Long-term alcohol intake enhances ADP-ribosylation of the multifunctional enzyme, phosphoglucomutase, in rat liver

✍ Scribed by F Nomura; M Noda; M Miyake; T Nakai

• Publisher: John Wiley and Sons
• Year: 1996
• Tongue: English
• Weight: 309 KB
• Volume: 24
• Category: Article
• ISSN: 0270-9139
• DOI: 10.1002/hep.510240543

✦ Synopsis

identified in various eukaryotic cells, and mounting evidence Adenosine diphosphate (ADP)-ribosylation is a postsuggests that endogenous ADP-ribosylation plays significant translational protein modification that, in turn, alters biological roles in mammalian cells. [7][8][9][10][11] These enzymes may several regulatory proteins in mammalian cells. We dembe involved in the regulation of adenylate cyclase, 12,13 Ca 2/ onstrated that long-term alcohol intake enhanced the release from mitochondria, 14 and the phosphorylation of nu-ADP-ribosylation of a 58-kd protein in rat liver plasma clear proteins. 15 In view of the diverse roles of ADP-ribosylamembranes. To assess the biological significance of this tion in cells, the effects of alcohol on this reaction are of phenomenon, we partially purified the 58-kd acceptor interest. We demonstrated that long-term alcohol intake reprotein from solubilized rat liver homogenates by two markably enhanced the endogenous ADP-ribosylation of a sequential preparative high-pressure liquid chromato-58-kd hepatic protein in the rat. 16 To further clarify the biographies. Microsequencing revealed that it was logical roles of this phenomenon, the 58-kd protein needed phosphoglucomutase (PGM) (EC 5,4,2,2). This enzyme to be identified. We describe here that the 58-kd protein is underwent negligible auto ADP-ribosylation, but the the multifunctional enzyme, phosphoglucomutase (PGM) (EC ADP-ribosylation was remarkably increased by adding 5,4,2,2). The modification of this enzyme by ADP-ribose was rat liver plasma membranes. The extent of the increase increased by chronic alcohol consumption. was greater in alcohol-fed rats than in pair-fed controls, suggesting enhanced enzyme activities toward ADP-ri-