Mazina T I, Pevzner R A
Zh Evol Biokhim Fiziol. 1979 Jan-Feb;15(1):22-8.
It has been shown that the activity of Ca(2+)-ATPase increases during development. Epinephrine in vivo increases the activity of Ca(2+)-ATPase in chick skeletal muscles. The effect of hormone is lacking at embryonic stages of development and appears only before hatching. In the presence of exogenous protein kinase, cAMP also increases the activity of the enzyme, this effect being observed also in embryonic muscles. Lack of effect of epinephrine on Ca(2+)-ATPase in embryonic muscles is associated with non-reactivity of their adenylate cyclase to catecholamines. Ca(2+)-ATPase itself already at embryonic period is ready to react to cAMP. It is concluded that Ca(2+)-ATPase of sarcoplasmic reticulum is one of the sites of action of catecholamines on calcium metabolism in muscle cell and that this action is realized via the system adenylate cyclase-cAMP-protein kinase.
研究表明,Ca(2+)-ATP酶的活性在发育过程中会增加。体内的肾上腺素会增加鸡骨骼肌中Ca(2+)-ATP酶的活性。在胚胎发育阶段,激素没有这种作用,这种作用仅在孵化前出现。在外源蛋白激酶存在的情况下,cAMP也会增加该酶的活性,这种作用在胚胎肌肉中也能观察到。胚胎肌肉中肾上腺素对Ca(2+)-ATP酶缺乏作用与它们的腺苷酸环化酶对儿茶酚胺无反应有关。Ca(2+)-ATP酶在胚胎期就已准备好对cAMP作出反应。得出的结论是,肌浆网的Ca(2+)-ATP酶是儿茶酚胺对肌肉细胞钙代谢作用的部位之一,并且这种作用是通过腺苷酸环化酶-cAMP-蛋白激酶系统实现的。