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Induction of vanilloid receptor channel activity by protein kinase C

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  • Louis S. Premkumar

    (Southern Illinois University School of Medicine)

  • Gerard P. Ahern

    (Southern Illinois University School of Medicine)

Abstract

Capsaicin or vanilloid receptors (VRs) participate in the sensation of thermal and inflammatory pain1,2,3. The cloned (VR1) and native VRs are non-selective cation channels directly activated by harmful heat, extracellular protons and vanilloid compounds4,5,6,7,8. However, considerable attention has been focused on identifying other signalling pathways in VR activation; it is known that VR1 is also expressed in non-sensory tissue1,9 and may mediate inflammatory rather than acute thermal pain3. Here we show that activation of protein kinase C (PKC) induces VR1 channel activity at room temperature in the absence of any other agonist. We also observed this effect in native VRs from sensory neurons, and phorbol esters induced a vanilloid-sensitive Ca2+ rise in these cells. Moreover, the pro-inflammatory peptide, bradykinin, and the putative endogenous ligand, anandamide, respectively induced and enhanced VR activity, in a PKC-dependent manner. These results suggest that PKC may link a range of stimuli to the activation of VRs.

Suggested Citation

  • Louis S. Premkumar & Gerard P. Ahern, 2000. "Induction of vanilloid receptor channel activity by protein kinase C," Nature, Nature, vol. 408(6815), pages 985-990, December.
    • Handle: RePEc:nat:nature:v:408:y:2000:i:6815:d:10.1038_35050121
    DOI: 10.1038/35050121
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