佛波酯和胰岛素刺激大鼠脂肪细胞中的蛋白激酶C亚型。

Phorbol ester and insulin stimulate protein kinase C isoforms in rat adipocytes.

作者信息

Ishizuka T, Yamamoto M, Kajita K, Nagashima T, Taniguchi O, Wada H, Itaya S, Yasuda K

机构信息

Third Department of Internal Medicine, Gifu University School of Medicine, Japan.

出版信息

Diabetes Res Clin Pract. 1994 Dec 16;26(2):91-9. doi: 10.1016/0168-8227(94)90145-7.

DOI:10.1016/0168-8227(94)90145-7

PMID:7705199

Abstract

We examined effect of insulin or 12-O-tetradecanoyl phorbol 13-acetate (TPA) on the subcellular redistribution of protein kinase C isoforms in rat adipocytes. Total Mono Q column-elutable novel PKCs (nPKCs) which are Ca(2+)-independent and phospholipid-dependent protein kinases, decreased in the cytosolic fraction and increased in the membrane fraction during treatment with insulin or phorbol ester for 10 min. Immunoblot analysis of novel PKCs, -epsilon, -delta and -zeta, showed that insulin stimulated the translocation of these PKC isoforms from cytosol to membrane, similar to the translocation of conventional Ca2+/phospholipid-dependent PKCs (cPKCs), -alpha, -beta, and -gamma. Phorbol esters stimulated the translocation of PKC-alpha, -beta, -gamma, -epsilon and -delta, but not PKC-zeta. These results suggest that (a) insulin and phorbol esters similarly stimulate the translocation of each PKC isoform except for PKC-zeta, and (b) the translocation of both nPKCs and cPKCs occurs during insulin and TPA actions in rat adipocytes.

摘要

我们研究了胰岛素或12 - O - 十四烷酰佛波醇 - 13 - 乙酸酯（TPA）对大鼠脂肪细胞中蛋白激酶C亚型亚细胞重分布的影响。总单Q柱洗脱的新型蛋白激酶C（nPKCs）是不依赖Ca(2+)且依赖磷脂的蛋白激酶，在用胰岛素或佛波酯处理10分钟期间，其在胞质部分减少，在膜部分增加。对新型蛋白激酶C - ε、 - δ和 - ζ的免疫印迹分析表明，胰岛素刺激这些蛋白激酶C亚型从胞质溶胶向膜的转位，类似于传统的依赖Ca2 + /磷脂的蛋白激酶C（cPKCs） - α、 - β和 - γ的转位。佛波酯刺激蛋白激酶C - α、 - β、 - γ、 - ε和 - δ的转位，但不刺激蛋白激酶C - ζ的转位。这些结果表明：（a）除蛋白激酶C - ζ外，胰岛素和佛波酯类似地刺激每种蛋白激酶C亚型的转位；（b）在大鼠脂肪细胞中胰岛素和TPA作用期间，新型蛋白激酶C和传统蛋白激酶C均发生转位。