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Lysophosphatidic acid‐induced activation of protein Ser/Thr kinases in cultured rat 3Y1 fibroblasts Possible involvement in rho p 21‐mediated signalling
Author(s) -
Kumagai Naokazu,
Morii Narito,
Ishizaki Toshimasa,
Watanabe Naoki,
Fujisawa Kazuko,
Saito Yuji,
Narumiya Shuh
Publication year - 1995
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(95)00478-r
Subject(s) - lysophosphatidic acid , pertussis toxin , kinase , chemistry , microbiology and biotechnology , protein kinase a , protein serine threonine kinases , mitogen activated protein kinase , signal transduction , receptor , g protein , biochemistry , biology
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 p 145, p 85, p 64165 and p 60, respectively) in addition to p 43 mitogen activated protein (MAP)‐kinase. Experiments using pertussis toxin and botulinum C3 exoenzyme showed that p 145, p 85, and p 64165 kinases were activated by a pertussis toxin‐insensitive rho p 21‐dependent pathway and that the activation of MAP‐kinase was mediated by both the pertussis toxin‐sensitive rho p 21‐independent and the pertussis toxin‐insensitive rho p 21‐dependent pathways.