Modulation of TMEM16A-channel activity as Ca²⁺ activated Cl⁻ conductance via the interaction with actin cytoskeleton in murine portal vein

J Pharmacol Sci. 2014;125(1):107-11. doi: 10.1254/jphs.14015sc. Epub 2014 Apr 25.

Abstract

TMEM16A is a major component of Ca(2+)-activated Cl(-) channel (CaCC) conductance in murine portal vein smooth muscle cells (mPVSMCs). Here, the regulation of CaCC activity by the actin cytoskeleton was examined in mPVSMCs. Actin disruption by cytochalasin D did not affect the current density, but increased the deactivation time constant in mPVSMCs. The elongated deactivation was recovered by jasplakinolide. When murine TMEM16A was transfected into HEK293 cells that have a poorly developed actin cytoskeleton, electrophysiological properties of CaCC currents were not changed by cytochalasin D. In conclusion, the CaCC activity in mPVSMCs is modified by the interaction of TMEM16A with abundant actin cytoskeleton.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actin Cytoskeleton / physiology*
  • Animals
  • Anoctamin-1
  • Cells, Cultured
  • Chloride Channels / genetics
  • Chloride Channels / physiology*
  • Cytochalasin D / pharmacology
  • Depsipeptides / pharmacology
  • Electrophysiological Phenomena / drug effects
  • Electrophysiological Phenomena / genetics*
  • HEK293 Cells
  • Humans
  • Mice
  • Muscle, Smooth, Vascular
  • Portal Vein / cytology*
  • Transfection

Substances

  • ANO1 protein, mouse
  • Anoctamin-1
  • Chloride Channels
  • Clca3a1 protein, mouse
  • Depsipeptides
  • jasplakinolide
  • Cytochalasin D