Lysophosphatidic acid‐induced activation of protein Ser/Thr kinases in cultured rat 3Y1 fibroblasts Possible involvement in rho p21‐mediated signalling

FEBS Letters

Morii, Narito¹  Kumagai, Naokazu¹  Fujisawa, Kazuko¹  Ishizaki, Toshimasa¹  Watanabe, Naoki¹  Saito, Yuji¹  Narumiya, Shuh¹ 

[1] Department of Pharmacology, Kyoto University Faculty of Medicine, Yoshida, Sakyo-ku, Kyoto 606, Japan

关键词: rho p21;    Lysophosphatidic acid;    Protein Ser/Thr kinase;    Botulinum C3 exoenzyme;    Pertussis toxin;    Rat 3Y1 fibroblast;    C3;    exoenzyme;    C3;    ADP-ribosyltransferase from Clostridium botulinum;    ERK;    extracellular signal-regulated kinase;    G-protein;    a heterotrimeric GTP-binding protein;    LPA;    lysophosphatidic acid;    MAP-kinase;    mitogen-activated protein kinase;    p125 FAK;    focal adhesion kinase of 125 KDa;    PBS;    phosphate-buffered saline;    PLC;    phospholipase C;    PKC;    protein kinase C;    PTX;    pertussis toxin;    rho p21;    the small GTP-binding protein of the rho gene product;   

DOI  :  10.1016/0014-5793(95)00478-R

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Renaturation kinase assay was used to detect protein kinases activated by lysophosphatidic acid (LPA) in cultured rat 3Y1 fibroblasts. LPA activated several Ser/Thr protein kinases with apparent molecular weights of 145K, 85K, 64–65K (a doublet), and 60K (each named p145, p85, p64165 and p60, respectively) in addition to p43 mitogen activated protein (MAP)-kinase. Experiments using pertussis toxin and botulinum C3 exoenzyme showed that p145, p85, and p64165 kinases were activated by a pertussis toxin-insensitive rho p21-dependent pathway and that the activation of MAP-kinase was mediated by both the pertussis toxin-sensitive rho p21-independent and the pertussis toxin-insensitive rho p21-dependent pathways.

【 授权许可】

Unknown