Bertorello A M, Aperia A, Walaas S I, Nairn A C, Greengard P
Department of Pediatrics, St. Göran's Children's Hospital, Karolinska Institutet, Stockholm, Sweden.
Proc Natl Acad Sci U S A. 1991 Dec 15;88(24):11359-62. doi: 10.1073/pnas.88.24.11359.
We have examined two distinct protein kinases, cAMP-dependent protein kinase and protein kinase C, for their ability to phosphorylate and regulate the activity of three different types of Na+,K(+)-ATPase preparation. cAMP-dependent protein kinase phosphorylated purified shark rectal gland Na+,K(+)-ATPase to a stoichiometry of approximately 1 mol of phosphate per mol of alpha subunit. Protein kinase C phosphorylated purified shark rectal gland Na+,K(+)-ATPase to a stoichiometry of approximately 2 mol of phosphate per mol of alpha subunit. The phosphorylation by each of the kinases was associated with an inhibition of Na+,K(+)-ATPase activity of about 40-50%. These two protein kinases also inhibited the activity of a partially purified preparation of Na+,K(+)-ATPase from rat renal cortex and the activity of Na+,K(+)-ATPase present in preparations of basolateral membrane vesicles from rat renal cortex.
我们研究了两种不同的蛋白激酶，即环磷酸腺苷（cAMP）依赖性蛋白激酶和蛋白激酶C，考察它们磷酸化并调节三种不同类型的钠钾ATP酶制剂活性的能力。cAMP依赖性蛋白激酶将纯化的鲨鱼直肠腺钠钾ATP酶磷酸化，化学计量比约为每摩尔α亚基1摩尔磷酸盐。蛋白激酶C将纯化的鲨鱼直肠腺钠钾ATP酶磷酸化，化学计量比约为每摩尔α亚基2摩尔磷酸盐。每种激酶的磷酸化作用均伴随着钠钾ATP酶活性约40 - 50%的抑制。这两种蛋白激酶还抑制了来自大鼠肾皮质的部分纯化的钠钾ATP酶制剂的活性以及存在于大鼠肾皮质基底外侧膜囊泡制剂中的钠钾ATP酶的活性。
