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Protein Kinase C — Structural Studies

  • Peter J. Parker
  • Richard Marais
  • Mona Bajaj
  • Fiona Mitchell
  • Peter King
  • Sue Young
  • Axel Ullrich
  • Silvia Stabel
Part of the Advances in Experimental Medicine and Biology book series (NATO ASI F, volume 231)

Abstract

Protein kinase C was first reported by Nishizuka and colleagues. This group identified a histone kinase activity that was irreversibly activated by mM concentrations of Ca2+ (Takai et al., 1977), an effect shown to be due to proteolysis of the holoenzyme by contaminating Ca2+-activated neutral protease (Inoue et al., 1977). Reversible activation was subsequently shown to occur in response to Ca2+ (~10-5M) and anionic phospholipid, phosphatidylserine being the most effective (Takai et al., 1979). Furthermore, activation could be effected at physiological Ca2+ concentrations (~10-6M) if the neutral lipid diacylglycerol was also present (Kishimoto et al., 1980). These characteristics of protein kinase C have led to the operational definition of the enzyme as a Ca2+/phospholipid dependent protein kinase.

Keywords

Protein Kinase Epidermal Growth Factor Receptor Phorbol Ester Dependent Protein Kinase Human Fetal Brain 
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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Copyright information

© Springer Science+Business Media New York 1988

Authors and Affiliations

  • Peter J. Parker
    • 1
  • Richard Marais
    • 1
  • Mona Bajaj
    • 1
  • Fiona Mitchell
    • 1
  • Peter King
    • 1
  • Sue Young
    • 2
  • Axel Ullrich
    • 3
  • Silvia Stabel
    • 1
  1. 1.Ludwig Institute for Cancer ResearchLondonEngland
  2. 2.Imperial Cancer Research FundLondonEngland
  3. 3.Genentech Inc.South San FranciscoUSA

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