Phospholipid-sensitive calcium-dependent protein kinase and its endogenous substrate proteins in rat pancreatic acinar cells.
Phospholipid-sensitive Ca2+-dependent protein kinase and its endogenous substrate proteins were examined in acinar cells from rat pancreas. The enzyme was clearly demonstrable by DEAE-cellulose chromatography of acinar cell extract. At least four endogenous substrate proteins (Mr = 38K, 30K, 22K and 15K) for this Ca2+-activated kinase were found in the acinar cell extract. These substrate proteins were maximally phosphorylated in the combined presence of Ca2+ and phosphatidylserine. Calmodulin was partially effective as a cofactor for phosphorylation of the 38K substrate protein, but ineffective for the other three. A slight Ca2+/phospholipid-dependent phosphorylation of 38K and 30K proteins, but not of 22K and 15K proteins was seen in extract of isolated pancreatic islets. The Ka for Ca2+ for phosphorylation of the endogenous acinar cell proteins was decreased more than ten-fold in the combined presence of phosphatidylserine and unsaturated diacylglycerol. The presence of this Ca2+/phospholipid-dependent protein kinase/protein phosphorylation system provides a potential mechanism of action for Ca2+ as a regulator of exocrine pancreatic function.
D000818:Animals; D001345:Autoradiography; D002118:Calcium / Q000494:pharmacology; D002147:Calmodulin / Q000494:pharmacology; D002848:Chromatography, DEAE-Cellulose; D066298:In Vitro Techniques; D008297:Male; D010179:Pancreas / Q000201:enzymology*; D010743:Phospholipids / Q000494:pharmacology; D011494:Protein Kinases / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains
D002147:Calmodulin; D010743:Phospholipids; D011494:Protein Kinases; D002118:Calcium