Celiac Sprue is a widely prevalent autoimmune disease of the small intestine. It is induced in genetically susceptible individuals by exposure to dietary gluten.
A 33-mer peptide was discovered with several characteristics that fit this role.
The findings are published in the latest issue of Science.
In vitro and in vivo studies in rats and humans demonstrated that it is stable toward breakdown by all gastric, pancreatic, and intestinal brush-border membrane proteases.
The peptide reacted with tissue transglutaminase, the major autoantigen in celiac sprue, with substantially greater selectivity than known natural substrates of this extracellular enzyme.
|33-mer peptide found in all food grains toxic in celiac sprue.
| Science |
It was found to be a potent inducer of gut-derived human T cell lines from all 14 celiac sprue patients looked at.
Homologues of this peptide were found in all food grains that are toxic to celiac sprue patients. However, they were absent from all nontoxic food grains.
In addition, the peptide could be detoxified in in vitro and in vivo assays by exposure to a bacterial prolyl endopeptidase, suggesting a strategy for oral peptidase supplement therapy for celiac sprue.