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Receptor Expression in Cultured Human Granulosa-Luteal Cells1
Departments of Clinical Chemistry and Obstetrics and Gynecology (A.R.) and the Haartman Institute, Department of Bacteriology and Immunology (R.J., O.R.), University of Helsinki, Helsinki, Finland
Address all correspondence and requests for reprints to: Dr. Ari Ristimäki, Research Laboratory, Department of Obstetrics and Gynecology, University of Helsinki, Haartmaninkatu 2, SF-00290 Helsinki, Finland.
PGF2
is a metabolite of arachidonic acid that triggers
regression of the corpus luteum. Recent animal studies have indicated
that PGF2 (FP) receptor messenger ribonucleic acid
(mRNA) is expressed in the corpus luteum. To understand the regulation
of the FP receptor in the ovary we have cloned a partial complementary
DNA (cDNA) sequence of the FP receptor from human granulosa cells
obtained from women undergoing in vitro fertilization.
The sequence of this cDNA is identical to the previously reported FP
receptor sequences obtained from human uterine and placental cDNA
libraries. Low levels of the FP receptor mRNA were observed in freshly
isolated granulosa cells or in cultured granulosa-luteal (GL) cells, as
detected by reverse transcriptase-PCR. hCG and 8-bromo-cAMP increased
the steady state levels of the FP receptor mRNAs after incubation for
24–48 h, as detected by Northern blot hybridization. The stimulatory
effect of hCG was concentration and culture stage dependent. Further,
hCG and 8-bromo-cAMP increased binding of radiolabeled
PGF2 to intact GL cells. In contrast, phorbol
12-myristate 13-acetate inhibited basal as well as hCG- and
8-bromo-cAMP-induced FP receptor mRNA expression and binding of the
radiolabeled ligand. In summary, hCG, 8-bromo-cAMP, and phorbol
12-myristate 13-acetate modulate the expression of the FP receptor in
human GL cells, which may represent a mechanism to regulate the
responsiveness of the ovary to PGF2.
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