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J. Biochem, 1988, Vol. 103, No. 2 342-347
© 1988 Japanese Biochemical Society

research-article

ADP-Ribosylation of Bradykinin and Effects on Its Biological Activities1

Koichi Mishima*, Yoshinori Tanigawa*, Nobumasa Hara**, Mikako Tsuchiya*, Takahisa Ushiroyama***, Yasuro Yoshimura**** and Makoto Shimoyama*

* Department of Biochemistry Izumo, Shimane 693
** Central Research Laboratories Izumo, Shimane 693
*** Department of Oral and Maxillofacial Surgery, Shimane Medical University Izumo, Shimane 693
**** Department of Obstetrics and Gynecology, Osaka Medical College Takatsuki, Osaka 569

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.

1This work was supported by Grants-in-aid for Scientific Research (No. 62580151) and Cancer Research (No. 62010086) from the Ministry of Education, Science and Culture of Japan.


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