Activation of protein kinase C is coupled to prostaglandin F synthesis in the ovary

studies in cultured swine granulosa cells

the technical assistance with, Paula Azimi, Diana Juchter and James Garmey of, Johannes D Veldhuis, Lawrence M. Demers

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

We have investigated the role of phospholipid-sensitive calcium-dependent protein kinase (protein kinase C) in prostaglandin F synthesis by monolayer cultures of swine granulosa cells. In this system, specific phorbol ester derivatives known to activate protein kinase C significantly augmented the production of prostaglandin F. Phorbol ester in conjunction with the ionophore A23187 synergistically increased prostaglandin F production. These stimulatory actions were dose- and time-dependent, and could be abolished by the cyclooxygenase inhibitor, indomethacin, or the protein synthesis inhibitor, cycloheximide. Moreover, the rank order of potency of phorbol esters in enhancing prostaglandin F production was concordant with that demonstrated for activation of protein kinase C in the swine ovary. In addition, a nonphorbol stimulator of protein kinase C, l-octanoyl-2-acetylglycerol, also significantly enhanced prostaglandin F biosynthesis. The synthesis of immunoassayable prostaglandin F was confirmed by high-pressure liquid Chromatographie purification of this radiolabeled metabolite of [3H]arachidonic acid. Thus, the present studies indicate that the protein kinase C effector pathway in the swine granulosa cell is functionally coupled to prostaglandin F production.

Original languageEnglish (US)
Pages (from-to)249-254
Number of pages6
JournalMolecular and Cellular Endocrinology
Volume49
Issue number2-3
DOIs
StatePublished - 1987
Externally publishedYes

Fingerprint

Dinoprost
Granulosa Cells
Protein Kinase C
Ovary
Swine
Chemical activation
Phorbol Esters
Protein Synthesis Inhibitors
Cyclooxygenase Inhibitors
Biosynthesis
Ionophores
Calcimycin
Cycloheximide
Metabolites
Arachidonic Acid
Indomethacin
Purification
Monolayers
Derivatives
Pressure

Keywords

  • (Activation)
  • (Ovary)
  • Granulosa cell
  • Prostaglandin F synthesis
  • Protein kinase C

ASJC Scopus subject areas

  • Endocrinology
  • Endocrinology, Diabetes and Metabolism

Cite this

Activation of protein kinase C is coupled to prostaglandin F synthesis in the ovary : studies in cultured swine granulosa cells. / with, the technical assistance; of, Paula Azimi, Diana Juchter and James Garmey; Veldhuis, Johannes D; Demers, Lawrence M.

In: Molecular and Cellular Endocrinology, Vol. 49, No. 2-3, 1987, p. 249-254.

Research output: Contribution to journalArticle

with, the technical assistance ; of, Paula Azimi, Diana Juchter and James Garmey ; Veldhuis, Johannes D ; Demers, Lawrence M. / Activation of protein kinase C is coupled to prostaglandin F synthesis in the ovary : studies in cultured swine granulosa cells. In: Molecular and Cellular Endocrinology. 1987 ; Vol. 49, No. 2-3. pp. 249-254.
@article{f2458c4015904fd7b4510ca03b714bd2,
title = "Activation of protein kinase C is coupled to prostaglandin F2α synthesis in the ovary: studies in cultured swine granulosa cells",
abstract = "We have investigated the role of phospholipid-sensitive calcium-dependent protein kinase (protein kinase C) in prostaglandin F2α synthesis by monolayer cultures of swine granulosa cells. In this system, specific phorbol ester derivatives known to activate protein kinase C significantly augmented the production of prostaglandin F2α. Phorbol ester in conjunction with the ionophore A23187 synergistically increased prostaglandin F2α production. These stimulatory actions were dose- and time-dependent, and could be abolished by the cyclooxygenase inhibitor, indomethacin, or the protein synthesis inhibitor, cycloheximide. Moreover, the rank order of potency of phorbol esters in enhancing prostaglandin F2α production was concordant with that demonstrated for activation of protein kinase C in the swine ovary. In addition, a nonphorbol stimulator of protein kinase C, l-octanoyl-2-acetylglycerol, also significantly enhanced prostaglandin F2α biosynthesis. The synthesis of immunoassayable prostaglandin F2α was confirmed by high-pressure liquid Chromatographie purification of this radiolabeled metabolite of [3H]arachidonic acid. Thus, the present studies indicate that the protein kinase C effector pathway in the swine granulosa cell is functionally coupled to prostaglandin F2α production.",
keywords = "(Activation), (Ovary), Granulosa cell, Prostaglandin F synthesis, Protein kinase C",
author = "with, {the technical assistance} and of, {Paula Azimi, Diana Juchter and James Garmey} and Veldhuis, {Johannes D} and Demers, {Lawrence M.}",
year = "1987",
doi = "10.1016/0303-7207(87)90219-X",
language = "English (US)",
volume = "49",
pages = "249--254",
journal = "Molecular and Cellular Endocrinology",
issn = "0303-7207",
publisher = "Elsevier Ireland Ltd",
number = "2-3",

}

TY - JOUR

T1 - Activation of protein kinase C is coupled to prostaglandin F2α synthesis in the ovary

T2 - studies in cultured swine granulosa cells

AU - with, the technical assistance

AU - of, Paula Azimi, Diana Juchter and James Garmey

AU - Veldhuis, Johannes D

AU - Demers, Lawrence M.

PY - 1987

Y1 - 1987

N2 - We have investigated the role of phospholipid-sensitive calcium-dependent protein kinase (protein kinase C) in prostaglandin F2α synthesis by monolayer cultures of swine granulosa cells. In this system, specific phorbol ester derivatives known to activate protein kinase C significantly augmented the production of prostaglandin F2α. Phorbol ester in conjunction with the ionophore A23187 synergistically increased prostaglandin F2α production. These stimulatory actions were dose- and time-dependent, and could be abolished by the cyclooxygenase inhibitor, indomethacin, or the protein synthesis inhibitor, cycloheximide. Moreover, the rank order of potency of phorbol esters in enhancing prostaglandin F2α production was concordant with that demonstrated for activation of protein kinase C in the swine ovary. In addition, a nonphorbol stimulator of protein kinase C, l-octanoyl-2-acetylglycerol, also significantly enhanced prostaglandin F2α biosynthesis. The synthesis of immunoassayable prostaglandin F2α was confirmed by high-pressure liquid Chromatographie purification of this radiolabeled metabolite of [3H]arachidonic acid. Thus, the present studies indicate that the protein kinase C effector pathway in the swine granulosa cell is functionally coupled to prostaglandin F2α production.

AB - We have investigated the role of phospholipid-sensitive calcium-dependent protein kinase (protein kinase C) in prostaglandin F2α synthesis by monolayer cultures of swine granulosa cells. In this system, specific phorbol ester derivatives known to activate protein kinase C significantly augmented the production of prostaglandin F2α. Phorbol ester in conjunction with the ionophore A23187 synergistically increased prostaglandin F2α production. These stimulatory actions were dose- and time-dependent, and could be abolished by the cyclooxygenase inhibitor, indomethacin, or the protein synthesis inhibitor, cycloheximide. Moreover, the rank order of potency of phorbol esters in enhancing prostaglandin F2α production was concordant with that demonstrated for activation of protein kinase C in the swine ovary. In addition, a nonphorbol stimulator of protein kinase C, l-octanoyl-2-acetylglycerol, also significantly enhanced prostaglandin F2α biosynthesis. The synthesis of immunoassayable prostaglandin F2α was confirmed by high-pressure liquid Chromatographie purification of this radiolabeled metabolite of [3H]arachidonic acid. Thus, the present studies indicate that the protein kinase C effector pathway in the swine granulosa cell is functionally coupled to prostaglandin F2α production.

KW - (Activation)

KW - (Ovary)

KW - Granulosa cell

KW - Prostaglandin F synthesis

KW - Protein kinase C

UR - http://www.scopus.com/inward/record.url?scp=0023119747&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0023119747&partnerID=8YFLogxK

U2 - 10.1016/0303-7207(87)90219-X

DO - 10.1016/0303-7207(87)90219-X

M3 - Article

VL - 49

SP - 249

EP - 254

JO - Molecular and Cellular Endocrinology

JF - Molecular and Cellular Endocrinology

SN - 0303-7207

IS - 2-3

ER -