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Related Experiment Videos

Smooth muscle protein kinase C

M P Walsh1, J E Andrea, B G Allen

  • 1Medical Research Council Group in Signal Transduction, University of Calgary, AB, Canada.

Canadian Journal of Physiology and Pharmacology
|November 1, 1994
PubMed
Summary

Protein kinase C (PKC) activation can cause smooth muscle contraction without increasing intracellular calcium. This calcium-independent pathway involves PKC epsilon and may regulate muscle contraction via thin filament protein phosphorylation.

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Area of Science:

  • Cellular Physiology
  • Molecular Biology
  • Biochemistry

Background:

  • Protein kinase C (PKC) is implicated in smooth muscle contraction.
  • Phorbol esters induce sustained contractions in some vascular smooth muscles.
  • These contractions can occur independently of changes in intracellular calcium concentration ([Ca]i) or myosin light chain phosphorylation.

Purpose of the Study:

  • To investigate the mechanism of calcium-independent smooth muscle contraction mediated by PKC.
  • To identify the specific PKC isoenzyme involved.
  • To elucidate the downstream signaling pathways activated by PKC in this process.

Main Methods:

  • Utilized saponin-permeabilized single ferret aortic smooth muscle cells.
  • Stimulated cells with phenylephrine at low free [Ca2+] (pCa 7.0-8.6).

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  • Administered the constitutively active PKC fragment (PKM) and a PKC inhibitor peptide.

    • Main Results:

    • Phenylephrine induced contraction at low [Ca2+] in permeabilized cells.
    • PKM also elicited contraction, comparable to phenylephrine-induced force.
    • Both contractions were reversed by a PKC-specific inhibitor peptide.
    • PKC epsilon is suggested as the likely calcium-independent isoenzyme involved.

    Conclusions:

    • Alpha-adrenergic agonists can trigger vascular smooth muscle contraction without an increase in [Ca]i.
    • This pathway involves diacylglycerol generation and activation of novel PKCs, likely PKC epsilon.
    • PKC activation may lead to thin filament protein (caldesmon, calponin) phosphorylation, altering cross-bridge cycling.