JBC DNA damage antibodies

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Volume 270, Number 14, Issue of April 7, 1995 pp. 8115-8121
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
Identification of Gangliosides as Inhibitors of ADP-ribosyltransferases of Pertussis Toxin and Exoenzyme C3 from Clostridium botulinum

(Received for publication, October 25, 1994; and in revised form, December 28, 1994)

Miki Hara-Yokoyama ,  Yoshio Hirabayashi ,  Fumitoshi Irie ,  Bunei Syuto ,  Kohji Moriishi ,  Hiroshi Sugiya ,  Shunsuke Furuyama

We have previously reported the presence of an endogenous inhibitory activity in bovine brain for the ADP-ribosylation of GTP-binding proteins catalyzed by pertussis toxin (PT) (Hara-Yokoyama, M., and Furuyama, S.(1989) Biochem. Biophys. Res. Commun. 160, 67-71). In the present study, we identified the inhibitor as a ganglioside. The screening of various gangliosides revealed that G most effectively inhibited the ADP-ribosyltransferase activities of both the holoenzyme and the catalytic subunit of PT. G is a ganglioside newly identified as one of the antigens recognized by the cholinergic neuron-specific antibody, anti-Chol-1alpha (Hirabayashi, Y., Nakao, T., Irie, F., Whittaker, V.P., Kon, K., and Ando, S.(1992) J. Biol. Chem. 267, 12973-12978). G also inhibited the PT-catalyzed NAD glycohydrolysis. Unlike PT activity, the ADP-ribosylation and the NAD glycohydrolysis catalyzed by the C3 exoenzyme from Clostridium botulinum type C were inhibited by G and G. The ADP-ribosylation catalyzed by either PT or the C3 exoenzyme was not inhibited by ceramide, galactocerebroside, or sialic acid. In addition to the inhibitory action of gangliosides on ADP-ribosylation, the importance of gangliosides as regulators of NAD metabolism is discussed.



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Copyright © 1995 by the American Society for Biochemistry and Molecular Biology.