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J. Biol. Chem., Vol. 269, Issue 12, 8772-8779, Mar, 1994
J Quintana, RW Hipkin, J Sanchez-Yague and M Ascoli
Using a cell line stably transfected with the rat follitropin (FSH)
receptor cDNA we demonstrate that the FSH receptor becomes phosphorylated
when cells are exposed to FSH. Since binding of FSH to its receptor results
in an increase in cAMP and inositol phosphate accumulation, we examined the
potential involvement of protein kinase A and C in mediating receptor
phosphorylation. Stimulation of protein kinase A does not appear to be
necessary because hFSH-induced receptor phosphorylation was minimally
impaired in a cell line that overexpresses cAMP phosphodiesterase.
Moreover, stimulation of the protein kinase A pathway with other agonists
result in minimal phosphorylation of the FSH receptor. Stimulation of the
protein kinase C with a phorbol ester did result in an increase in receptor
phosphorylation, and down-regulation of the protein kinase C decreased, but
did not abolish, the FSH-induced receptor phosphorylation. The possible
impact of phosphorylation on the functions of the receptor was examined by
testing if conditions that lead to phosphorylation decrease the ability of
FSH to stimulate cAMP synthesis. Our data show that as with the addition of
FSH, addition of a phorbol ester also results in a decrease in the ability
of FSH to stimulate cAMP synthesis.
Follitropin (FSH) and a phorbol ester stimulate the phosphorylation of the FSH receptor in intact cells
Department of Pharmacology, University of Iowa College of Medicine, Iowa City 52242-1109.
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