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. 1995 Jun 5;366(1):11-6.
doi: 10.1016/0014-5793(95)00478-r.

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

N Kumagai  1 , N Morii, T Ishizaki, N Watanabe, K Fujisawa, Y Saito, S Narumiya
Affiliations
Free article

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

N Kumagai et al. FEBS Lett. .
Free article

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 rho p21-dependent pathway and that the activation of MAP-kinase was mediated by both the pertussis toxin-sensitive rho p21-independent and the pertussis toxin-insensitive rho p21-dependent pathways.

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