HORMONAL CONTROL OF C-KINASE AND CORPUS LUTEUM FUNCTION

虽然促黄体生成素(黄体生成素)的许多作用 黄体被认为是由cAMP介导的，cAMP的确切作用机制 黄体生成素是未知的。据推测，促黄体生成素诱导的卵巢事件 由cAMP介导的组织通过cAMP依赖的蛋白激酶发生。 蛋白质的磷酸化是翻译后的主要方式之一。 调节细胞功能的机制。我们最近做了 描述了卵巢组织中另一个重要的信使系统，即 与蛋白质的磷酸化有关。受体介导的秒数增加 源于磷脂酰肌醇代谢的信使(二酰甘油和 肌醇磷酸盐)导致钙激活-和 磷脂依赖蛋白激酶(C-Kinase)。监管 黄体生成素等激素对肌醇磷脂代谢的影响 黄体中的C-激酶提示C-激酶活性的控制 与黄体的功能有关。《公约》的具体目标 建议的研究是提纯和进一步鉴定这种新的蛋白质 激活剂及其在大鼠和牛体内的生理学意义 黄体。该酶将进行纯化，目标为1) 确定C-激酶活性所需的特定辅助因子，2) 制备抗C-激酶的单抗用于检测 和C-激酶的定量，以及3)底物特异性的测定 C-激酶的活性。C-激酶的生理作用将通过1)进行检验 确定酶活性是否在整个生命周期内变化 黄体和2)确定酶活性是否受 黄体生成素或其他已知的调节黄体功能的因素。可能的 C-激酶在黄体功能调节中的作用 通过检测其在1)促性腺激素结合，2)受体中的作用而确定 磷酸化，3)腺苷环化酶激活，4)黄体酮 综合。这些研究将通过监测 外源和内源底物蛋白的磷酸化。这个 对卵巢C-激酶的拟议研究可能为我们提供新的视角 黄体生成素的作用机制与激素诱导之间的联系 C-激酶活性和黄体功能的变化。

Although many of the effects of luteinizing hormone (LH) in the corpus luteum are thought to be mediated by cAMP, the exact mechanism of action of LH is unknown. It is presumed that the LH-induced events in ovarian tissues mediated by cAMP occur via cAMP-dependent protein kinases. Phosphorylation of proteins is one of the major post-translational mechanisms by which cellular functions are regulated. We have recently described another important messenger system in ovarian tissues which is linked to protein phosphorylation. Receptor-mediated increases in second messengers derived from phosphoinositide metabolism (diacylglycerol and inositol phosphates) lead to the activation of a calcium- and phospholipid-dependent protein kinase (C-kinase). The regulation of phosphoinositide metabolism by LH and other hormones and the presence of C-kinase in the corpus luteum suggest that the control of C-kinase activity is related to the function of the corpus luteum. The specific aims of the proposed research are to purify and further characterize this new protein kinase and evaluate its physiological significance in rat and bovine corpora lutea. The enzyme will be purified with the objectives of 1) determining the specific co-factors required for C-kinase activity, 2) producing monoclonal antibodies to C-kinase for the purpose of detection and quantitation of C-kinase, and 3) determining the substrate specificity of C-kinase. The physiological role for C-kinase will be examined by 1) determining whether or not enzyme activity varies throughout the life span of the corpus luteum and 2) determining if enzyme activity is regulated by LH or other factors known to regulate luteal function. The possible involvement of C-kinase in the regulation of luteal function will be determined by examining its role in 1) gonadotropin binding, 2) receptor phosphorylation, 3) adenylate cyclase activation, and 4) progesterone synthesis. These studies will be carried out by monitoring the phosphorylation of both exogenous and endogenous substrate proteins. The proposed studies on the ovarian C-kinase may provide new insight into the mechanism of LH action and establish a link between hormonally-induced changes in C-kinase activation and corpus luteum function.