was a 150 percent increase in service and support animals — pets, often dogs, that accompany people with disabilities — carried onboard since 2015.… Delta said that it flies some 700 service animals a day. Among them, customers have attempted to fly with comfort turkeys, gliding possums, snakes, spiders, and other unusual pets.”
    Fresh from an unsavory incident with an “emotional support” peacock incident, United Airlines has followed Delta’s lead and set stricter rules for emotional support animals. United’s rules also took effect March 1, 2018.
    So, to the relief of many bewildered passengers and crew, no more comfort turkeys, geese, possums or other questionable pets will be flying on Delta or United without meeting the airlines' strict new requirements for service and emotional support animals.

    Celiac disease is an autoimmune condition that affects around 1% of the population. People with celiac disease suffer an autoimmune reaction when they consume wheat, rye or barley. The immune reaction is triggered by certain proteins in the wheat, rye, or barley, and, left untreated, causes damage to the small, finger-like structures, called villi, that line the gut. The damage occurs as shortening and villous flattening in the lamina propria and crypt regions of the intestines. The damage to these villi then leads to numerous other issues that commonly plague people with untreated celiac disease, including poor nutritional uptake, fatigue, and myriad other problems.
    Celiac disease mostly affects people of Northern European descent, but recent studies show that it also affects large numbers of people in Italy, China, Iran, India, and numerous other places thought to have few or no cases.
    Celiac disease is most often uncovered because people experience symptoms that lead them to get tests for antibodies to gluten. If these tests are positive, then the people usually get biopsy confirmation of their celiac disease. Once they adopt a gluten-free diet, they usually see gut healing, and major improvements in their symptoms. 
    Symptoms of celiac disease can range from the classic features, such as diarrhea, upset stomach, bloating, gas, weight loss, and malnutrition, among others.
    Celiac disease can often less obvious symptoms, such fatigue, vitamin and nutrient deficiencies, anemia, to name a few. Often, these symptoms are regarded as less obvious because they are not gastrointestinal in nature. You got that right, it is not uncommon for people with celiac disease to have few or no gastrointestinal symptoms. That makes spotting and connecting these seemingly unrelated and unclear celiac symptoms so important.
    Currently, most people diagnosed with celiac disease do not show symptoms, but are diagnosed on the basis of referral for elevated risk factors. 

    Gluten intolerance is a generic term for people who have some sort of sensitivity to gluten. These people may or may not have celiac disease. Researchers generally agree that there is a condition called non-celiac gluten sensitivity. That term has largely replaced the term gluten-intolerance. What’s the difference between celiac disease and non-celiac gluten-sensitivity? 
    Gluten triggers symptoms and immune reactions in people with celiac disease. Gluten can also trigger symptoms in some people with NCGS, but the similarities largely end there.

    There are four main differences between celiac disease and non-celiac gluten sensitivity:
    No Hereditary Link in NCGS
    Researchers know for certain that genetic heredity plays a major role in celiac disease. If a first-degree relative has celiac disease, then you have a statistically higher risk of carrying genetic markers DQ2 and/or DQ8, and of developing celiac disease yourself. NCGS is not known to be hereditary. Some research has shown certain genetic associations, such as some NCGS patients, but there is no proof that NCGS is hereditary. No Connection with Celiac-related Disorders
    Unlike celiac disease, NCGS is so far not associated with malabsorption, nutritional deficiencies, or a higher risk of autoimmune disorders or intestinal malignancies. No Immunological or Serological Markers
    People with celiac disease nearly always test positive for antibodies to gluten proteins. Researchers have, as yet, identified no such antobodies or serologic markers for NCGS. That means that, unlike with celiac disease, there are no telltale screening tests that can point to NCGS. Absence of Celiac Disease or Wheat Allergy
    Doctors diagnose NCGS only by excluding both celiac disease, an IgE-mediated allergy to wheat, and by the noting ongoing adverse symptoms associated with gluten consumption. WHAT ABOUT IRRITABLE BOWEL SYNDROME (IBS) AND IRRITABLE BOWEL DISEASE (IBD)?
    IBS and IBD are usually diagnosed in part by ruling out celiac disease. Many patients with irritable bowel syndrome are sensitive to gluten. Many experience celiac disease-like symptoms in reaction to wheat. However, patients with IBS generally show no gut damage, and do not test positive for antibodies to gliadin and other proteins as do people with celiac disease. Some IBS patients also suffer from NCGS.

    To add more confusion, many cases of IBS are, in fact, celiac disease in disguise.

    That said, people with IBS generally react to more than just wheat. People with NCGS generally react to wheat and not to other things, but that’s not always the case. Doctors generally try to rule out celiac disease before making a diagnosis of IBS or NCGS. 
    Crohn’s Disease and celiac disease share many common symptoms, though causes are different.  In Crohn’s disease, the immune system can cause disruption anywhere along the gastrointestinal tract, and a diagnosis of Crohn’s disease typically requires more diagnostic testing than does a celiac diagnosis.  
    Crohn’s treatment consists of changes to diet and possible surgery.  Up to 10% of Crohn's patients can have both of conditions, which suggests a genetic connection, and researchers continue to examine that connection.
    Is There a Connection Between Celiac Disease, Non-Celiac Gluten Sensitivity and Irritable Bowel Syndrome? Large Number of Irritable Bowel Syndrome Patients Sensitive To Gluten Some IBD Patients also Suffer from Non-Celiac Gluten Sensitivity Many Cases of IBS and Fibromyalgia Actually Celiac Disease in Disguise CELIAC DISEASE DIAGNOSIS
    Diagnosis of celiac disease can be difficult. 

    Perhaps because celiac disease presents clinically in such a variety of ways, proper diagnosis often takes years. A positive serological test for antibodies against tissue transglutaminase is considered a very strong diagnostic indicator, and a duodenal biopsy revealing villous atrophy is still considered by many to be the diagnostic gold standard. 
    But this idea is being questioned; some think the biopsy is unnecessary in the face of clear serological tests and obvious symptoms. Also, researchers are developing accurate and reliable ways to test for celiac disease even when patients are already avoiding wheat. In the past, patients needed to be consuming wheat to get an accurate test result. 
    Celiac disease can have numerous vague, or confusing symptoms that can make diagnosis difficult.  Celiac disease is commonly misdiagnosed by doctors. Read a Personal Story About Celiac Disease Diagnosis from the Founder of Celiac.com Currently, testing and biopsy still form the cornerstone of celiac diagnosis.
    There are several serologic (blood) tests available that screen for celiac disease antibodies, but the most commonly used is called a tTG-IgA test. If blood test results suggest celiac disease, your physician will recommend a biopsy of your small intestine to confirm the diagnosis.
    Testing is fairly simple and involves screening the patients blood for antigliadin (AGA) and endomysium antibodies (EmA), and/or doing a biopsy on the areas of the intestines mentioned above, which is still the standard for a formal diagnosis. Also, it is now possible to test people for celiac disease without making them concume wheat products.

    Until recently, biopsy confirmation of a positive gluten antibody test was the gold standard for celiac diagnosis. It still is, but things are changing fairly quickly. Children can now be accurately diagnosed for celiac disease without biopsy. Diagnosis based on level of TGA-IgA 10-fold or more the ULN, a positive result from the EMA tests in a second blood sample, and the presence of at least 1 symptom could avoid risks and costs of endoscopy for more than half the children with celiac disease worldwide.

    Currently the only effective, medically approved treatment for celiac disease is a strict gluten-free diet. Following a gluten-free diet relieves symptoms, promotes gut healing, and prevents nearly all celiac-related complications. 
    A gluten-free diet means avoiding all products that contain wheat, rye and barley, or any of their derivatives. This is a difficult task as there are many hidden sources of gluten found in the ingredients of many processed foods. Still, with effort, most people with celiac disease manage to make the transition. The vast majority of celiac disease patients who follow a gluten-free diet see symptom relief and experience gut healing within two years.
    For these reasons, a gluten-free diet remains the only effective, medically proven treatment for celiac disease.
    There is currently no enzyme or vaccine that can replace a gluten-free diet for people with celiac disease.
    There are enzyme supplements currently available, such as AN-PEP, Latiglutetenase, GluteGuard, and KumaMax, which may help to mitigate accidental gluten ingestion by celiacs. KumaMax, has been shown to survive the stomach, and to break down gluten in the small intestine. Latiglutenase, formerly known as ALV003, is an enzyme therapy designed to be taken with meals. GluteGuard has been shown to significantly protect celiac patients from the serious symptoms they would normally experience after gluten ingestion. There are other enzymes, including those based on papaya enzymes.

    Additionally, there are many celiac disease drugs, enzymes, and therapies in various stages of development by pharmaceutical companies, including at least one vaccine that has received financial backing. At some point in the not too distant future there will likely be new treatments available for those who seek an alternative to a lifelong gluten-free diet. 

    For now though, there are no products on the market that can take the place of a gluten-free diet. Any enzyme or other treatment for celiac disease is intended to be used in conjunction with a gluten-free diet, not as a replacement.

    The most common disorders associated with celiac disease are thyroid disease and Type 1 Diabetes, however, celiac disease is associated with many other conditions, including but not limited to the following autoimmune conditions:
    Type 1 Diabetes Mellitus: 2.4-16.4% Multiple Sclerosis (MS): 11% Hashimoto’s thyroiditis: 4-6% Autoimmune hepatitis: 6-15% Addison disease: 6% Arthritis: 1.5-7.5% Sjögren’s syndrome: 2-15% Idiopathic dilated cardiomyopathy: 5.7% IgA Nephropathy (Berger’s Disease): 3.6% Other celiac co-morditities include:
    Crohn’s Disease; Inflammatory Bowel Disease Chronic Pancreatitis Down Syndrome Irritable Bowel Syndrome (IBS) Lupus Multiple Sclerosis Primary Biliary Cirrhosis Primary Sclerosing Cholangitis Psoriasis Rheumatoid Arthritis Scleroderma Turner Syndrome Ulcerative Colitis; Inflammatory Bowel Disease Williams Syndrome Cancers:
    Non-Hodgkin lymphoma (intestinal and extra-intestinal, T- and B-cell types) Small intestinal adenocarcinoma Esophageal carcinoma Papillary thyroid cancer Melanoma CELIAC DISEASE REFERENCES:
    Celiac Disease Center, Columbia University
    Gluten Intolerance Group
    National Institutes of Health
    U.S. National Library of Medicine
    Mayo Clinic
    University of Chicago Celiac Disease Center

    Jefferson Adams
    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