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Found 4 results

  1. Celiac.com 06/22/2015 - Currently available digestive enzymes do not fully degrade gluten, and are thus of questionable use for people with celiac disease or gluten intolerance, say a team of researchers. Prior research had shown that post-proline cutting enzyme effectively degrade the immunogenic gluten peptides. Several existing digestive enzyme supplements claim to promote gluten degradation. The research team set out to assess the degradation of immunogenic gluten epitopes by currently available digestive enzymes. The team included G. Janssen, C. Christis, Y. Kooy-Winkelaar, L. Edens, D. Smith, P. van Veelen, and F. Koning. They are variously affiliated with the Department of Immunohematology and Blood Transfusion, Leiden University Medical Centre, Leiden, The Netherlands, DSM Food Specialties in Delft, The Netherlands, and DSM Food Specialties in South Bend, Indiana, USA. For their study, they assessed five commercially available digestive enzyme supplements along with purified digestive enzymes. They assessed these enzymes using enzyme assays and mass spectrometric identification. They monitored gluten epitope degradation using R5 ELISA, mass spectrometric analysis of the degradation products, and T cell proliferation assays. They found that the enzyme supplements leave the nine immunogenic epitopes of the 26-mer and 33-mer gliadin fragments largely intact. This is due to the high proline content of gluten molecules, which prevents gastrointestinal proteases from fully degrading them, leaving large proline-rich gluten fragments intact, including an immunogenic 33-mer from α-gliadin and a 26-mer from γ-gliadin. These latter peptides can trigger pro-inflammatory T cell responses resulting in tissue remodeling, malnutrition and a variety of other complications. In contrast, the pure enzyme AN-PEP effectively degraded all nine epitopes in the pH range of the stomach at much lower dose. From these results, the team concludes that most of the currently available digestive enzyme supplements are ineffective in degrading immunogenic gluten epitopes, but the AN-PEP do effectively degrade gliadin fragments. Source: PLoS One. 2015 Jun 1;10(6):e0128065. doi: 10.1371/journal.pone.0128065.
  2. Celiac.com 10/02/2015 - Many people with celiac disease or gluten-intolerance take digestive enzymes, hoping for some protection against accidental gluten-contamination. Post-proline cutting enzymes have been shown to effectively degrade the immunogenic gluten peptides and have been proposed as oral supplements. Several existing digestive enzyme supplements also claim to aid in gluten degradation. However, not all gluten proteins are the same. The gluten proteins that are particularly active in triggering an adverse immune reaction in celiac disease are known as immunogenic 33-mer from α-gliadin and a 26-mer from γ-gliadin. So, how effective are currently available digestive enzyme supplements ineffective in breaking down these specific gliadins that triggers immune reactions in people with celiac disease? A team of researchers recently set out to determine the effectiveness of such existing enzyme supplements in comparison with a well characterized post-proline cutting enzyme, Prolyl EndoPeptidase from Aspergillus niger (AN-PEP). The research team included G.Janssen, C. Christis, Y. Kooy-Winkelaar, L. Edens, D. Smith, P. van Veelen, and F. Koning. They are variously affiliated with the Department of Immunohematology and Blood Transfusion at Leiden University Medical Centre in Leiden, The Netherlands, DSM Food Specialties, Delft, The Netherlands, and DSM Food Specialties in South Bend, Indiana, USA. For their study, the team subjected each of the five commercially available digestive enzyme supplements along with purified digestive enzymes to 1) enzyme assays and 2) mass spectrometric identification. Gluten epitope degradation was monitored by 1) R5 ELISA, 2) mass spectrometric analysis of the degradation products and 3) T cell proliferation assays. Their findings show that, due to the high proline content of gluten molecules, gastrointestinal proteases are unable to fully degrade them leaving large proline-rich gluten fragments intact, including an immunogenic 33-mer from α-gliadin and a 26-mer from γ-gliadin. Basically, none of the currently available digestive enzyme supplements are effective in degrading immunogenic gluten epitopes. This means that these enzymes are not likely to be helpful to people with celiac disease. Share your thoughts in our comments section below. Source: PLoS One. 2015 Jun 1;10(6):e0128065. doi: 10.1371/journal.pone.0128065. eCollection 2015.
  3. Celiac.com 10/20/2010 - U.S. doctors and patients looking for accurate early diagnosis of celiac disease now have a state of the art celiac disease assay with a high level of sensitivity and specificity. The US Food and Drug Administration (FDA) has given 510(k) clearance for the first two fully automated gliadin tests featuring deamidated peptides for celiac disease. Manufactured by Phadia US, the tests, EliA GliadinDP IgA and EliA GliadinDP IgG, are designed to be used in conjunct with other laboratory and clinical findings in the early diagnosis of celiac disease. According to Gabi Gross, autoimmune franchise leader for Phadia US, "EliA GliadinDP IgA and EliA GliadinDP IgG will offer physicians who suspect a possible case of celiac disease, antibody tests with the lowest number of false positive results." This means less "unnecessary endoscopies and biopsies," she adds. EliA GliadinDP IgA and EliA GliadinDP IgG will offer antibody tests with the lowest number of false positive results for doctors who suspect a patient has celiac disease. The assays are optional on Laboratory Systems Phadia 100Є and Phadia 250 instruments with features like quick turnaround, monthly calibration, onboard instrument dilution, and a discrete single-well, random-access, nonmicrotiter plate format. Phadia also manufactures other approved CLIA moderately complex assays in the EliA autoimmune product line, including anticardiolipin IgG/IgM, anti-B2-glycoprotein 1 IgG/IgM, cyclic citrullinated peptide, tissue transglutaminase IgA/ IgG, gliadin IgA/IgG, dsDNA, antinuclear antibody screen, and ENA antibodies to the following antigens: Sm, U1RNP, RNP70, Ro, La, Scl-70, CENP, and Jo-1. Source: Medscape
  4. Celiac.com 03/05/2010 - A team of researchers recently studied therelationship between increased levels of antigliadin antibodies andintestinal barrier gene variants. The research team included V.M. Wolters, B. Z. Alizadeh, M. E. Weijerman, A. Zhernakova, I. M. vanHoogstraten, M. L. Mearin, M. C. Wapenaar, C.Wijmenga, M. W. Schreurs.They are affiliated with the Department of Pediatric Gastroenterology,UMC Utrecht, Utrecht, The Netherlands. Numerous genes may affectintestinal barrier function, including MAGI2, MYO9B, and PARD3, whichhave a close association with celiac disease. Gauging intestinalpermeability is tough to do, so researchers can test indirectly byusing antibodies against gliadin and Baker's yeast (anti-Saccharomycescerevisiae antibodies). The goal of the study was to determinewhether intestinal permeability, represented by antibodies againstgliadin, was connected to MAGI2, MYO9B, and PARD3. The teamanalyzed patients with Down syndrome, a population with suspectedincreased intestinal permeability. The team examined connectionsbetween AGA and ASCA. The team genotyped 126 Down syndromepatients for six single-nucleotide polymorphisms in MAGI2 (rs1496770,rs6962966, rs9640699), MYO9B (rs1457092, rs2305764), and PARD3(rs10763976). They then performed an allele dosage associationof these risk genes and AGA levels. They also found a strongcorrelation between AGA and ASCA (p < 0.01). Subjects withone or more risk genotypes showed lower average AGA levels (trend testp = 0.007) and made up a larger number of patients with normal AGAlevels (p = 9.3 x 10(-5)). Celiac-associated risk genotypesare associated with lower AGA values rather than higher AGA values.This all means that, regarding the increased prevalence of elevated AGAin patients with Down syndrome, there are other immunologic factors atplay. These may involve altered induction and/or maintenance oftolerance. Source: Hum Immunol. 2010 Feb 3.
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