ADP-ribosylation of bradykinin and effects on its biological activities.
We investigated the ADP-ribosylation of bradykinin by hen liver nuclear ADP-ribosyltransferase. Two Arg residues of the peptide were modified by this enzyme. Arg1 was preferentially modified as compared to Arg9; the Vmax/Km for Arg1 was 3 times higher than that for Arg9. These results were given support by data observed in experiments with des-Arg1 and des-Arg9 bradykinin; the Vmax/Km for des-Arg9 bradykinin was 3 times that for des-Arg1 bradykinin. ADP-ribosylation suppressed the biological activity of bradykinin, as related to both binding and contractile activities. The extent of ADP-ribosylation-induced suppression of both activities was higher in the case of the modification of Arg1 than that of Arg9. In view of the observation of ADP-ribosyltransferase activity in skeletal, cardiac, and smooth muscles (Soman, G. et al. (1984) Biochem. Biophys. Res. Commun. 120, 973-980; Shimoyama, M. et al. (1987) in The 8th International Symposium on ADP-Ribosylation, Texas, abstract p. 13), bradykinin functioning in the contraction of smooth muscle may be modified in this way in vivo.
D036002:ADP Ribose Transferases; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001120:Arginine / Q000378:metabolism; D001920:Bradykinin / Q000378:metabolism* / Q000494:pharmacology; D002645:Chickens; D002851:Chromatography, High Pressure Liquid; D005260:Female; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D010430:Pentosyltransferases / Q000378:metabolism*; D010447:Peptide Hydrolases / Q000378:metabolism; D051381:Rats; D014590:Uterine Contraction / Q000187:drug effects
D000596:Amino Acids; D001120:Arginine; D036002:ADP Ribose Transferases; D010430:Pentosyltransferases; D010447:Peptide Hydrolases; D001920:Bradykinin