In vitro activation of adenylate cyclase of atrophic celiac intestinal mucosa by wheat gliadin-derived peptides.
In order to demonstrate that gliadin peptides may interact with cell membranes of celiac small intestinal mucosa, the capacity of these peptides to activate the cell membrane enzyme adenylate cyclase was tested. The addition of peptides from bread wheat purified A-gliadin and whole gliadin (proteins that are toxic for celiac patients) enhanced the adenylate cyclase activity of crude cell membrane preparations obtained from atrophic small intestinal mucosa of celiac patients. No activation of adenylate cyclase of this tissue was observed with peptides from proteins nontoxic for celiac patients (bread wheat albumin and maize prolamin). Gliadin peptides did not activate adenylate cyclase of morphologically normal small intestinal mucosa from normal subjects or from celiac patients in remission. These results, therefore, suggest that peptides from bread wheat gliadin may interact with cell membrane of atrophic small intestinal mucosa of celiac patients.
D000262:Adenylyl Cyclases / Q000378:metabolism*; D000328:Adult; D001284:Atrophy; D002446:Celiac Disease / Q000201:enzymology* / Q000473:pathology; D002462:Cell Membrane / Q000201:enzymology; D002648:Child; D004789:Enzyme Activation; D005903:Gliadin / Q000302:isolation & purification / Q000494:pharmacology*; D006801:Humans; D007413:Intestinal Mucosa / Q000201:enzymology* / Q000473:pathology; D007421:Intestine, Small; D010446:Peptide Fragments / Q000302:isolation & purification / Q000494:pharmacology; D010940:Plant Proteins / Q000494:pharmacology*
D010446:Peptide Fragments; D010940:Plant Proteins; D005903:Gliadin; D000262:Adenylyl Cyclases