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      Frequently Asked Questions About Celiac Disease   04/24/2018

      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 is Celiac Disease and the Gluten-Free Diet? 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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    PROLYL ENDOPROTEASE ENZYME MAY ALLOW PATIENTS WITH CELIAC DISEASE TO SAFELY EAT GLUTEN ON OCCASION


    Jefferson Adams

    Enzyme Quickly Breaks Down Wheat Protein


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    Celiac.com 05/23/2007 - The results of a study recently published in the journal Gut suggest that the enzyme prolyl endoprotease from Aspergillus niger (AN-PEP) taken along with meals might allow patients with celiac disease to safely consume gluten on occasion.

    The negative effects of celiac disease are due in large part to an immune response to gluten.

    Because proline-rich gluten proteins resist the digestive enzymes of the gastro-intestinal tract, they are very likely suspects in the generation of this immune response.

    A team of doctors in the Netherlands set out to assess the abilities of a post-proline cutting enzyme, prolyl endoprotease from Aspergillus niger (AN-PEP) in breaking down gluten. The research team was made up of doctors Cristina Mitea (1), Robert Havenaar (2), Jan Wouter Drijfhout (1), Luppo Edens (3), Liesbeth Dekking (1)* and Frits Koning (1).

    The study was not performed on actual celiac patients, but used a dynamic system that mimics the human gastrointestinal tract (TIM system). Using the TIM system, the team performed two experiments. The first used the TIM-system to process a slice of bread with and without the presence of AN-PEP. The second experiment used the TIM-system to process standard fast food items, again both with and without the presence of AN-PEP.

    Samples of the digesting food were taken from the TIM systems stomach, duodenum, jejunum and ileum compartments from zero to four hours after the beginning of the experiment. These samples were evaluated for levels of immunogenic peptides from gliadins and glutenins by monoclonal antibody based competition assays, Western blot analysis and proliferation T-cell assays.

    Results of both experiments showed that AN-PEP broke down gluten in the stomach so effectively that almost no gluten reached the duodenum compartment. Because these results show that AN-PEP is capable of speeding the breakdown of gluten in a gastrointestinal system that closely mimics live digestion, the team concluded that AN-PEP might offer celiac patients an opportunity to stray from their strict gluten free diets from time to time.

    Participating Institutions:
    1 Dept of Immunohematology and Blood Transfusion,
    Leiden University Medical Center, Leiden, Netherlands.
    2 TNO Quality of Life, Zeist, Netherlands
    3 DSM Food Specialties, Delft, Netherlands

    Gut. Published Online First: 9 May 2007. doi:10.1136/gut.2006.111609

    health writer who lives in San Francisco and is a frequent author of articles for Celiac.com.

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    Guest Cecily Baldwin

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    Thought this article was interesting and helpful, as I had been researching AN-PEP and was finding it hard to find anything other than totally clinical or repeat articles. Thanks for this one. Easy to read and understand.

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    admin

    Celiac.com 2/13/2003 - This new study emphasizes the importance of following a strict gluten-free diet, and getting regular follow-up biopsies after your diagnosis. It also speaks to the need to discover whether or not you may have additional food intolerance, such as to cows milk (casein), soy, corn, etc., as some of these can also cause intestinal damage similar to that of celiac disease. -Scott Adams

    Lee SK, Lo W, Memeo L, Rotterdam H, Green PH.
    Gastrointest Endosc 2003 Feb;57(2):187-91
    Current affiliations: Department of Surgical Pathology and Medicine, Columbia University College of Physicians and Surgeons, New York, New York.
    BACKGROUND: The diagnosis of celiac disease requires characteristic histopathological changes in an intestinal biopsy with clinical improvement in response to a gluten-free diet. Endoscopy with procurement of biopsy specimens is often performed to document response to the diet, but there are little data on the appearance of treated celiac disease. This study examined the endoscopic and histopathological appearance of the duodenum of patients with celiac disease whose diet was gluten-free.
    METHODS: A cohort of 39 adult patients (mean age 52 years, range 20-74 years) with biopsy-proven celiac disease was retrospectively reviewed. All had responded clinically to a gluten-free diet that they had maintained for a mean of 8.5 years (range 1-45 years). The endoscopic and histopathological appearances of the duodenal mucosa were reviewed. Blinded review of the diagnostic (initial) and post-treatment biopsy specimens was also performed to assess response of individual patients to the diet.
    RESULTS: The endoscopic appearance was normal in 23%, reduced duodenal folds were present in 46%, scalloping of folds in 33%, mucosal fissures in 44%, and nodularity in 33%. There was more than 1 abnormality present in 46%. Histology was normal in only 21%. The remainder had villous atrophy (69% partial, 10% total). Paired (diagnostic and follow-up) biopsy specimens were reviewed blindly for 12 patients. The mean (SD) intraepithelial lymphocyte count fell from 61 (22) to 38 (17) (normal
    CONCLUSIONS: Despite a good clinical response, abnormal endoscopic and histopathological appearances persist in the majority of patients with celiac disease treated with a gluten-free diet.
    PMID: 12556782

    admin
    J Pharmacol Exp Ther. 2004 May 13
    Piper JL, Gray GM, Khosla C. Stanford University.
    Celiac.com 11/28/2004 - A study by researchers at Stanford University looked at the ability of Prolyl endopeptidase (PEP)--a specific type of enzyme--to break down gliadin peptides in a living organism--rats. In an effort to determine whether a resistance to the break down of proteins by proteases enzymes is the cause of toxicity of the Pro- and Gln-rich peptides, the scientists analyzed the digestive resistance of a panel of alpha and gamma-gliadin peptides that are believed to induce gluten toxicity--all of which happen to be very resistant to gastric and pancreatic protease digestion--but can be broken down by intestinal brush border peptidases. The researchers determined that supplementation of PEP substantially reduced the concentrations of these peptides, and they determined a pharmacologically useful PEP dosage. According to the researchers: "This data verifies and extends our earlier proposal that gliadin peptides, while resistant to proteolysis, can be processed efficiently by PEP supplementation. Indeed, PEP may be able to treat Celiac Sprue by reducing or eliminating such peptides from the intestine."

    Jefferson Adams
    Celiac.com 06/03/2010 - Clinical presentation of celiac disease can vary considerably from patient to patient. Most patients with celiac disease present atypical symptoms. Moreover, most patients who present abdominal symptoms in primary care do not have celiac disease, and so diagnostic tests for celiac disease are not necessary and should be avoided.
    A team of researchers recently conducted a systematic review of diagnostic testing for celiac disease among patients with abdominal symptoms.
    The team included Daniëlle A. W. M. van der Windt, PhD; Petra Jellema, PhD; Chris J. Mulder, MD, PhD; C. M. Frank Kneepkens, MD, PhD; and Henriëtte E. van der Horst, MD, PhD. Their article appears in the Journal of the American Medical Association.
    The goal of the research was to review and summarize evidence on the performance of diagnostic tests for spotting celiac disease in adults who present abdominal symptoms in primary care or similar settings.
    To obtain initial data, the team search MEDLINE (from January 1966  through December 2009, and EMBASE from January 1947 through December 2009. They also conducted a physical search of references for additional relevant studies.
    The team chose cohort or nested case-control diagnostic studies which included adults presenting non-acute abdominal symptoms, which featured celiac disease prevalence of 15% or less, and in which the tests included gastrointestinal symptoms or serum antibody screens.
    Two independent reviewers conducted studies tool and data extraction. They then calculated sensitivities and specificities for each study and computed pooled estimates using bivariate analysis where there was clinical and statistical homogeneity.
    In all, the team included sixteen studies encompassing 6085 cases in their review.
    Specificity, sensitivity, and confidence intervals for predicting celiac disease varied with abdominal symptoms.  For patients presenting with classic diarrhea, for example, predictive sensitivity ranged from 0.27 to 0.86, while specificity ranged from 0.21 to 0.86.
    Pool estimates for 8 studies on IgA antiendomysial antibodies were 0.90, with a 95% confidence interval [CI] (0.80-0.95) for sensitivity and 0.99, with a 95% CI (0.98-1.00) for specificity, with a positive likelihood ratio [LR] of 171 and negative LR of 0.11.
    Pool estimates for IgA antitissue transglutaminase antibodies (7 studies) were 0.89, with a 95% CI (0.82-0.94) and 0.98 at 95% CI (0.95-0.99), respectively, with a positive LR of 37.7 and negative LR of 0.11.
    IgA and IgG antigliadin antibodies showed variable results, especially for sensitivity, which ranged from 0.46-0.87 for IgA, and from 0.25-0.93 for IgG.
    One recent study using deamidated gliadin peptides showed good specificity (0.94), but the target population offered limited supporting evidence.
    For adults who present abdominal symptoms in primary care or other unscreened settings, IgA antitissue transglutaminase antibodies and IgA antiendomysial antibodies offer high sensitivity and specificity for diagnosing celiac disease.
    SOURCE:  JAMA. 2010;303(17):1738-1746. doi:10.1001/jama.2010.549


    Jefferson Adams
    Celiac.com 08/10/2012 - A diagnosis of Celiac disease is measured mainly by an adverse response to gluten, yet there is very little in the way of data regarding gluten challenge in adults on a gluten-free diet.
    A research team recently studied the kinetics of histological, serological, and symptomatic responses to gluten challenge in adults with celiac disease.
    The research team included D. Leffler, D. Schuppan, K. Pallav, R. Najarian, J.D. Goldsmith, J. Hansen, T. Kabbani T, M. Dennis, and C.P. Kelly. They are affiliated with Beth Israel Deaconess Medical Center in Boston, Massachusetts.
    For their study, the team wanted to address a lack of data regarding the kinetics of responses to gluten, which causes assessment issues in clinical practice and research when gluten-challenge is performed.
    For their study, the researchers recruited twenty adults with biopsy-proven coeliac disease. For each participant, the team conducted two run-in visits followed by a 14-day gluten-challenge at a randomly assigned dose of 3 or 7.5 g of gluten/day.
    Patients visited study team doctors at 3, 7, 14 and 28 days after the start of their gluten challenge.
    The researchers performed duodenal biopsy during the run-in and at days 3 and 14 of gluten challenge.
    The team used two pathologists to measure villous height to crypt depth ratio (Vh:celiac disease) and intraepithelial lymphocyte (IEL) count/100 enterocytes. Upon each visit, the team also assessed antibodies to tissue transglutaminase and deamidated gliadin peptides, lactulose to mannitol ratio (LAMA) and any physical symptoms.
    Compared to the initial data, results after 14 days showed substantially lower Vh:celiac disease (2.2-1.1, p
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    The team concludes by noting that a 14-day gluten challenge at or above 3 g of gluten/day triggers cellular, tissue, and blood changes in most adults with celiac disease.
    These findings will help researchers create more accurate clinical trials, and show that many individuals will meet celiac diagnostic criteria after a basic 2-week gluten challenge.
    Source:
    Gut. 2012 May 22.

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    Tammy Rhodes
    Celiac.com 04/24/2018 - Did you know in 2017 alone, the United States had OVER TENS OF THOUSANDS of people evacuate their homes due to natural disasters such as fires, floods, hurricanes, tornadoes and tsunamis? Most evacuation sites are not equipped to feed your family the safe gluten free foods that are required to stay healthy.  Are you prepared in case of an emergency? Do you have your Gluten Free Emergency Food Bag ready to grab and go?  
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    Connie Sarros
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    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. 
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    Source:
    fdfworld.com

    Jefferson Adams
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    Source:
    PLoS One. 2018; 13(3): e0193764. doi: & 10.1371/journal.pone.0193764