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."