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Found 6 results

  1. Betty Wedman-St Louis, PhD, RD

    Phosphates in Processed Foods Equals Inflammation in GI Tract

    Celiac.com 07/18/2016 - Dietary phosphorus occurs naturally in dairy foods, animal meats, and legumes but according to the Institute of Medicine, high levels of phosphorus can be a contributor to cardiovascular, kidney and osteoporosis disorders. While phosphorus is considered an essential nutrient, the increased amounts found in processed foods via additives like anti-caking agents, stabilizers and leavening agents or acidifiers does not have to be stated on the nutrition label. Individuals following a gluten-free diet need to consider the health implications of phosphates found in processed foods eaten regularly in their diet. Reducing carbonated beverages is the best way to reduce phosphorus levels in the diet. Extra attention needs to be paid to the ingredient statement on foods. Ingredient statements may include these declarations: tri-calcium phosphate, tri-magnesium phosphate, disodium phosphate, di-potassium phosphate. Just because the label states "natural" or "organic" does not mean it is a healthy food for daily consumption. Fresh is best! Here is a guide to where phosphates can be found in gluten-free processed foods: Baked goods- cake mixes, donuts, refrigerated dough (pyrophosphates are used for leavening and as a dough "improver") Beverages- phosphoric acid in colas (acidulant), pyrophosphate in chocolate milk to suspend cocoa, pyrophosphate in buttermilk for protein dispersion, tri-calcium phosphate in orange juice for fortification, tetra-sodium phosphate in strawberry flavored milk to bind iron to pink color Cereals- phosphate in dry cereals to aid flow through extruder, fortification of vitamins Cheese- phosphoric acid in cottage cheese to set acidification, phosphate in dips, sauces, cheese slices and baked chips for emulsifying action and surface agent Imitation Dairy Products (non-dairy products)- phosphate as buffer for smooth mixing into coffee and as anti-caking agent for dry powders Egg Products- phosphate for stability and color + foam improvement Ice Cream- pyrophosphate to prevent gritty texture Meat Products- tri-phosphate for injections into ham, corned beef, sausage, franks, bologna, roast beef for moisture Nutrition Bars & Meal Replacement Drinks- phosphates for fortification and microbiological stability Potatoes- phosphate in baked potato chips to create bubbles on the surface, pyrophosphate in French fries, hash browns, potato flakes to inhibit iron induced blackening Poultry- tri-phosphate for moisture and removal of salmonella and campylobacter pathogens Pudding & Cheesecakes- phosphate to develop thickened texture Seafood- tri-phosphate in shrimp for mechanical peeling, pyrophosphate in canned tuna and crab to stabilize color and crystals, surimi (crab/sea sticks) tri-phosphate and pyrophosphate as cryoprotectant to protein {surimi contains gluten and is not recommended for gluten-free diets] Hyperphosphate levels can contribute to muscle aches, calcification of coronary arteries and skeletal issues. Many food companies do not provide phosphorus analysis information because it is not required on the label but here is a representative sample of phosphorus levels in some commonly consumed on a gluten-free diet. Peanuts (1 ounce) 150 mg Yogurt (1 cup) 300 mg M&M Peanuts (1.74 oz pkg) 93 mg Rice Krispies Cereal (1 cup) 200 mg Dietary recommendations for an adult for Phosphorus is 800 to 1000 mg.
  2. Celiac.com 03/24/2014 - Two new studies have confirmed colonization of gluten-degrading bacteria in the human mouth and in the upper gastrointestinal tracts respectively. Both studies come out of the Department of Periodontology and Oral Biology, Boston University Henry M. Goldman School of Dental Medicine in Boston, Massachusetts. The research teams included Maram Zamakhchari, Guoxian Wei, Floyd Dewhirst, Jaeseop Lee, Detlef Schuppan, Frank G. Oppenheim, and Eva J. Helmerhorst. Gluten is notoriously hard for mammals to digest, because gliadin proteins resist mammalian proteolytic enzymes in the gut, so researchers wanted to find sources of gluten-digesting microbial enzymes from the upper gastro-intestinal tract. These microbial enzymes have the potential to neutralize the gluten peptides that act as celiac disease triggers. In the first study the researchers assessed proteolytic activity in suspended dental plaque towards a) gliadin-derived paranitroanilide(pNA)-linked synthetic enzyme substrates a mixture of natural gliadins and c) synthetic highly immunogenic gliadin peptides (33-mer of α2-gliadin and 26-mer of γ-gliadin). In addition, they conducted gliadin zymography to establish the approximate molecular weights and pH activity profiles of the gliadin-degrading oral enzymes and performed liquid iso-electric focusing to determine overall enzyme iso-electric points. Their results provide the first known evidence of gluten-degrading microorganisms associated with the upper gastro-intestinal tract. Such microorganisms may play a hitherto unappreciated role in the digestion of dietary gluten and thus protection from celiac disease in subjects at risk. In the second study, the team employed a selective plating strategy using gluten agar to obtain oral microorganisms with gluten-degrading capacity. They then used16S rDNA gene sequencing to carry out microbial speciations. To determine enzyme activity, they used gliadin-derived enzymatic substrates, gliadins in solution, gliadin zymography, and 33-mer a-gliadin and 26-mer c-gliadin immunogenic peptides. They separated fragments of the gliadin peptides by RP-HPLC, and structurally characterized them using mass spectrometry. They found that strains Rothia mucilaginosa and Rothia aeria showed high gluten-degrading activity. For example, gliadins (250 mg/ml) added to Rothia cell suspensions (OD620 1.2) degraded by 50% after 30 minutes of incubation. Importantly, the 33-mer and 26-mer immunogenic peptides were also cleaved, primarily C-terminal to Xaa-Pro-Gln (XPQ) and Xaa-Pro-Tyr (XPY). The major gliadin-degrading enzymes produced by the Rothia strains were 70–75 kDa in size, and the enzyme expressed by Rothia aeria was active over a wide pH range (pH 3–10). While the human digestive enzyme system lacks the capacity to cleave immunogenic gluten, such activities are naturally present in the oral microbial enzyme repertoire. Taken together, these studies suggest a potential for these bacteria to fuel the development of compounds that can degrade of harmful gluten peptides that trigger celiac disease in susceptible individuals. Source: PLoS One. 2011;6(9):e24455. doi: 10.1371/journal.pone.0024455. http://www.ncbi.nlm.nih.gov/pubmed/20948997
  3. Celiac.com 04/12/2010 - A team of researchers recently set out to look at connections between psoriasis, the liver, and the gastrointestinal tract. The team was made up of Paolo Gisondi, Micol Del Giglio, Alessandra Cozzi & Giampiero Girolomoni. They are associated with the Section of Dermatology and Venereology of the Department of Medicine, at the University of Verona, Italy. Psoriasis is a common chronic inflammatory, immune-mediated skin disease that is often tied to other disorders, including psoriatic arthropathy, chronic inflammatory bowel diseases, and cardio-metabolic disorders. Additionally, about 50% of all patients patients with psoriasis suffer from non-alcoholic fatty liver disease, from 0.2–4.3% suffer from celiac disease, and about one half of one percent suffer from Crohn's disease. These associated conditions may have some common genetic traits, as well as common inflammatory pathways, and their presence offers important implications in the global approach to treating psoriasis. In particular, common systemic antipsoriatic drugs might have a negative affect on associated cardio-metabolic conditions and nonalcoholic fatty liver disease, and may have important interactions with drugs commonly used to treat psoriasis. Moreover, the team emphasizes the importance of encouraging psoriasis patients to drastically improve their modifiable cardiovascular and liver risk factors, especially obesity, alcohol and smoking intake, because improvements could have positive impact on both the psoriasis and the patient's general well-being. Source: Dermatologic Therapy, Volume 23 Issue 2, Pages 155 - 159 - DOI: 10.1111/j.1529-8019.2010.01310.x
  4. Celiac.com 09/12/2011 - Exogenous enzymes are enzymes that are created outside of the body. Doctors use exogenous enzymes, usually orally, to treat several diseases, such as pancreatic insufficiency and lactose intolerance. Because these enzymes are protein-based, they can be inactivated and/or digested in the gastrointestinal (GI) tract. A research team recently established a convenient fluorescence-based test to measure the activity of therapeutic enzymes live and in real time in the GI tract. The research team included Gregor Fuhrmann and Jean-Christophe Leroux. They are affiliated with the Department of Chemistry and Applied Biosciences, Institute of Pharmaceutical Sciences in Zurich, Switzerland. To establish proof of their principle, the team applied their assay to proline-specific endopeptidases (PEPs), a group of enzymes recently proposed as adjuvant therapy for celiac disease, which is a very common immunogenetic enteropathy. To do so, they took a short PEP-specific peptide sequence from larger immunotoxic sequences of gluten. They then labeled each sequence with a fluorescent dye and a corresponding quencher. Once the enzyme sequence split, they dequenched the fluorescence emission and then used an live imaging system to detect the result. The team then evaluated PEPs originating from Flavobacterium meningosepticum (FM) and Myxococcus xanthus (MX) after oral administration in rats. While MX PEP could not split the peptide in the stomach, FM PEP showed significant gastric activity reaching 40–60% of the maximal live signal intensity. However, both enzymes produced similar fluorescence signals in the small intestine. Using an antacid significantly enhanced MX PEP’s gastric activity due to increased pH and/or inhibition of stomach proteases. By using this simple method, the team was able to observe differences in the live performance of PEPs, which could not be identified under laboratory conditions. This imaging method could be used for live study other oral enzymes and may prove useful in improving current treatments. Source: PNAS 108:9032-9037. DOI:10.1073/pnas.1100285108
  5. A team of Swiss researchers recently set out to examine the nature of T cell-mediated immuno-regulation in the gastrointestinal tract. The research team was made up of doctors L. Saurer and C. Mueller of the Institute of Pathology at the University of Bern in Switzerland. In the human intestinal tract, just a single layer of epithelial cells divides innate and adaptive immune effector cells from a wide array of antigens. Here, the immune system faces a tall task in accepting beneficial flora and dietary antigens while preventing the dissemination of potential pathogens. When the tightly controlled process of immune system reactions breaks down, harmful inflammation and damage may result. In light of this, a great deal of focus has shifted toward 'conventional' regulatory CD4+ T cells, including naturally occurring and adaptive CD4+ CD25+ Foxp3+ T cells, Th3 and Tr1 cells. However, control mechanisms in the intestinal mucosa are highly intricate, and include adaptations of non-haematopoietic cells and innate immune cells in addition to the presence of unconventional T cells with regulatory properties such as resident TCRγδ or TCRαβ CD8+ intraepithelial lymphocytes. In the study, L. Saurer and C. Mueller seek to provide an overview of the present body of knowledge on standard and non-standard regulatory T cell subsets (Tregs), with particular focus on clinical data and the potential role or malfunctioning of Tregs in four major human gastrointestinal diseases, i.e. inflammatory bowel diseases, celiac disease, food allergy and colorectal cancer. Their data confirms most of the findings derived from experimental animal models, and has implications for clinical immunology, food allergy, immunoregulation, immunotherapy, mucosal immunology, and regulatory T cell protocols. Their findings appear in the February 2009 issue of Allergy.
  6. Celiac.com 03/06/2009 - A report in the February 3rd issue of Digestive and Liver Disease highlights the present understanding of transglutaminase function in gastrointestinal and liver diseases and therapeutic strategies that target transglutaminase activities. A team of American and Italian researchers recently set out to review the current body of literature regarding transglutaminase function in gastrointestinal and liver diseases and therapeutic strategies that target transglutaminase activities. The research team was made up of doctors L. Elli, C.M. Bergamini, C.M. Bardella, and D. Schuppan. They are associated with one or more of the following: Center for Prevention and Diagnosis of Celiac Disease, Fondazione IRCCS Ospedale Maggiore Policlinico, Mangiagalli e Regina Elena, in Milan, Italy; the Department of Biochemistry, University of Ferrara, Via Luigi Borsari, Ferrara, Italy; the Department of Medical Sciences, University of Milan, Italy; and the Beth Israel Deaconess Medical Center and Harvard Medical School, Boston, USA. Their report in the February issue of Digestive and Liver Disease highlights the present understanding of transglutaminase function in gastrointestinal and liver diseases and therapeutic strategies that target transglutaminase activities. Transglutaminases are a group of eight presently recognized calcium-dependent enzymes that act as catalysts to cross-link or deamidate proteins. They play a role in key biological functions such as the healing of wounds, the repair of damaged tissue, fibro-genesis, apoptosis, inflammation and management of the cell cycle. Thus, they play a role in numerous key patho-mechanisms of autoimmune, inflammatory and degenerative diseases, a number of which involve the gastrointestinal system. Transglutaminase 2 is of central importance, as it is crucial to the pathogenesis of celiac disease, and influences inflammation and fibro-genesis in inflammatory bowel and chronic liver disease. The recent review has implications for celiac disease, collagen, Crohn's disease, extra-cellular matrix, gliadin, inflammatory bowel disease; NFkB, and ulcerative colitis. Dig Liver Dis. 2009 Feb 3.
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