Endogenous ADP-ribosylation in skeletal muscle membranes.
The characteristics of ADP-ribosyltransferase activity in skeletal muscle membranes have been studied. The membrane enzymes can ADP-ribosylate exogenous substrates such as guanylhydrazones, polyarginine, lysozyme, and histones. The properties of the enzyme are investigated by using diethylaminobenzylidineaminoguanidine as a model substrate. Incubation of the membranes with [32P]adenylate-labeled NAD results in the labeling of a number of cellular proteins. Magnesium ions, detergents, and diethylaminobenzylidineaminoguanidine stimulated the ADP-ribosylation of membrane proteins, whereas L-arginine methyl ester and arginine inhibited ADP-ribosylation. The labeling of specific proteins in the sarcoplasmic reticulum and glycogen pellet is influenced significantly by detergents, nucleotides, and thiols. The hydroxylamine sensitivity of the ADP-ribose linkage in the membrane proteins is similar to that reported for (ADP-ribose)-arginine linkage. Snake venom phosphodiesterase digestion of the ADP-ribosylated membranes produces 5'-AMP as the major acid-soluble digestion product. The results suggest that the primary mode of modification is mono(ADP-ribosyl)ation. The ADP-ribosyltransferase activity in the membrane preparations is not extracted under conditions used for solubilization of extrinsic proteins, suggesting that the activity is associated with some integral membrane protein.
D036002:ADP Ribose Transferases; D000818:Animals; D006657:Histones / Q000378:metabolism; D008565:Membrane Proteins / Q000378:metabolism; D008935:Mitoguazone / Q000378:metabolism; D009113:Muramidase / Q000378:metabolism; D009132:Muscles / Q000201:enzymology*; D010430:Pentosyltransferases / Q000378:metabolism*; D010455:Peptides / Q000378:metabolism; D012508:Sarcolemma / Q000201:enzymology*; D013552:Swine
D006657:Histones; D008565:Membrane Proteins; D010455:Peptides; C015462:polyarginine; D036002:ADP Ribose Transferases; D010430:Pentosyltransferases; D009113:Muramidase; D008935:Mitoguazone