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Multiple Intracellular Peptide Mediators of Insulin Action

  • K. Cheng
  • M. Thompson
  • C. Schwartz
  • C. Malchoff
  • S. Tamura
  • J. Craig
  • E. Locher
  • J. Larner

Abstract

This chapter discusses a cluster of insulin mediator peptides that duplicate in vitro the following insulin actions in the cell: (1) inhibit cyclic adenosine monophosphate (cAMP)dependent protein kinase, (2) stimulate pyruvate dehydrogenase (PDH) phosphatase, (3) inhibit hormone-stimulated adenylate cyclase, and (4) stimulate glycogen synthase phosphoprotein phosphatase. Also discussed is a post-insulin receptor defect in human leprechaun fibroblast cells that sheds light on the mechanism of action of insulin. Finally, the possible relationship between insulin receptor phosphorylation and mediator formation is considered. It is clear that several mediators of varying molecular size is formed from proteins in the cell membrane following insulin binding to the receptor and that these mediators carry out some of the actions of insulin constituting the pleiotypic program. A model of mediator formation similar to the pro-opiomelanocortin model of peptide hormone formation is proposed. A recent review of this topic has appeared.(1)

Keywords

Insulin Action Pyruvate Dehydrogenase Insulin Binding Multiple Mediator Mediator Formation 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. 1.
    Lamer, J., J. Cyclic Nucleotide Res., 1982, 8: 289–296.Google Scholar
  2. 2.
    Lamer, J., Huang, L.C., Brooker, G., Murad, F., and Miller, T.B., 1974, Fed. Proc. 33: 61.Google Scholar
  3. 3.
    Saltiel, A., Siegel, M.I., Jacobs, S., and Cuatrecasas, P., 1982, Proc. Natl. Acad. Sci. USA 79: 3513–3517.PubMedCrossRefGoogle Scholar
  4. 4.
    Smith, C.H., and Lamer, J., 1972, Biochem. Biophys. Acta 264: 224–228.PubMedCrossRefGoogle Scholar
  5. 5.
    Takai, Y., Kishimoto, A., Iwasa, Y., Kawahara, Y., Mori, T., and Nishizuka, Y., 1979, J. Biol. Chem. 254: 3692–3695.PubMedGoogle Scholar
  6. 6.
    Perisic, O., and Traugh, J.A., 1983, J. Biol. Chem. 258: 9589–9592.PubMedGoogle Scholar
  7. 7.
    Hershko, A., and Ciechanover, A., 1982, Annu. Rev. Biochem. 51: 335–364.PubMedCrossRefGoogle Scholar
  8. 8.
    Craig, J.W., Lamer, J., Locker, E.F., and Elders, M.J., 1984, Mol. and Cell. Biochem.,in press.Google Scholar

Copyright information

© Plenum Press, New York 1985

Authors and Affiliations

  • K. Cheng
    • 1
  • M. Thompson
    • 1
  • C. Schwartz
    • 1
  • C. Malchoff
    • 3
  • S. Tamura
    • 1
  • J. Craig
    • 2
  • E. Locher
    • 2
  • J. Larner
    • 1
  1. 1.Department of PharmacologyUniversity of Virginia School of MedicineCharlottesvilleUSA
  2. 2.Department of Internal MedicineUniversity of Virginia School of MedicineCharlottesvilleUSA
  3. 3.Departments of Pharmacology and Internal MedicineUniversity of Virginia School of MedicineCharlottesvilleUSA

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