title: Prostaglandin F2 alpha initiates polyphosphatidylinositol hydrolysis and membrane translocation of protein kinase C in swine ovarian cells.
abstract: The biochemical mechanisms subserving the inhibitory actions of prostaglandin F2 alpha on ovarian cells are not known. Since the protein kinase C pathway is coupled to steroidogenesis in an inhibitory fashion in pig granulosa cells, we have tested the hypothesis that prostaglandin F2 alpha activates this phospholipid-dependent, calcium-stimulated effector pathway. Using monolayer cultures of swine granulosa cells, we now report that prostaglandin F2 alpha is capable of activating critical components of the protein kinase C pathway, including the production of water-soluble inositol phosphates, liberation of free arachidonic acid, release of endogenous diacylglycerol, and translocation of cytosolic protein kinase C to the phospholipid-enriched membrane microenvironment.
mesh_terms: D000818:Animals; D016718:Arachidonic Acid; D001095:Arachidonic Acids / Q000378:metabolism; D001692:Biological Transport / Q000187:drug effects; D002462:Cell Membrane / Q000378:metabolism; D002478:Cells, Cultured; D003600:Cytosol / Q000378:metabolism; D004075:Diglycerides / Q000378:metabolism; D015237:Dinoprost; D005260:Female; D006107:Granulosa Cells / Q000187:drug effects / Q000378:metabolism*; D006868:Hydrolysis; D015544:Inositol 1,4,5-Trisphosphate; D007295:Inositol Phosphates / Q000378:metabolism; D007700:Kinetics; D010716:Phosphatidylinositols / Q000378:metabolism*; D011460:Prostaglandins F / Q000494:pharmacology*; D011493:Protein Kinase C / Q000378:metabolism*; D013552:Swine
chemical_list: D001095:Arachidonic Acids; D004075:Diglycerides; D007295:Inositol Phosphates; D010716:Phosphatidylinositols; D011460:Prostaglandins F; D016718:Arachidonic Acid; D015544:Inositol 1,4,5-Trisphosphate; D015237:Dinoprost; D011493:Protein Kinase C