Hypoxia induces activation and subcellular translocation of focal adhesion kinase (p125FAK) in cultured rat cardiac myocytes

被引:35
作者
Seko, Y [1 ]
Takahashi, N
Sabe, H
Tobe, K
Kadowaki, T
Nagai, R
机构
[1] Univ Tokyo, Grad Sch Med, Dept Cardiovasc Med, Tokyo, Japan
[2] Univ Tokyo, Grad Sch Med, Dept Metab Dis, Tokyo, Japan
[3] Juntendo Univ, Sch Med, Dept Immunol, Tokyo 113, Japan
[4] Asahi Life Fdn, Inst Adult Dis, Tokyo, Japan
[5] Osaka Biosci Inst, Dept Mol Biol, Osaka, Japan
关键词
D O I
10.1006/bbrc.1999.1185
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
We previously reported that hypoxia caused rapid activation of RAS/mitogen-activated protein kinase (MAPK) pathway, two other stress-activated MAPK family members, stress-activated protein kinase (SAPK) and p38MAPK, and Src family tyrosine kinases, p60(c-src) and p59(c-fyn) in cultured rat cardiac myocytes. In this study, to elucidate how hypoxia affects adhesive interaction between cardiac myocytes and extracellular matrix (ECM), we investigated the molecular mechanism of the activation of focal adhesion-associated tyrosine kinases p125(FAK) and paxillin. Here, we show that hypoxia induced tyrosine phosphorylation of p125(FAK) and paxillin and that hypoxia-induced activation of p125(FAK) was accompanied by its increased association with adapter proteins Shc and GRB2, and non-receptor type tyrosine kinase p60(c-src). Furthermore, hypoxia caused subcellular translocation of p125(FAK) from perinuclear sites to the focal adhesions. These results strongly suggest that p125(FAK) is one of the most important components in hypoxia-induced intracellular signaling in cardiac myocytes and may play a pivotal role in adhesive interaction between cardiac myocytes and ECM. (C) 1999 Academic Press.
引用
收藏
页码:290 / 296
页数:7
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