Protein kinase C isozymes and the regulation of diverse cell responses

Edward C. Dempsey, Alexandra C. Newton, Daria Mochly-Rosen, Alan P. Fields, Mary E. Reyland, Paul A. Insel, Robert O. Messing

Research output: Contribution to journalArticlepeer-review

674 Scopus citations


Individual protein kinase C (PKC) isozymes have been implicated in many cellular responses important in lung health and disease, including permeability, contraction, migration, hypertrophy, proliferation, apoptosis, and secretion. New ideas on mechanisms that regulate PKC activity, including the identification of a novel PKC kinase, 3-phosphoinositide-dependent kinase-1 (PDK-1), that regulates phosphorylation of PKC, have been advanced. The importance of targeted translocation of PKC and isozyme-specific binding proteins (like receptors for activated C-kinase and caveolins) is well established. Phosphorylation state and localization are now thought to be key determinants of isozyme activity and specificity. New concepts on the role of individual PKC isozymes in proliferation and apoptosis are emerging. Opposing roles for selected isozymes in the same cell system have been defined. Coupling to the Wnt signaling pathway has been described. Phenotypes for PKC knockout mice have recently been reported. More specific approaches for studying PKC isozymes and their role in cell responses have been developed. Strengths and weaknesses of different experimental strategies are reviewed. Future directions for investigation are identified.

Original languageEnglish (US)
Pages (from-to)L429-L438
JournalAmerican Journal of Physiology - Lung Cellular and Molecular Physiology
Issue number3 23-3
StatePublished - 2000


  • 3-Phosphoinositide-dependent kinase-1
  • Apoptosis
  • Proliferation
  • Pulmonary disease
  • Receptor for activated C-kinase
  • Transgenic mice

ASJC Scopus subject areas

  • Physiology
  • Pulmonary and Respiratory Medicine
  • Physiology (medical)
  • Cell Biology


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