Effect of Polyamines on Protein Kinase C Activation Process

  • Maria Stella Moruzzi
  • Giorgio Piccinini
  • Bruna Tadolini
  • Maria Giuseppina Monti
  • Bruno Barbiroli
  • Gabriele Mezzetti
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 250)


Protein phosphorylation and dephosphorylation are major mechanisms for signal transduction in biological systems (Krebs, 1985) and are fundamental in the regulation of many cellular activities (Rubin and Rosen, 1975). The Ca2+ and phospholipid-dependent protein kinase C (PKC) is a key regulatory enzyme believed to be involved in basic cell functions such as proliferation and differentiation (Schwantke et al., 1985). Activation of PKC by diacylglycerol (DAG) has linked the activity of this enzyme to the function of many stimuli acting via phosphatidylinositol turnover (Berridge, 1987). Indeed DAG has been postulated to be the second messenger able to activate PKC without a change in cytosolic Ca2+ concentration. Biologically active phorbol esters which usually act as tumor promoters also activate PKC and are presumed to exert their functions in this way; indeed this enzyme appears to be a cellular phorbol ester receptor (Ashendel, 1985).


Phorbol Ester Phospholipid Vesicle Acidic Phospholipid PDBu Binding Phorbol Dibutyrate 


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Copyright information

© Plenum Press, New York 1988

Authors and Affiliations

  • Maria Stella Moruzzi
    • 1
  • Giorgio Piccinini
    • 1
  • Bruna Tadolini
    • 1
    • 2
  • Maria Giuseppina Monti
    • 1
  • Bruno Barbiroli
    • 1
    • 3
  • Gabriele Mezzetti
    • 1
  1. 1.Istituto di Chimica BiologicaUniversità di ModenaItaly
  2. 2.Dipartimento di BiochimicaUniversità di BolognaItaly
  3. 3.Cattedra di Biologia MolecolareUniversité di BolognaItaly

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