Modulation of TMEM16A-Channel Activity as Ca2+ Activated Cl− Conductance via the Interaction With Actin Cytoskeleton in Murine Portal Vein
Abstract.: TMEM16A is a major component of Ca2+-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...
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doaj-198a282206f147199978e85d5f00ad4a2020-11-24T22:00:36ZengElsevierJournal of Pharmacological Sciences1347-86132014-01-011251107111Modulation of TMEM16A-Channel Activity as Ca2+ Activated Cl− Conductance via the Interaction With Actin Cytoskeleton in Murine Portal VeinJunya Ohshiro0Hisao Yamamura1Yoshiaki Suzuki2Yuji Imaizumi3Department of Molecular and Cellular Pharmacology, Graduate School of Pharmaceutical Sciences, Nagoya City University, Nagoya 467-8603, JapanDepartment of Molecular and Cellular Pharmacology, Graduate School of Pharmaceutical Sciences, Nagoya City University, Nagoya 467-8603, JapanDepartment of Molecular and Cellular Pharmacology, Graduate School of Pharmaceutical Sciences, Nagoya City University, Nagoya 467-8603, JapanDepartment of Molecular and Cellular Pharmacology, Graduate School of Pharmaceutical Sciences, Nagoya City University, Nagoya 467-8603, Japan; Corresponding author. yimaizum@phar.nagoya-cu.ac.jpAbstract.: TMEM16A is a major component of Ca2+-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. Keywords:: TMEM16A, actin cytoskeleton, portal veinhttp://www.sciencedirect.com/science/article/pii/S1347861319301586 |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Junya Ohshiro Hisao Yamamura Yoshiaki Suzuki Yuji Imaizumi |
spellingShingle |
Junya Ohshiro Hisao Yamamura Yoshiaki Suzuki Yuji Imaizumi Modulation of TMEM16A-Channel Activity as Ca2+ Activated Cl− Conductance via the Interaction With Actin Cytoskeleton in Murine Portal Vein Journal of Pharmacological Sciences |
author_facet |
Junya Ohshiro Hisao Yamamura Yoshiaki Suzuki Yuji Imaizumi |
author_sort |
Junya Ohshiro |
title |
Modulation of TMEM16A-Channel Activity as Ca2+ Activated Cl− Conductance via the Interaction With Actin Cytoskeleton in Murine Portal Vein |
title_short |
Modulation of TMEM16A-Channel Activity as Ca2+ Activated Cl− Conductance via the Interaction With Actin Cytoskeleton in Murine Portal Vein |
title_full |
Modulation of TMEM16A-Channel Activity as Ca2+ Activated Cl− Conductance via the Interaction With Actin Cytoskeleton in Murine Portal Vein |
title_fullStr |
Modulation of TMEM16A-Channel Activity as Ca2+ Activated Cl− Conductance via the Interaction With Actin Cytoskeleton in Murine Portal Vein |
title_full_unstemmed |
Modulation of TMEM16A-Channel Activity as Ca2+ Activated Cl− Conductance via the Interaction With Actin Cytoskeleton in Murine Portal Vein |
title_sort |
modulation of tmem16a-channel activity as ca2+ activated cl− conductance via the interaction with actin cytoskeleton in murine portal vein |
publisher |
Elsevier |
series |
Journal of Pharmacological Sciences |
issn |
1347-8613 |
publishDate |
2014-01-01 |
description |
Abstract.: TMEM16A is a major component of Ca2+-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. Keywords:: TMEM16A, actin cytoskeleton, portal vein |
url |
http://www.sciencedirect.com/science/article/pii/S1347861319301586 |
work_keys_str_mv |
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