Redistribution of phospholipid/calcium-dependent protein kinase and altered phosphorylation of its soluble and particulate substrate proteins in phorbol ester-treated rat pancreatic acini.
The biological activity of phorbol esters, such as 12-O-tetra-decanoylphorbol-13-acetate, have been associated with activation of phospholipid/Ca2+-dependent protein kinase. Treatment of rat pancreatic acini with 12-O-tetradecanoylphorbol-13-acetate (10(-6) M) resulted in a sustained translocation of phospholipid/Ca2+-dependent protein kinase activity to the membrane site. The pattern of phosphorylation of at least two substrate proteins (Mr 22,000 and 18,000) for this Ca2+-dependent protein kinase was also altered following exposure to phorbol ester, these phosphoproteins disappearing from the soluble fraction and appearing in the particulate. Concurrently, 12-O-tetradecanoylphorbol-13-acetate stimulated amylase release from intact acini in a time- and dose-dependent fashion. These results suggest a potential role for phospholipid/Ca2+-activated protein kinase in the regulation of pancreatic exocrine function.
Wooten
M W
MW
Wrenn
R W
RW
D000681:Amylases / Q000378:metabolism; D000818:Animals; D066298:In Vitro Techniques; D008297:Male; D010179:Pancreas / Q000187:drug effects* / Q000201:enzymology / Q000378:metabolism; D010704:Phorbols / Q000494:pharmacology*; D010766:Phosphorylation; D011493:Protein Kinase C; D011494:Protein Kinases / Q000032:analysis*; D011506:Proteins / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology*
D010704:Phorbols; D011506:Proteins; D011494:Protein Kinases; D011493:Protein Kinase C; D000681:Amylases; D013755:Tetradecanoylphorbol Acetate