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An endogenous redox molecule, thioredoxin, regulates transactivation of epidermal growth factor receptor and activation of NF‐κB by lysophosphatidic acid
Author(s) -
Hirota Kiichi,
Murata Miyahiko,
Itoh Tatsuya,
Yodoi Junji,
Fukuda Kazuhiko
Publication year - 2001
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/s0014-5793(01)02094-4
Subject(s) - transactivation , lysophosphatidic acid , microbiology and biotechnology , epidermal growth factor receptor , chemistry , thioredoxin , biology , signal transduction , transcription factor , biochemistry , receptor , gene
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.