Premium
ROCK1 induces ERK nuclear translocation in PDGF‐BB‐stimulated migration of rat vascular smooth muscle cells
Author(s) -
Zhao Ying,
Lv Miao,
Lin HaiShuang,
Hong Yan,
Yang FuChun,
Sun YunLiang,
Guo Yan,
Cui Ying,
Li Sheng,
Gao Ying
Publication year - 2012
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1002/iub.598
Subject(s) - rock1 , vascular smooth muscle , microbiology and biotechnology , mapk/erk pathway , phosphorylation , platelet derived growth factor receptor , rock2 , p38 mitogen activated protein kinases , transfection , signal transduction , small interfering rna , chemistry , protein kinase a , biology , rho associated protein kinase , growth factor , endocrinology , biochemistry , gene , receptor , smooth muscle
It has been known that Rho‐associated protein kinase (ROCK) signaling regulates the migration of vascular smooth muscle cells (VSMCs). However, the isoform‐specific roles of ROCK and its underlying mechanism in VSMC migration are not well understood. The current study thus aimed to investigate the roles of ROCK1/2 and their relationship to the MAPK signaling pathway in platelet‐derived growth factor (PDGF)‐induced rat aorta VSMC migration by manipulating ROCK gene expression. The results revealed that ROCK1 small interfering ribonucleic acid (siRNA) rather than ROCK2 siRNA decreased PDGF‐BB‐generated VSMC migration, and upregulation of ROCK1 expression via transfection of constructed pEGFP‐C1/ROCK1 plasmid further increased the migration of PDGF‐BB‐treated VSMCs. In PDGF‐treated VSMCs, ROCK1 siRNA did not affect the phosphorylation levels of ERK and p38 in the cytoplasm, but decreased the level of ERK phosphorylation in the nucleus. These findings demonstrate that activated ROCK1 can promote VSMC migration through facilitating phosphorylation and nuclear translocation of ERK protein. © 2011 IUBMB Life,, 2011.