Azhar S, Fanelli C, Menon K M
Endocr Res Commun. 1978;5(1):1-19. doi: 10.1080/07435807809073632.
Incubation of rat ovarian slices with choriogonadotropin resulted in stimulation of cyclic AMP dependent protein kinase activity in a time and dose dependent manner. However, prior exposure of animals to choriogonadotropin in vivo resulted in a decreased sensitivity to subsequent in vitro stimulation by the same hormone. This decreased sensitivity was due to a lesion in the hormone receptor adenylate cyclase system rather than a change in the property of protein kinase with respect to its stimulation by cyclic AMP. Unchanged levels of cyclic AMP formation in these ovaries were evidenced by the lack of inhibition of [3H] cyclic AMP binding. In the untreated controls, however, choriogonadotropin in vitro resulted in inhibition [3H] cyclic AMP binding activity suggesting endogenous occupation parallel to protein kinase activation. These results are indicative of the linear coupling of hormone receptor-adenylate cyclase-protein kinase system and point out the in vivo role of protein kinase activation in choriogonadotropin mediated regulation of ovarian function.
用绒毛膜促性腺激素孵育大鼠卵巢切片，会以时间和剂量依赖的方式刺激环磷酸腺苷依赖性蛋白激酶活性。然而，动物在体内预先接触绒毛膜促性腺激素会导致对随后相同激素的体外刺激敏感性降低。这种敏感性降低是由于激素受体腺苷酸环化酶系统的损伤，而非蛋白激酶受环磷酸腺苷刺激的特性发生改变。这些卵巢中环磷酸腺苷生成水平未变，这一点可通过缺乏对[3H]环磷酸腺苷结合的抑制来证明。然而，在未处理的对照中，体外的绒毛膜促性腺激素会导致[3H]环磷酸腺苷结合活性受到抑制，这表明内源性占据与蛋白激酶激活平行。这些结果表明激素受体 - 腺苷酸环化酶 - 蛋白激酶系统存在线性偶联，并指出了蛋白激酶激活在绒毛膜促性腺激素介导的卵巢功能调节中的体内作用。
