TMEM16A inhibits angiotensin II-induced basilar artery smooth muscle cell migration in a WNK1-dependent manner.
- Author:
Huaqing ZHENG
1
;
Xiaolong LI
1
;
Xin ZENG
1
;
Chengcui HUANG
1
;
Mingming MA
1
;
Xiaofei LV
1
;
Yajuan ZHANG
1
;
Lu SUN
1
;
Guanlei WANG
1
;
Yanhua DU
1
;
Yongyuan GUAN
1
Author Information
- Publication Type:Journal Article
- Keywords: AngII, angiotensin II; BASMCs, basilar artery smooth muscle cells; CaCC, Ca2+-activated chloride channel; F-actin, filamentous actin; FAK; FAK, focal adhesion kinase; Hypertension; Integrin; MLC20, myosin light chain 20; MLCK, myosin light chain kinase; MLCP, myosin light chain phosphates; MYPT1, myosin phosphatase target subunit 1; RhoA/ROCK; SMTg, smooth muscle-specific TMEM16A transgenic mice; TMEM16A; VSMC migration; VSMCs, vascular smooth muscle cells; Vascular remodeling; WNK1; WNK1, with-no-lysine kinase 1
- From: Acta Pharmaceutica Sinica B 2021;11(12):3994-4007
- CountryChina
- Language:English
- Abstract: Vascular smooth muscle cell (VSMC) migration plays a critical role in the pathogenesis of many cardiovascular diseases. We recently showed that TMEM16A is involved in hypertension-induced cerebrovascular remodeling. However, it is unclear whether this effect is related to the regulation of VSMC migration. Here, we investigated whether and how TMEM16A contributes to migration in basilar artery smooth muscle cells (BASMCs). We observed that AngII increased the migration of cultured BASMCs, which was markedly inhibited by overexpression of TMEM16A. TMEM16A overexpression inhibited AngII-induced RhoA/ROCK2 activation, and myosin light chain phosphatase (MLCP) and myosin light chain (MLC20) phosphorylation. But AngII-induced myosin light chain kinase (MLCK) activation was not affected by TMEM16A. Furthermore, a suppressed activation of integrin
