Activation of big mitogen-activated protein kinase-1 regulates smooth muscle cell replication.
Activation of big mitogen-activated protein kinase-1 regulates smooth muscle cell replication.
复制标题
大丝裂原激活蛋白激酶 1 的激活可调节平滑肌细胞的复制。
DOI：
10.1161/hq0302.105343
复制
发表时间：
2002
期刊：
影响因子：
--
通讯作者：
Reidy,MichaelA
中科院分区：
文献类型：
--
作者：
Luo,Honglin;Reidy,MichaelA
This study examined the activation of big mitogen-activated protein (MAP) kinase-1 (BMK1) in rat carotid smooth muscle cells (SMCs). Platelet-derived growth factor, fibroblast growth factor-2, sorbitol, and serum all increased the activation of BMK1 in rat carotid SMCs, whereas angiotensin II, phorbol esters, and tumor necrosis factor-α had only slight effects. With the exception of tumor necrosis factor-α, all these factors phosphorylated extracellular signal–regulated kinase (ERK)1/2. The MAPK kinase inhibitor (MEKI), U0126 (1 μmol/L), blocked ERK1/2 phosphorylation and at higher doses (5 μmol/L) blocked BMK1 phosphorylation. This inhibitor also blocked SMC DNA synthesis in a dose-dependent manner. When SMCs were transfected with an adenoviral construct expressing dominant mutant BMK1 and stimulated with fibroblast growth factor-2, a significantly smaller increase in cyclin D1 and cyclin A expression and in retinoblastoma factor phosphorylation was detected compared with the increase in cells transfected with an adenoviral construct expressing green fluorescent protein (GFP). SMC DNA synthesis was significantly blocked in the cells transfected with the dominant mutant BMK1. These data support the suggestion that BMK1 is important and necessary for mitogen-induced SMC proliferation.
