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Estradiol Elevates Protein Kinase C Catalytic Activity in the Preoptic Area of Female Rats¹

Department of Neuroscience, Albert Einstein College of Medicine, Bronx, New York 10461

Address all correspondence and requests for reprints to: Michael Ansonoff, Department of Neuroscience, F113, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, New York 10461. E-mail: ansonoff{at}aecom.yu.edu

Estrogen acts in the brain to regulate female reproductive physiology and behavior, and protein kinase C (PKC) is estrogen-regulated in many estrogen-responsive tissues. We examined whether estrogen regulates PKC in the hypothalamus (HYP) and preoptic area (POA), brain regions which mediate estrogenic control of female reproductive function. PKC activity in tissue from hormone-treated and control female rats was measured, in the presence of phorbol ester and calcium, by quantifying ³²P incorporation into a substrate peptide. PKC catalytic activity increased significantly in POA tissue extracts from estradiol-treated, ovariectomized (OVX) female rats but not in HYP or cortical extracts. Phorbol ester potentiation of cAMP accumulation also was examined to determine whether the ability of PKC to potentiate adenylyl cyclase activity was affected by estrogen. PKC stimulation potentiated forskolin-induced cAMP accumulation to a greater degree in POA, but not HYP, slices from estrogen-treated OVX female rats. PKC enzyme levels were examined using phorbol-12,13-dibutyrate binding assays and immunoblots. Estrogen treatment did not change phorbol ester binding affinity or the density of binding sites in the POA or HYP. Immunoblots for the , ß, and PKC isoforms combined, or the PKC isoform alone, did not detect differences between hormone-treated and control OVX female rats. Therefore, estrogen treatment increased PKC catalytic activity in the POA of OVX female rats but not in the HYP. However, the increased PKC catalytic activity was not correlated with detectable changes in the level of the , ß, or PKC isoforms or in the density of phorbol ester binding sites.

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