Abstract
The major function of vascular smooth muscle cells (VSMCs) is to maintain normal vascular tone via coordinated contraction‐relaxation cycling. Angiotensin II (Ang II), a vasoactive peptide, induces vascular smooth muscle cell (VSMC) contraction. SM22α, an actin binding protein, is highly expressed in contractile VSMCs. It is unclear whether SM22α plays a role in Ang II‐induced contraction. In the present study, differentiation of VSMCs in vitro was induced by all trans retinoic acid (ATRA), and the roles of SM22α in contraction of VSMCs were assessed using specific siRNA. Knockdown of SM22α significantly attenuated the contractility in redifferentiated VSMCs, which is associated with the suppression of Ang II‐induced activation of extracellular signal regulated kinase (ERK) signaling pathway. The loss of SM22α proteins inhibited the formation of actin stress fibres. Furthermore, disruption of the actin filament network by cytochalasin D impaired the activation of ERK pathway. Overall, our results suggest SM22α regulates VSMC contraction through mediates Ang II‐induced ERK activation and actin stress fibre formation.Source of funding: This study was supported by the National Natural Science Foundation of China (31071003).
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