ADP-ribosylation of myelin basic protein by cholera toxin.
Cholera toxin ADP-ribosylates four types of myelin basic proteins (MBPs) of Mr 14,000, 17,500, 19,000 and 22,000 in rat brain myelin. On an analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, MBP underwent mono- and multi-(ADP-ribosyl)ation by cholera toxin and thus modified MBP migrated on the gel as several discrete protein bands, the molecular masses of which were apparently larger by 500-2000 daltons than that of the corresponding untreated MBP. On average, 1.1 mol of ADP-ribosyl residue was incorporated into 1 mol of MBP. Four types of purified MBPs were also ADP-ribosylated by cholera toxin dependent on GTP and the protein factor for the ADP-ribosylation. The results show evidence that MBP is one of major and specific substrates of cholera toxin in brain membranes.
Department of Pharmacology, Saga Medical School, Japan.
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Enomoto
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Asakawa
D001921:Brain / Q000187:drug effects / Q000201:enzymology*; D002462:Cell Membrane / Q000187:drug effects / Q000201:enzymology; D002772:Cholera Toxin / Q000494:pharmacology*; D004591:Electrophoresis, Polyacrylamide Gel; D007700:Kinetics; D008970:Molecular Weight; D004676:Myelin Basic Protein / Q000378:metabolism*; D009243:NAD / Q000494:pharmacology; D011065:Poly(ADP-ribose) Polymerases / Q000378:metabolism*; D013379:Substrate Specificity
D004676:Myelin Basic Protein; D009243:NAD; D002772:Cholera Toxin; D011065:Poly(ADP-ribose) Polymerases