Chymodenin, a duodenal peptide: specific stimulation of chymotrypsinogen secretion

Abstract

Chymodenin, a basic porcine duodenal peptide, was administered to anesthetized rabbits intravenously or added to the medium bathing the isolated pancreas. In the 10(-8)M range, chymodenin rapidly increased chymotrypsinogen (ChTg) secretion, did not increase lipase secretion, and modestly enhanced protein secretion (which could be attributed primarily to augmented ChTg secretion). The increased ChTg output was too rapid to be the result of increased rates of protein synthesis and could not be attributed to the exocytosis os zymogen granule contents because of the enzyme-;pecific nature of the response. In contrast to shymodenin, cholinergic stimulation in vitro produced a relatively lipase-rich, chymotrypsinogen-poor secretion. Lipase and ChTg outputs, which varied relatively independently under unstimulated conditions, covaried in the presence of chymodenin. The existence of a duodenal peptide that produces an enzyme-specific response supports the hypothesis that the secretion of digestive enzymes during digestion is a highly regulated process in which the enzyme content of pancreatic secretion varies with differences in the composition of intestinal substrates.