D60-sensitive tyrosine phosphorylation is involved in Fas-mediated phospholipase D activation
Experimental & Molecular Medicine
; : 303-309, 2001.
Artigo
em Inglês
| WPRIM (Pacífico Ocidental)
| ID: wpr-144625
Biblioteca responsável:
WPRO
ABSTRACT
Both Fas and PMA can activate phospholipase D via activation of protein kinase Cbeta in A20 cells. Phospholipase D activity was increased 4 fold in the presence of Fas and 2.5 fold in the presence of PMA. The possible involvement of tyrosine phosphorylation in Fas-induced activation of phospholipase D was investigated. In five minute after Fas cross-linking, there was a prominent increase in tyrosine phosphorylated proteins, and it was completely inhibited by D609, a specific inhibitor of phosphatidylcholine-specific phospholipase C (PC-PLC). A tyrosine kinase inhibitor, genistein, can partially inhibit Fas-induced phospholipase D activation. There were no effects of genistein on Fas-induced activation of PC-PLC and protein kinase C. These results strongly indicate that tyrosine phosphorylation may in part account for the increase in phospholipase D activity by Fas cross-linking and D609 can block not only PC-PLC activity but also tyrosine phosphorylation involved in Fas-induced phospholipase D activation.
Texto completo:
Disponível
Base de dados:
WPRIM (Pacífico Ocidental)
Assunto principal:
Fosfolipases Tipo C
/
Fosfolipase D
/
Fosforilação
/
Fosforilcolina
/
Solubilidade
/
Tionas
/
Tirosina
/
Hidrocarbonetos Aromáticos com Pontes
/
Células Tumorais Cultivadas
/
Água
Tipo de estudo:
Estudo diagnóstico
Limite:
Animais
Idioma:
Inglês
Revista:
Experimental & Molecular Medicine
Ano de publicação:
2001
Tipo de documento:
Artigo