Lysophosphatidic acid induces tyrosine phosphorylation and activation of MAP‐kinase and focal adhesion kinase in cultured Swiss 3T3 cells

FEBS Letters

Morii, Narito¹  Kumagai, Naokazu¹  Fujisawa, Kazuko¹  Nakao, Kazuwa²  Narumiya, Shuh¹  Yoshimasa, Takaaki² 

[1] Department of Pharmacology, Kyoto University Faculty of Medicine, Kyoto 606, Japan;Second Division, Department of Medicine, Kyoto University Faculty of Medicine, Kyoto 606, Japan

关键词: Lysophosphatidic acid;    Protein tyrosine phosphorylation;    Protein tyrosine kinase;    MAP-kinase;    Focal adhesion kinase;    Signal transduction;    LPA;    lysophosphatidic acid;    MAP-kinase;    mitogen-activated protein kinase;    ERK;    extracellular signal-regulated kinase;    FAK;    focal adhesion kinase;    ITS;    insulin-transferrin-sodium selenite;    MBP;    myelin basic protein;    TBS;    Tris-buffered saline;   

DOI  :  10.1016/0014-5793(93)80236-N

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Lysophosphatidic acid (LPA) added to serum-starved Swiss 3T3 cells induced, in a time- and concentration-dependent manner, tyrosine phosphorylation of multiple proteins, including proteins of 43, 64, 88 kDa and a group of proteins between 110 and 130 kDa. Among them, two proteins, p43 and p120, were identified as mitogen-activated protein kinase (MAP-kinase) and focal adhesion kinase (FAK), respectively, by immunoprecipitation and immunoblot analysis. Tyrosine phosphorylation of p64 peaked at l min and declined rapidly, whereas that of MAP-kinase and FAK peaked at 5 and 10 min after the addition of LPA, respectively. The activity of MAP-kinase determined as phosphorylation of myelin basic protein increased transiently about 3-fold at 5 min, and correlated with tyrosine phosphorylation. These results indicate that tyrosine phosphorylation of these proteins is a part of the signal transduction by LPA and may be involved in its mitogenic responses.

【 授权许可】

Unknown