The biochemical mechanisms subserving the inhibitory actions of prostaglandin F2α 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 F2α activates this phospholipid-dependent, calcium-stimulated effector pathway. Using monolayer cultures of swine granulosa cells, we now report that prostaglandin F2α 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.
|Original language||English (US)|
|Number of pages||6|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - Nov 30 1987|
ASJC Scopus subject areas
- Molecular Biology