熊去氧胆酸可促进大鼠肝细胞胞质溶胶中的蛋白质磷酸化。

Ursodeoxycholate promotes protein phosphorylation in the cytosol of rat hepatocytes.

作者信息

Capuano F, Barone M, D'Eri N, Russo E, Varone D, Francavilla A, Papa S

机构信息

Institute of Medical Biochemistry and Chemistry, University of Bari, Italy.

出版信息

Biochem Mol Biol Int. 1997 Feb;41(2):329-37. doi: 10.1080/15216549700201341.

DOI:10.1080/15216549700201341

PMID:9063573

Abstract

A study is presented of the effect of the bile salt ursodeoxycholate (UDC) on protein phosphorylation by [gamma-32P]ATP in the cytosol from rat hepatocytes. Gel electrophoresis and corresponding autoradiograms of cytosolic proteins show that UDC promotes phosphorylation of at least eight different protein bands. Four of them (the 36, 60, 64 and 76 kDa) are phosphorylated by Ca2+ and phospholipid-dependent protein kinase (PKC); three (the 31, 51 and 71 kDa) are phosphorylated by cAMP-dependent protein kinase (PKA) and one protein band, with molecular weight of 34 kDa, apparently contains substrates of both PKC and PKA. Data are reported indicating that UDC can directly affect the intrinsic activity of protein kinases.

摘要

本文呈现了一项关于胆汁盐熊去氧胆酸（UDC）对大鼠肝细胞胞质溶胶中[γ-32P]ATP介导的蛋白质磷酸化作用的研究。胞质蛋白的凝胶电泳及相应放射自显影片显示，UDC可促进至少八条不同蛋白条带的磷酸化。其中四条（36、60、64和76 kDa）由Ca2+和磷脂依赖性蛋白激酶（PKC）磷酸化；三条（31、51和71 kDa）由cAMP依赖性蛋白激酶（PKA）磷酸化，一条分子量为34 kDa的蛋白条带显然同时含有PKC和PKA的底物。报告的数据表明，UDC可直接影响蛋白激酶的内在活性。