A stimulatory role for the protein kinase C pathway in ovarian prostaglandin synthesis: studies with cultured swine granulosa cells.
A calcium-sensitive, lipid-activated protein kinase is present in ovarian granulosa cells and may modulate granulosa cell function through an effect on granulosa cells prostaglandin F2 alpha biosynthesis. Phorbol-ester activation of this protein kinase elicits a dose- and time-dependent augmentation in the synthesis of PGF2 alpha by swine granulosa cells which can be inhibited by inhibitors of prostaglandin and protein synthesis. Our studies support a linkage between protein kinase C activation and prostaglandin F2 alpha synthesis by these cells.
D000818:Animals; D002478:Cells, Cultured; D015237:Dinoprost; D005260:Female; D006107:Granulosa Cells / Q000187:drug effects / Q000378:metabolism; D010053:Ovary / Q000378:metabolism*; D011453:Prostaglandins / Q000096:biosynthesis*; D011460:Prostaglandins F / Q000096:biosynthesis; D011493:Protein Kinase C / Q000378:metabolism*; D013552:Swine; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology
D011453:Prostaglandins; D011460:Prostaglandins F; D015237:Dinoprost; D011493:Protein Kinase C; D013755:Tetradecanoylphorbol Acetate