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Celiac.com 04/20/2017 - More people than ever are following a gluten-free diet, but does the diet carry health risks that could cause harm in the long run? That's a very possible scenario, according to a report published in the journal Epidemiology. The report presents strong data to suggest that numerous gluten-free food staples contain high levels of toxic metals, which means that many gluten-free eaters could face higher risks for cancer and other chronic illnesses. Moreover, the US studies both reveal that people who follow a gluten-free diet have twice as much arsenic in their urine as those who eat a non-gluten-free diet. They also have 70 per cent more mercury in their blood, along with high levels of other toxic metals, such as lead and cadmium. Clearly the report invites further study to determine if these potentially negative effects are merely statistical, or if they are actually represented in corresponding numbers of gluten-free dieters. So, look for more study to see if people eating gluten-free are actually having higher rates of cancer and other toxic metal-related disorders. Meantime, you may be able to mitigate negative effects of a gluten-free diet by choosing products with lower levels of toxic metals. California-grown rice, for example seems to have lower levels compared to Chinese rice. If you follow a gluten-free diet for medical reasons, keep an eye out for symptoms related to toxic metal exposure, and consult a doctor if you think you are experiencing such symptoms. Read more at: Celiac.com. Does a Gluten-free Diet Mean Higher Arsenic and Mercury Levels? Read more at The Daily Mail.
Jefferson Adams posted an article in Celiac Disease & Gluten Intolerance ResearchCeliac.com 03/09/2009 - A team of researchers based in Finland recently demonstrated for the first time that B. lactis probiotic bacteria are capable of shielding epithelial cells from cellular damage caused by gliadin exposure. The research team was made up of doctors K. Lindfors, T. Blomqvist, K. Juuti-Uusitalo, S. Stenman, J. Venäläinen, M. Mäki and K. Kaukinen. They are associated with the Paediatric Research Centre for the Medical School of the Finland’s University of Tampere, the Department of Peadiatrics, and the Department of Gastroenterology and Alimentary Tract Surgery at Tampere University Hospital, and the Department of Pharmacology and Toxicology of the Finland’s University of Kuopio. In people with celiac disease, wheat gliadin causes serious intestinal symptoms and damages the small-bowel mucosa. Untreated, this can leave the individual at risk of developing various cancers and numerous associated conditions. Most all of this can be reversed or prevented if detected and treated early enough. Currently, the only effective treatment for celiac disease is a strict life-long gluten-free diet. However, a 100% gluten-free diet is nearly impossible to maintain, with so many gluten-free products containing trace amounts of gluten. Because of this, people with celiac disease face regular gluten contamination. Also because of this, acceptable alternatives are desirable. Earlier studies have indicated that probiotic bacteria might be used in sourdough fermentation to induce the hydrolysis of celiac toxic gluten in food manufacturing, and thereby benefit people with celiac disease. Although several studies have addressed the ability of probiotic bacteria to detoxify gliadin after an extensive incubation period, the team found none that investigated whether various live probiotic bacteria can inhibit gliadin-induced toxic effects directly on epithelial cells. In this study the team set out to determine whether probiotics Lactobacillus fermentum or Bifidobacterium lactis might block the toxic effects of gliadin in intestinal cell culture conditions. To assess the degree to which live probiotics were able to block peptic-tryptic digested gliadin-induced degradation of human colon cells Caco-2, the team measured epithelial permeability by transepithelial resistance, actin cytoskeleton arrangements by the extent of membrane ruffling and expression of tight junctional protein ZO-1. B. lactis inhibited the gliadin-induced increase dose-dependently in epithelial permeability, and, at higher concentrations totally eliminated the gliadin-induced reduction in transepithelial resistance. That is, B. lactis decreased or eliminated the compromise in cell-wall resistance caused by gliadin. This means that B. lactis overcame the mechanism that gives rise to the decreased cell resistance and the increased permeability that occurs during an adverse reaction to wheat gliadin. The B. lactis strain also interfered with the creation of membrane ruffles in Caco-2 cells caused by gliadin exposure. Furthermore, it also shielded the tight junctions of Caco-2 cells from the toxic effects of gliadin, as shown by the way in which ZO-1 is expressed. The researchers concluded that live B. lactis bacteria might achieve partial to full blockage of gliadin toxicity gluten/gliadin-induced damage in the small-intestinal mucosa of people with celiac disease, and that it merits further study concerning its potential as a dietary supplement to guard against any silent damage associated with accidental gluten-contamination in celiac disease. Clinical and Experimental Immunology, 152: 552–558
Jefferson Adams posted an article in Gluten-Free Grains and FloursCeliac.com 06/30/2010 - Presently, the only proven treatment for celiac disease is a lifelong gluten-free diet. As part of a gluten-free diet, people with celiac disease are encouraged to avoid consuming foods containing rye, along with avoiding wheat and barley. However, there is surprisingly little evidence to document the adverse effects of rye in cases of celiac disease. To address this deficiency, a team of clinicians set out to determine conclusively whether rye should be excluded from the celiac diet. The team included S. M. Stenman, K. Lindfors, J. I. Venäläinen, A. Hautala, P. T. Männistö, J. A. Garcia-Horsman, A. Kaukovirta-Norja, S. Auriola, T. Mauriala, M. Mäki, and K. Kaukinen They are affiliated variously with the Department of Pediatrics, and the Pediatric Research Center of the Medical School University of Tampere, the Department of Gastroenterology and Alimentary Tract Surgery at Tampere University Hospital, the Department of Pharmacology and Toxicology, the Department of Pharmaceutical Chemistry at the University of Kuopio, the Division of Pharmacology and Toxicology, the Division of Pharmaceutical Chemistry at the University of Helsinki, and Technical Research Centre of Finland. The goal of the team was to determine whether rye secalin triggers toxic reactions in vitro in intestinal epithelial cell models to the same degree as wheat gliadin. Moreover, they examined whether the harmful effects of secalin can be reduced by germinating cereal enzymes from oat, wheat and barley to hydrolyze secalin into short fragments as a pretreatment. The data showed that secalin did trigger toxic reactions in intestinal Caco-2 epithelial cells in a similar manner to gliadin. Secalin triggered epithelial cell layer permeability, tight junctional protein occludin and ZO-1 distortion, and actin reorganization. High-performance liquid chromatography and mass spectroscopy (HPLC-MS), showed that germinating barley enzymes best degraded the secalin and gliadin peptides. Further in vitro analysis showed that germinating barley enzyme pretreatment ameliorated all toxic secalin-triggered reactions. From these results, the team concludes that germinating enzymes from barley offer efficient degradation of rye secalin. In future, these enzymes might be utilized as a novel medical treatment for celiac disease or in food processing in order to develop high-quality celiac-safe food products. Such enzyme treatments might pave the way for either new treatments for celiac disease, or, new methods of processing rye for production of new, celiac-safe foods. SOURCE: Clinical & Experimental Immunology DOI:10.1111/j.1365-2249.2010.04119.x
Scott Adams posted an article in Frequently Asked QuestionsMost of the wheat grain and of white flour is made up of starch granules. Starch granules make up about 75% of grain or of white flour. In the processes used to make wheat starch, a small amount of the gluten protein (actually mostly the gliadin fraction, but not entirely), sticks to the surface of the starch granules. The amount depends on the washing method, how many times the granules are washed, and factors like that. Wheat starch can be made very low in surface protein and it is only the surface protein that is of concern (there are some internal granule proteins, but we are pretty sure that they are not gluten proteins). For more information on Codex wheat starch visit the Codex Wheat Starch page.