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
Externally publishedYes

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

Fingerprint

Dive into the research topics of 'Lysophosphatidic acid-induced activation of protein Ser/Thr kinases in cultured rat 3Y1 fibroblasts Possible involvement in rho p21-mediated signalling'. Together they form a unique fingerprint.

Cite this