Membrane Signal Transduction via Protein Kinase C

  • C. W. Mahoney
  • R. Lüthy
  • A. Azzi

Abstract

Protein kinase C (PKC) is thought to play an important role in the signal transduction across the cell membrane in different cell types (Nishizuka 1984). Many different activators act via this pathway. PKC is activated by diacylglycerols that are produced by a phospholipase C as a consequence of the binding of an activator to a receptor. The activated PKC then phosphorylates intracellular substrates, which lead to the responses of the cell to the extracellular activator (Fig. 1). On the other hand, purified PKC binds phorbol esters, substances which have been known for many years as tumor promoters and nonphysiological cell activators (Hecker and Schmidt 1974). PKC is a Ca2+-activated, phospholipid-dependent enzyme and is modulated by phorbol esters and diacylglycerols: they activate PKC by lowering the amount of Ca2+ and phosphatidylserine needed for maximal activity (Castagna et al. 1982). The binding of radioactive phorbol esters can be inhibited competitively by diacylglycerols (Sharkey et al. 1984, Sharkey and Blumberg 1985), suggesting that diacylglycerol and phorbol esters have the same binding site.

Keywords

Vortex Manifold Iodine Superoxide Phenyl 

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Babior BM, Cohen HJ (1981) Leucocyte function. Churcill Livingstone Ed, New York, pp 1–38Google Scholar
  2. Bradford M (1976) Anal Biochem 72: 248–255PubMedCrossRefGoogle Scholar
  3. Castagna M, Takai Y, Kaibuchi K, Sano K, Kikkawa U, Nishizuka Y (1982) J Biol Chem 257: 7847–7851PubMedGoogle Scholar
  4. Hecker E, Schmidt R (1974) Chem Org Naturst 31: 377–467Google Scholar
  5. Hecker E, Schmidt R (1979) Fortschr Chem Org Naturstoff 31: 377–467CrossRefGoogle Scholar
  6. Inoue M, Kishimoto A, Takai Y, Nishizuka Y (1977) J Biol Chem 252: 7610–7616PubMedGoogle Scholar
  7. Kikkawa U, Minakuchi R, Takai Y, Nishizuka Y (1983) Methods Enzymol 99: 288–298PubMedCrossRefGoogle Scholar
  8. Kuo JF, Andersson RGG, Wise BC, Mackerlova L, Salomonsson I, Brackett NL, Katoh N, Shoji M, Wrenn RW (1980) Proc Natl Acad Sci USA 77: 7039–7043PubMedCrossRefGoogle Scholar
  9. Mori T, Takai Y, Yu B, Takahasi J, Nishizuka Y (1982) J Biochem 91: 427–431PubMedGoogle Scholar
  10. Nishizuka Y (1984) Nature (London) 308: 693–698CrossRefGoogle Scholar
  11. Schatzman RC, Raynor RL, Fritz RB, Kuo JF (1983) Biochem J 209: 435–443PubMedGoogle Scholar
  12. Sharkey NA, Blumberg PM (1985) Biochem Biophys Res Commun 133: 1051–1056PubMedCrossRefGoogle Scholar
  13. Sharkey NA, Leach KL, Blumberg PM (1984) Proc Natl Acad Sci USA 81: 607–610PubMedCrossRefGoogle Scholar
  14. Spector T (1978) Anal Biochem 86: 142–146PubMedCrossRefGoogle Scholar
  15. Walsh MP, Valentine KA, Ngai PK, Carruthers CA, Hollenberg MD (1984) Biochem J 224: 117–127PubMedGoogle Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 1986

Authors and Affiliations

  • C. W. Mahoney
  • R. Lüthy
  • A. Azzi

There are no affiliations available

Personalised recommendations