Stimulated protein kinase activity during acute pancreatitis in rats. Possible mediation by proteolysis, lipolysis, and bile salts.
The rate of protein phosphorylation, as catalyzed by the protein kinase enzymes, was measured in the pancreas of rats with acute experimental pancreatitis. Two different methods were used to induce pancreatitis in rats: retrograde injection of deoxycholate (DOC) into the pancreatic duct, or daily intravenous administration of DL-ethionine. Basal protein kinase activity was elevated in rats with acute experimental pancreatitis. This increase in activity was not dependent on free Ca2+ and did not result from elevated cAMP levels. To assess the possible role of digestive enzymes in protein kinase activation, tissue extracts from healthy controls were subjected to mild treatment with digestive enzymes and DOC. Trypsin, chymotrypsin, phospholipase A, and DOC produced protein kinase activation of a similar magnitude as found in diseased tissue. Results indicate that stimulated protein kinase activity in tissue of animals with acute pancreatitis may arise from the action of digestive enzymes.
D000208:Acute Disease; D000818:Animals; D001647:Bile Acids and Salts / Q000378:metabolism* / Q000494:pharmacology; D002268:Carboxypeptidases / Q000494:pharmacology; D002918:Chymotrypsin / Q000494:pharmacology; D003840:Deoxycholic Acid / Q000494:pharmacology; D000431:Ethanol / Q000494:pharmacology; D008066:Lipolysis; D010179:Pancreas / Q000187:drug effects; D010195:Pancreatitis / Q000201:enzymology*; D010740:Phospholipases / Q000494:pharmacology; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains; D014357:Trypsin / Q000494:pharmacology
D001647:Bile Acids and Salts; D003840:Deoxycholic Acid; D000431:Ethanol; D011494:Protein Kinases; D010740:Phospholipases; D002268:Carboxypeptidases; D002918:Chymotrypsin; D014357:Trypsin