Ballermann B J, Marala R B, Sharma R K
Renal Division, Brigham and Women's Hospital, Boston, MA.
Biochem Biophys Res Commun. 1988 Dec 15;157(2):755-61. doi: 10.1016/s0006-291x(88)80314-0.
The nature and regulation of atrial natriuretic peptide (ANP)-sensitive guanylate cyclase in rat renal glomerular membranes was examined. By affinity crosslinking techniques, three bands with apparent molecular masses of 180, 130 and 64 kDa were specifically labeled with [125I]ANP. A specific antibody to the 180 kDa membrane guanylate cyclase of rat adrenocortical carcinoma recognized a 180 kDa band on Western blot analysis of solubilized, GTP-affinity purified glomerular membrane proteins. The same antibody completely inhibited ANP-stimulated guanylate cyclase activity in glomerular membrane fractions. Partially purified protein kinase C inhibited ANP-stimulated guanylate cyclase activity in glomerular membrane fractions. It is concluded that a 180 kDa ANP-sensitive guanylate cyclase is present in glomerular membranes, and that this enzyme is inhibited directly by protein kinase C.
研究了大鼠肾小球膜中对心房利钠肽（ANP）敏感的鸟苷酸环化酶的性质和调节。通过亲和交联技术，用[125I]ANP特异性标记了三条表观分子量分别为180、130和64 kDa的条带。针对大鼠肾上腺皮质癌180 kDa膜鸟苷酸环化酶的特异性抗体，在对溶解的、经GTP亲和纯化的肾小球膜蛋白进行蛋白质印迹分析时识别出一条180 kDa的条带。相同抗体完全抑制肾小球膜组分中ANP刺激的鸟苷酸环化酶活性。部分纯化的蛋白激酶C抑制肾小球膜组分中ANP刺激的鸟苷酸环化酶活性。得出的结论是，肾小球膜中存在一种180 kDa的对ANP敏感的鸟苷酸环化酶，并且该酶直接受到蛋白激酶C的抑制。
