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  • Scott Adams
    Scott Adams

    Prolyl-Endopeptidase Enzymes (PEP) Not Practical in the Detoxification of Gliadin Peptides in Celiac Disease

    Reviewed and edited by a celiac disease expert.

    Gastroenterology Volume 129, Issue 3, Pages 786-796 (September 2005)

    Celiac.com 09/14/2005 - Researchers have long thought that the resistance of gliadin prolamines to digestive enzymes is a primary contributor to celiac disease—which leads to the intestinal permeability and inflammation in those who are at risk. Taking prolyl-endopeptidase enzymes (PEP) orally has been proposed and explored as a possible treatment for celiac disease (including extensive research done at Stanford Universitys Celiac Sprue Research Foundation – CSRF). In an effort to determine the feasibility of such a treatment, researchers in France conducted both in vitro (outside a living organism) and ex vivo—using biopsy specimens of active celiac disease patients—studies on the effects of PEP on gliadin peptides.


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    For the in vitro studies the researchers used radio-reverse-phase high-performance liquid chromatography and mass spectrometry to analyze the degradation by PEP of 3H-labeled gliadin peptides 56-88 (33-mer). In the ex vivo studies the researchers added PEP and 3H-peptides together onto the mucosal side of duodenal biopsy specimens that were mounted in Using chambers, and the peptide transport and digestion were analyzed using radio-reverse-phase high-performance liquid chromatography.

    The results indicate that in both in vitro and ex vivo studies the gliadin peptides were only partly degraded by 20 mu/ml of PEP. This concentration of PEP decreased the quantity of intact gliadin peptides (31-49 and 56-88) that crossed the intestinal biopsy specimens, but did not prevent the intestinal passage of toxic or immunostimulatory metabolites—for this the researchers determined that PEP concentrations of at least 500 mu/ml for at least 3 hours was required to achieve full detoxification of gliadin peptides, and thus prevent intestinal transport of active fragments—unfortunately this finding virtually eliminates PEP as a possible treatment option for those with celiac disease.

    The researchers conclude optimistically, however: "After prolonged exposure to high concentrations of PEP, the amount of immunostimulatory gliadin peptides reaching the local immune system in celiac patients is decreased. These results provide a basis to establish whether such conditions are achievable in vivo (in living organisms)."


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    Guest Ramesh Shah, Ph.D.

    Posted

    I agree with your observations; however, your conclusion that .."unfortunately this finding virtually eliminates PEP as a possible treatment option for those with celiac disease". I have seen better and more convincing results with an ANPEP preparation (with which I am familiar with) in in vivo simulation model (TIM) and also very encouraging and complete degradation of gluten in the stomach even before it reaches duodenum. Only time will tell, if it helps gluten intolerant individuals and also celiac sufferers.

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    Celiac.com's Founder and CEO, Scott was diagnosed with celiac disease  in 1994, and, due to the nearly total lack of information available at that time, was forced to become an expert on the disease in order to recover. Scott launched the site that later became Celiac.com in 1995 "To help as many people as possible with celiac disease get diagnosed so they can begin to live happy, healthy gluten-free lives."  In 1998 he founded The Gluten-Free Mall which he sold in 2014. He is co-author of the book Cereal Killers, and founder and publisher of Journal of Gluten Sensitivity.

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