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.
N1 - Funding Information:
We thank Chris McNett for the skillful preparation of the manuscript, the Gwaltney-Smithfield Packing Corporation for providing swine ovaries, Paula P. Azimi for the artwork, and Dr. Julianne J. Sando for her expert advice and assistance in the conduct of this work. This work was supported in part by NIH Grant No. R 01 HD16806 and RCDA No. 1 K04 HD 00634 (J.D.V.).
PY - 1987/2
Y1 - 1987/2
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
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U2 - 10.1016/0303-7207(87)90219-X
DO - 10.1016/0303-7207(87)90219-X
M3 - Article
C2 - 3104113
AN - SCOPUS:0023119747
SN - 0303-7207
VL - 49
SP - 249
EP - 254
JO - Molecular and Cellular Endocrinology
JF - Molecular and Cellular Endocrinology
IS - 2-3
ER -