Modulation of Ca(v)3.2 T-type Ca2+ channels by protein kinase C

FEBS Lett. 2003 Jul 17;547(1-3):37-42. doi: 10.1016/s0014-5793(03)00665-3.


Although T-type Ca2+ channels have been implicated in numerous physiological functions, their regulations by protein kinases have been obscured by conflicting reports. We investigated the effects of protein kinase C (PKC) on Ca(v)3.2 T-type channels reconstituted in Xenopus oocytes. Phorbol-12-myristate-13-acetate (PMA) strongly enhanced the amplitude of Ca(v)3.2 channel currents (approximately 3-fold). The augmentation effects were not mimicked by 4alpha-PMA, an inactive stereoisomer of PMA, and abolished by preincubation with PKC inhibitors. Our findings suggest that PMA upregulates Ca(v)3.2 channel activity via activation of oocyte PKC.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Calcium Channels, T-Type / physiology*
  • Cloning, Molecular
  • Humans
  • Kinetics
  • Membrane Potentials / drug effects
  • Membrane Potentials / physiology
  • Oocytes / drug effects
  • Oocytes / physiology
  • Protein Kinase C / metabolism*
  • Recombinant Proteins / metabolism
  • Tetradecanoylphorbol Acetate / pharmacology
  • Xenopus


  • CACNA1H protein, human
  • Calcium Channels, T-Type
  • Recombinant Proteins
  • Protein Kinase C
  • Tetradecanoylphorbol Acetate