Abstract
Mono-ADP-ribosylation, In which the ADP-ribosyl moiety is transferred from NAD to an acceptor protein, is one of the important posttranslational modifications of cellular proteins. Because mounting evidence suggests significant biological roles of this reaction in transmembrane signal transduction and other cell metabolic reactions, we assessed how long-term alcohol intake alters toxin catalyzed- and endogenous mono-ADP-ribosylation in the liver of a rat model. We first found that thiol-preactivated cholera toxin-catalyzed ADP-ribosylation of the alpha-subunit of the stimulatory GTP-binding protein was enhanced after long-term alcohol intake. Unexpectedly, but interestingly, this enhancement was not accompanied by a concomitant increase of cholera toxin-catalyzed stimulation of the adenylate cyclase activity. We also found that long-term alcohol intake remarkably enhanced endogenous mono-ADP-ribosylation of a 58 kDa protein in plasma membranes. Thus, long-term alcohol intake stimulated endogenous, as well as, toxin-catalyzed mono-ADP-ribosylations. Characterization of the 58 kDa protein may uncover pathophysiological roles of this interesting phenomenon in alcohol-induced liver damage.
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