Review Protein kinase C and T cell activation

  • Nicola Berry
  • Yasutomi Nishizuka
Part of the European Journal of Biochemistry book series (EJB REVIEWS, volume 1990)


Understanding the intracellular mechanisms by which binding of ligands, such as hormones and growth factors, to their specific receptors elicits the appropriate cellular response has long been a topic of great interest. Considerable excitement was generated when it was recognised that several receptor-ligand interactions operate via the hydrolysis of inositol phospholipids. This yields, at least, two ‘second messengers’, namely, inositol 1,4,5-trisphosphate [Ins(l,4,5)P 3], which causes the release of Ca2+ from intracellular stores, and 1,2- diacylglycerol (ac2Gro), which activates the serine/threonine-specific enzyme, protein kinase C(PKC), reviewed in [1] and [2]. The pertinent question that follows is, how do PKC activation and elevation of the intracellular Ca2 + concentration evoke cell responses? In this review, attention has been focussed on PKC, and the consequences of its activation in resting human T cells. Evidence that PKC activity is, at least partially, responsible for activation of resting human T cells will be examined, and some of the more recent research investigating how PKC activation elicits this cell response will be described.


Phorbol Ester Accessory Cell Protein Kinase Domain Inositol Phospholipid Accessory Signal 
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.







protein kinase C




interleukin-2 receptor


55-fDa subunit of the IL-2R


T cell receptor


lymphocyte function-associated antigen-3








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Copyright information

© FEBS 1990

Authors and Affiliations

  • Nicola Berry
    • 1
  • Yasutomi Nishizuka
    • 1
  1. 1.Department of BiochemistryKobe University School of MedicineKobeJapan

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