An endogenous redox molecule, thioredoxin, regulates transactivation of epidermal growth factor receptor and activation of NF‐κB by lysophosphatidic acid

FEBS Letters

Hirota, Kiichi³  Itoh, Tatsuya³  Yodoi, Junji¹  Fukuda, Kazuhiko³  Murata, Miyahiko² 

[1] Department of Biological Responses, Institute of Virus Research, Kyoto University, 54 Shogoin-Kawaharacho, Sakyo-Ku, Kyoto 606-8507, Japan;Department of Integrative Brain Science, Graduate School of Medicine, Kyoto University, Yoshida, Sakyo-Ku, Kyoto, Japan;Department of Anesthesia, Kyoto University Hospital, Kyoto University, 54 Shogoin-Kawaharacho, Sakyo-Ku, Kyoto 606-8507, Japan

关键词: Lysophosphatidic acid;    Nuclear factor κB;    Thioredoxin;    Redox;    LPA;    1-acyl-2-lyso-sn-glycero-3-phosphate (lysophosphatidic acid);    G protein;    GTP-binding protein;    GPCR;    G protein-coupled receptor;    ROI;    reactive oxygen intermediate;    TRX;    thioredoxin;   

DOI  :  10.1016/S0014-5793(01)02094-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Lysophosphatidic acid (LPA) is the smallest and simplest of all the glycerophospholipids that activates a specific GTP-binding protein coupled receptor to evoke multiple cellular responses. In this paper, we have demonstrated that LPA stimulates nuclear factor (NF)-κB-dependent gene induction in a neuronal cell line, NG108-15 and that this is under redox regulation by an endogenous molecule, thioredoxin. We also have shown that redox-sensitive transactivation of epidermal growth factor receptor by LPA confers NF-κB activation and small GTPase proteins are involved in this pathway.

【 授权许可】

Unknown