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