Abstract
Protein phosphorylation has been implicated as a key response to gonadotropic stimulation of ovarian cells. The second messenger systems, which would act by control of protein phosphorylation, include the adenylate cyclase/cAMP/A-kinase system (1) and the phosphoinositide hydrolysis system (2). Hydrolysis of phospatidylinositol 4,5-bisphosphate leads to the generation of 1,2-diacylglycerol, activation of diacylglycerol-dependent protein kinases (the C-kinases) (2, 3), and the generation of inositol 1,4,5- triphosphate, promoting release of Ca++(2) and activation of Ca++/ calmodulin-dependent kinases (1). Ovarian tissues have been shown to contain protein kinases in each of the above classes. The functional significance of each class of protein kinases is not yet fully defined, but the existence of hormone-regulated parameters for each class of kinase in the ovary suggests that the kinases participate in the mediation of or modulation of hormone-regulated cellular responses. Ovarian A-kinases are regulated acutely (4) and chronically (5) by gonadotropic stimulation. Estrogen is also required for stimulated levels of mRNA for A-kinase regulatory subunit (RIIβ) in the rat granulosa cell (6). Ca++/calmodulin kinase III, which phosphorylates the protein synthesis elongation factor EF2, is regulated by estrogen in the rat corpus luteum of pregnancy (7). Levels of lipid-derived second messengers, 1,2-diacylglycerol (DAG) and inositol 1,4,5-triphosphate, are regulated by gonadotropin, prostaglandin, and GnRH exposure in ovarian cells (8–11).
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Maizels, E.T., Jackiw, V., Miller, J.B., Cutler, R.E., Carney, E.M., Hunzicker-Dunn, M. (1991). Variant Diacylglycerol—Dependent Protein Phosphotransferase Activity in Ovarian Tissues. In: Gibori, G. (eds) Signaling Mechanisms and Gene Expression in the Ovary. Serono Symposia USA. Springer, New York, NY. https://doi.org/10.1007/978-1-4612-3200-1_5
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DOI: https://doi.org/10.1007/978-1-4612-3200-1_5
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