Modulation of TMEM16A-channel activity as Ca²⁺ activated Cl⁻ conductance via the interaction with actin cytoskeleton in murine portal vein.
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.
Department of Molecular and Cellular Pharmacology, Graduate School of Pharmaceutical Sciences, Nagoya City University, Japan.
Junya
J
Ohshiro
Hisao
H
Yamamura
Yoshiaki
Y
Suzuki
Yuji
Y
Imaizumi
D008841:Actin Cytoskeleton / Q000502:physiology*; D000818:Animals; D000075369:Anoctamin-1; D002478:Cells, Cultured; D018118:Chloride Channels / Q000235:genetics / Q000502:physiology*; D015638:Cytochalasin D / Q000494:pharmacology; D047630:Depsipeptides / Q000494:pharmacology; D055724:Electrophysiological Phenomena / Q000187:drug effects / Q000235:genetics*; D057809:HEK293 Cells; D006801:Humans; D051379:Mice; D009131:Muscle, Smooth, Vascular; D011169:Portal Vein / Q000166:cytology*; D014162:Transfection
C531181:ANO1 protein, mouse; D000075369:Anoctamin-1; D018118:Chloride Channels; C116464:Clca3a1 protein, mouse; D047630:Depsipeptides; C057531:jasplakinolide; D015638:Cytochalasin D