A stimulatory role for the protein kinase C pathway in ovarian prostaglandin synthesis

studies with cultured swine granulosa cells.

L. M. Demers, Johannes D Veldhuis

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

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.

Original languageEnglish (US)
Pages (from-to)1117-1121
Number of pages5
JournalAdvances in prostaglandin, thromboxane, and leukotriene research
Volume17 B
StatePublished - 1987
Externally publishedYes

Fingerprint

Granulosa Cells
Protein Kinase C
Prostaglandins
Dinoprost
Swine
Protein Kinases
Protein Synthesis Inhibitors
Phorbol Esters
Calcium
Lipids

ASJC Scopus subject areas

  • Medicine(all)

Cite this

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title = "A stimulatory role for the protein kinase C pathway in ovarian prostaglandin synthesis: studies with cultured swine granulosa cells.",
abstract = "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.",
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AB - 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.

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