The 52 kDa Adp-Ribosylated Protein in the Rat Heart Plasma Membrane: Is It Gsa?

  • Kathryn K. McMahon
  • Kristien J. Piron
Conference paper


G proteins1 are a family of heterotrimeric molecules that are implicated in a variety of signal transduction processes (for review see 1). ADP-ribosylation is a covalent modification which transfers the ADP-ribose moiety of NAD to cellular acceptor proteins. Several bacterial toxins posses this ADP-ribosyltransferase activity and modify several G proteins. For example, cholera toxin can ADP-ribosylate the α subunits of the G proteins Gs and transducin (1). These toxins may mimic endogenous processes and G proteins may be endogenously ADP-ribosylated. Indeed several authors have demonstrated that Gsα can be ADP-ribosylated by endogenous ADP-ribosyltransferases (2-6). In liver membranes, a 55 kDa protein which was speculated to be Gsα is ADP-ribosylated in both the absence and presence of cholera toxin. In the presence of isoproterenol ADP-ribosylation of this protein is increased (6). In NG108-15 hybrid cells (5) and in platelets (4) ADP-ribosylation of Gsα has been implicated in heterologous desensitization to prostacyclins. Recently, it was also shown that in canine sarcolemma, adenylyl cyclase might be regulated by endogenous, reversible ADP-ribosylation of Gsα (7).


Cholera Toxin Plasma Membrane Fraction Signal Transduction Process Guanine Nucleotide Binding Protein Liver Membrane 
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  1. 1.
    Freissmuth, M., Casey, P.J., and Gilman, A.G. (1989) FASEB J. 3, 2125–2131.PubMedGoogle Scholar
  2. 2.
    Jacquemin, C., Thibout, H., Lambert, B. and Correze, C. (1986) Nature 323, 182–184.PubMedCrossRefGoogle Scholar
  3. 3.
    Clark, J.A., Terwilliger, R.Z., Nestler, E.J. and Duman, R.S. (1989) Society for Neuroscience Abstracts Vol. 15, 435.Google Scholar
  4. 4.
    Molina y Vedia, L., Nolan, R.D. and Lapetina, E.G. (1989) Biochem. J. 261, 841–845.PubMedGoogle Scholar
  5. 5.
    Donnelly, L.E., Boyd, R.S., and MacDermot, J. (1991) Br. J. Pharmacol. 102, 34P.Google Scholar
  6. 6.
    Reilly, T.M., Bechner, S., McHugh, E.M. and Blechner, M. (1981) Biochem. Biophys. Res. Commun. 98, 1115–1120.PubMedCrossRefGoogle Scholar
  7. 7.
    Quist, E.E., Coyle, D.L., Aboul-Ela, N. and Jacobson, M.K. (1991) FASEB J. 5, A1506.Google Scholar
  8. 8.
    Piron, K.J. and McMahon, K.K. (1990) Biochem. J. 270, 591–597.PubMedGoogle Scholar
  9. 9.
    Harris, B.A., Robishow, J.D., Mumby, S.M. and Gilman, A.G. (1985) Science 229, 1274–1277.PubMedCrossRefGoogle Scholar
  10. 10.
    Graziano, M. P., Freissmuth, M. and Gilman, A.G. (1989) J. Biol. Chem. 264, 409–418.PubMedGoogle Scholar
  11. 11.
    Piron, KJ. and McMahon, K.K. (1991) FASEB J. 5, A1177.Google Scholar
  12. 12.
    Mumby, S.M. and Gilman, A.G. (1991) Methods of Enzymology, 195, 215–233.CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1992

Authors and Affiliations

  • Kathryn K. McMahon
  • Kristien J. Piron

There are no affiliations available

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