The programming of cell function at the transcriptional level during ovarian development and maturation requires control mechanisms in which cyclic AMP and cyclic AMP-dependent protein kinases are believed to be actively involved. The function of cellular proteins may be altered or modulated through the action of cyclic AMP-dependent protein kinases which are under control by gonadotropic hormones (FSH/LH) through the action of cyclic AMP. This research program is desinged to elucidate the effects of FSH and/or LH on the ontogeny of cytoplasmic and nuclear cyclic AMP-dependent protein kinases and the effects of these protein kinases on the phosphorylation of nuclear proteins during postnatal ovarian development in the rat.
We aim to determine (a) the rate of biosynthesis of ovarian cytoplasmic and nuclear cyclic AMP-dependent protein kinases; (b) quantitate the levels of the regulatory subunits RI and RII and the catalytic subunit C during postnatal ovarian development by immunochemical methods; (c) determine the translocation of cytoplasmic cyclic AMP-dependent protein kinase to chromatin acceptor sites; (d) determine the phosphorylation patterns of nuclear proteins during postnatal development before and after gonadotropin stimulation; and (e) determine the degree of in vivo phosphorylation and dephosphorylation of ovarian RNA polymerase II during postnatal development before and after gonadotropin stimulation. The data will contribute toward elucidation of the factors involved in the cyclic AMP and protein kinase-mediated control of ovarian development and function.
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