Abstract：
: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.
journal_name
Life Scijournal_title
Life sciencesauthors
Wrenn RWdoi
10.1016/0024-3205(83)90770-1subject
Has Abstractpub_date
1983-05-16 00:00:00pages
2385-92issue
20eissn
0024-3205issn
1879-0631pii
0024-3205(83)90770-1journal_volume
32pub_type
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