Activation of adenylate cyclase by forskolin in rat brain and testis.
Activation of adenylate cyclase by forskolin in rat brain and testis.
复制标题
毛喉素在大鼠脑和睾丸中激活腺苷酸环化酶。
DOI：
10.1016/0003-9861(83)90421-6
复制
发表时间：
1983
影响因子：
3.9
通讯作者：
A. Mizutani
中科院分区：
文献类型：
--
作者：
M. Sano;S. Kitajima;A. Mizutani
从大鼠大脑中检测到洗涤剂分散的腺苷酸环化酶有两种组分，一种对Ca ~（2+）和钙调素敏感，另一种对氟或鸟苷酰-5 ′-亚氨基二磷酸（Gpp（NH）p）敏感。在存在或不存在其他酶活化剂（例如，NaF、Gpp（NH）p、钙调蛋白）。其中G/F蛋白完全缺乏的催化亚基组分也被毛喉素激活。在出生后1-35天的发育过程中，大脑和小脑颗粒制剂中的基础腺苷酸环化酶活性进行性增加。虽然大脑和小脑酶的氟敏感性在出生后的发展过程中增加，毛喉素的反应性保持不变。有没有增强的可溶性腺苷酸环化酶（从大鼠睾丸）的测定条件下，有一个显着的刺激作用的颗粒酶。用Lubrol PX或胆酸盐溶解酶的结果表明，毛喉素对环化酶的作用不需要G/F蛋白或钙调蛋白，我们对脑酶的研究结果支持这一观点。关于可溶性睾丸环化酶的数据（这种酶对毛喉素的反应较差或不存在）表明，它缺乏一种可以赋予更大刺激的蛋白质（除了催化单位）。目前的结果不排除另一种解释，即毛喉素刺激腺苷酸环化酶的直接相互作用的催化亚基，如果催化蛋白质确实有很大的不同，在不同种类的细胞和他们的反应，这种二萜。
Detergent-dispersed adenylate cyclase from rat cerebrum was detected in two components, one sensitive to Ca2+and calmodulin and another sensitive to fluoride or guanyl-5′-yl imidodiphosphate (Gpp(NH)p). The enzyme activity of both components was markedly augmented by forskolin assayed in the presence or absence of other enzyme activators (e.g., NaF, Gpp(NH)p, calmodulin). The catalytic subunit fraction in which G/F protein was totally lacking was also activated by forskolin. During 1–35 days of postnatal development, the basal adenylate cyclase activities in either cerebrum and cerebellum particulate preparations progressively increased. While the fluoride sensitivity of the cerebrum and cerebellum enzyme increased during postnatal development, the responsiveness to forskolin remained unaltered. There was no enhancement of soluble adenylate cyclase (from rat testis) by forskolin under the assay conditions in which there was a marked stimulatory action on the particulate enzyme. The results seen with the solubilized enzyme, with either Lubrol PX or cholate, indicate that the effects of forskolin on the cyclase do not require either G/F protein or calmodulin and the results of our study of brain enzymes support this view. Data on soluble testis cyclase (a poor or absent response to forskolin by this enzyme) imply that it lacks a protein (other than the catalytic unit) which could confer greater stimulation. The present results do not rule out an alternative explanation that forskolin stimulates adenylate cyclase by a direct interaction with the catalytic subunit, if the catalytic proteins do differ widely in various species of cells and their response to this diterpene.