Regulation of Growth Factor Receptors by Protein Kinase C

  • Laura M. Mudd
  • Mohan K. Raizada


Insulin, insulin-like growth factor-I (IGF-I) and epidermal growth factor (EGF) all act to stimulate growth in many tissues. All three growth factors must first bind to specific membrane receptors to exert their actions. Upon binding of the appropriate ligand, these growth factor receptors exhibit increased tyrosine kinase activity, which is thought to be the second messenger, or pathway by which they cause some, if not all, of their effects within the cell (Evered et al., 1985; Raizada et al., 1986). Activation of these receptors by ligand binding causes different physiological effects in different cell types. These receptors also differ with regard to regulation of the receptors and/or of events beyond the receptors. As protein kinase C (PKC) has been shown to mimic some of these receptor actions and inhibit others, much attention has been focused on the effects of PKC on the tyrosine kinase receptors in order to determine first whether, and then how, PKC regulates those receptors. The following is a brief review of those studies.


Epidermal Growth Factor Receptor Insulin Receptor Phorbol Ester Insulin Binding Epidermal Growth Factor Receptor Phosphorylation 
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Copyright information

© Plenum Press, New York 1989

Authors and Affiliations

  • Laura M. Mudd
    • 1
  • Mohan K. Raizada
    • 1
  1. 1.Department of PhysiologyUniversity of FloridaGainesvilleUSA

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