Actions of Gila monster venom on dispersed acini from guinea pig pancreas

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Abstract
Venom from Gila monster (Helodermatidae) contained a pancreatic secretagogue. In dispersed acini from guinea pig pancreas, the venom increased enzyme secretion to the same extent as did vasoactive intestinal peptide, secretin or PHI [amino terminal histidine and carboxy terminal isoleucine peptide]. The abilities of vasoactive intestinal peptide and Gila monster venom to stimulate enzyme secretion were not altered by boiling but were abolished by incubation with trypsin or chymotrypsin. Like vasoactive intestinal peptide, secretin and PHI, the venom caused a 50- to 60-fold increase in cellular cAMP and inhibited binding of 125I-vasoactive intestinal peptide to its membrane receptors on pancreatic acini. The action of venom on enzyme secretion was inhibited by [Gln9]secretin-(5-27), a vasoactive intestinal peptide receptor antagonist, but was not altered by atropine, a cholinergic receptor antagonists, or by dibutyryl cGMP, a cholecystokinin receptor antagonist. Gila monster venom contained no immunoreactive vasoactive intestinal peptide by radioimmunoassay. Venom from Gila monster contained a peptide that stimulated pancreatic enzyme secretion by interacting with vasoactive intestinal peptide receptors on pancreatic acinar cells and activating adenylate cyclase and increasing cellular cAMP.

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