在培养的兔主动脉平滑肌细胞中具有不同功能的两种蛋白激酶C

Two types of protein kinase C with different functions in cultured rabbit aortic smooth muscle cells.

作者信息

Kariya K, Kawahara Y, Fukuzaki H, Hagiwara M, Hidaka H, Fukumoto Y, Takai Y

机构信息

Department of Biochemistry, Kobe University School of Medicine, Japan.

出版信息

Biochem Biophys Res Commun. 1989 Jun 30;161(3):1020-7. doi: 10.1016/0006-291x(89)91345-4.

DOI:10.1016/0006-291x(89)91345-4

PMID:2742575

Abstract

Incubation of cultured rabbit aortic smooth muscle cells (SMC) with phorbol-12, 13-dibutyrate (PDBu) for 48 h caused the down-regulation of protein kinase C (PKC) to the level of 30-40% of that in the control cells. The proliferative and antiproliferative actions of PKC were abolished in parallel with the loss of the down-regulation-sensitive component of PKC, but the inhibitory actions in the whole blood serum (WBS)-induced phospholipase C (PLC) reactions and intracellular Ca2+ mobilization were not affected. Immunoblot analysis with specific monoclonal antibodies against three PKC isozymes (type I, II and III) revealed that only the type III isozyme was detected in rabbit aortic SMC and that this isozyme completely disappeared after the incubation with PDBu. These results indicate that the type III isozyme is responsible for the proliferative and antiproliferative actions and suggest that the unidentified isozyme(s) is involved in the inhibitory actions in the WBS-induced PLC reactions and intracellular Ca2+ mobilization in rabbit aortic SMC.

摘要

将培养的兔主动脉平滑肌细胞（SMC）与佛波醇-12,13-二丁酸酯（PDBu）孵育48小时，导致蛋白激酶C（PKC）下调至对照细胞中该酶水平的30%-40%。PKC的增殖和抗增殖作用与PKC下调敏感成分的丧失同时被消除，但对全血血清（WBS）诱导的磷脂酶C（PLC）反应和细胞内Ca2+动员的抑制作用不受影响。用针对三种PKC同工酶（I型、II型和III型）的特异性单克隆抗体进行免疫印迹分析表明，在兔主动脉SMC中仅检测到III型同工酶，并且该同工酶在与PDBu孵育后完全消失。这些结果表明III型同工酶负责增殖和抗增殖作用，并提示未鉴定的同工酶参与兔主动脉SMC中WBS诱导的PLC反应和细胞内Ca2+动员的抑制作用。