MONO-ADP-RIBOSYLATION OF GS BY AN EUKARYOTIC ARGININE-SPECIFIC ADP-RIBOSYLTRANSFERASE STIMULATES THE ADENYLATE-CYCLASE SYSTEM

被引：24

作者：

INAGEDA, K

NISHINA, H

TANUMA, SI

机构：

[1] Department of Life Science, Faculty of Bioscience, Biotechnology Tokyo Institute of Technology Nagatsuta, Midori-ku, Yokohama

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1991年 / 176卷 / 03期

关键词：

D O I：

10.1016/0006-291X(91)90383-I

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

An arginine-specific ADP-ribosyltransferase, named ADP-ribosyltransferase A, was partially purified from human platelets using polyarginine as an ADP-ribose acceptor. When human platelet membranes were incubated with the transferase A in the presence of NAD+, Gs, a stimulatory guanine nucleotide-binding protein of the adenylate cyclase was specifically mono-ADP-ribosylated. ADP-ribose transfer to Gs by this enzyme was suppressed when membranes were pre-ADP-ribosylated by cholera toxin. Incubation of membranes with the transferase A resulted in activation of the adenylate cyclase system. This stimulatory effect of the transferase A on the adenylate cyclase system was inhibited by the presence of polyarginine. These results indicate a role of ADP-ribosyltransferase A in regulation of the adenylate cyclase system via endogenous mono-ADP-ribosylation of Gs. © 1991.

引用

页码：1014 / 1019

页数：6

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