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

Naokazu Kumagai, Narito Morii, Toshimasa Ishizaki, Naoki Watanabe, Kazuko Fujisawa, Yuji Saito, Shuh Narumiya

    Research output: Contribution to journalArticlepeer-review

    21 Citations (Scopus)

    Abstract

    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 rhop21-dependent pathway and that the activation of MAP-kinase was mediated by both the pertussis toxin-sensitive rhop21-independent and the pertussis toxin-insensitive rhop21-dependent pathways.

    Original languageEnglish
    Pages (from-to)11-16
    Number of pages6
    JournalFEBS Letters
    Volume366
    Issue number1
    DOIs
    Publication statusPublished - 1995 Jun 5

    Keywords

    • Botulinum C3 exoenzyme
    • Lysophosphatidic acid
    • Pertussis toxin
    • Protein Ser/Thr kinase
    • Rat 3Y1 fibroblast
    • rhop21

    ASJC Scopus subject areas

    • Biophysics
    • Structural Biology
    • Biochemistry
    • Molecular Biology
    • Genetics
    • Cell Biology

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