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Lysophosphatidic acid induces tyrosine phosphorylation and activation of MAP‐kinase and focal adhesion kinase in cultured Swiss 3T3 cells
Author(s) -
Kumagai Naokazu,
Morii Narito,
Fujisawa Kazuko,
Yoshimasa Takaaki,
Nakao Kazuwa,
Narumiya Shuh
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80236-n
Subject(s) - lysophosphatidic acid , tyrosine phosphorylation , phosphorylation , focal adhesion , map2k7 , microbiology and biotechnology , tyrosine , ptk2 , biology , mitogen activated protein kinase , mapk14 , tyrosine kinase , mitogen activated protein kinase kinase , receptor tyrosine kinase , signal transduction , biochemistry , protein kinase c , cyclin dependent kinase 2 , protein kinase a , receptor
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.