Lee D J, Rosenfeldt H, Grinnell F
Department of Cell Biology and Neuroscience, UT Southwestern Medical Center, Dallas, Texas 75235, USA.
Exp Cell Res. 2000 May 25;257(1):190-7. doi: 10.1006/excr.2000.4866.
Studies were carried out to characterize changes in MAP kinase activation during contraction of collagen matrices by fibroblasts under isometric tension. We found that both ERK and p38 MAP kinases were activated during contraction, as determined by immunoblotting and in vitro kinase assays. ERK activation was biphasic, with peaks at 10 min and 2 h; whereas p38 activation was monophasic, with a single peak at 10 min. Activation of ERK, but not p38, appeared to depend at least in part on the Gi class of heterotrimeric G proteins. The results show that ERK and p38 cooperate in contraction-stimulated activation of c-fos transcription.
开展了多项研究以表征成纤维细胞在等长张力下收缩胶原基质过程中丝裂原活化蛋白激酶(MAP激酶)激活的变化。我们发现,通过免疫印迹和体外激酶测定确定,在收缩过程中细胞外信号调节激酶(ERK)和p38 MAP激酶均被激活。ERK的激活是双相的,在10分钟和2小时出现峰值;而p38的激活是单相的,在10分钟出现单个峰值。ERK的激活似乎至少部分依赖于异源三聚体G蛋白的Gi类,而p38则不然。结果表明,ERK和p38在收缩刺激的c-fos转录激活中协同作用。