Lysophosphatidic acid‐induced activation of protein Ser/Thr kinases in cultured rat 3Y1 fibroblasts Possible involvement in  rho   p 21‐mediated signalling | Zendy

Kumagai Naokazu | Zendy; Morii Narito | Zendy; Ishizaki Toshimasa | Zendy; Watanabe Naoki | Zendy; Fujisawa Kazuko | Zendy; Saito Yuji | Zendy; Narumiya Shuh | Zendy

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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.

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