Actions of Gila monster venom on dispersed acini from guinea pig pancreas
| Autor: | Jean-Pierre Raufman, Robert T. Jensen, Jerry D. Gardner, J. J. Pisano, V. E. Sutliff |
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| Rok vydání: | 1982 |
| Předmět: |
Male
Carbonyl Cyanide m-Chlorophenyl Hydrazone medicine.medical_specialty Physiology Receptors Drug Guinea Pigs Vasoactive intestinal peptide Venom Cholecystokinin receptor Secretin Theophylline Physiology (medical) Internal medicine Cyclic AMP medicine Animals Gila monster Receptor Pancreas Hepatology biology Venoms Vasoactive intestinal peptide receptor Gastroenterology Lizards biology.organism_classification Trypsin Peptide Fragments Endocrinology Amylases Amphibian Venoms Vasoactive Intestinal Peptide medicine.drug |
| Zdroj: | American Journal of Physiology-Gastrointestinal and Liver Physiology. 242:G470-G474 |
| ISSN: | 1522-1547 0193-1857 |
| DOI: | 10.1152/ajpgi.1982.242.5.g470 |
| Popis: | Venom from Gila monster (family Helodermatidae) contains 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. 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 antagonist, or by dibutyryl cGMP, a cholecystokinin receptor antagonist. Gila monster venom contained no immunoreactive vasoactive intestinal peptide by radioimmunoassay. These results indicate that venom from Gila monster contains a peptide that can stimulate pancreatic enzyme secretion by interacting with vasoactive intestinal peptide receptors on pancreatic acinar cells and thereby activating adenylate cyclase and increasing cellular cAMP. |
| Databáze: | OpenAIRE |
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