Plesneva S A, Shpakov A O, Kuznetsova L A, Pertseva M N
M. Sechenov Institute of Evolutionary Physiology and Biochemistry, Russian Acad. Sci., Russia, 194223, St. Petersburg, pr. M. Toreza, 44.
Ross Fiziol Zh Im I M Sechenova. 2001 Aug;87(8):1106-17.
Activation of proteinkinase C with diacylglycerol or phorbol-12-myristate-13-acetate in the rat muscle membrane or Anodonta cygnea mollusc blocks the insulin stimulating signal to adenylyl cyclase via tyrosinekinase type receptor. The same occurs with stimulating effect of biogenic amines to adenylyl cyclase via serpentine type receptor. Transduction of the inhibitory signal induced with isoproterenol to adenylyl cyclase remained unchanged in case of the proteinkinase C activation. The findings suggest that phorbol-sensitive proteinkinase C realizes a negative regulation of insulin-sensitive adenylyl cyclase signalling system. This negative regulation might prove a universal mechanism of the adenylyl cyclase system desensitisation.
用二酰基甘油或佛波醇 - 12 - 肉豆蔻酸酯 - 13 - 乙酸酯激活大鼠肌膜或圆田螺软体动物中的蛋白激酶C，可阻断胰岛素通过酪氨酸激酶型受体向腺苷酸环化酶发出的刺激信号。生物胺通过蛇形受体对腺苷酸环化酶的刺激作用也会出现同样情况。在蛋白激酶C激活的情况下，异丙肾上腺素诱导的对腺苷酸环化酶的抑制信号转导保持不变。这些发现表明，佛波醇敏感的蛋白激酶C实现了对胰岛素敏感的腺苷酸环化酶信号系统的负调控。这种负调控可能是腺苷酸环化酶系统脱敏的普遍机制。
