D60-sensitive tyrosine phosphorylation is involved in Fas-mediated phospholipase D activation
Experimental & Molecular Medicine
;
: 303-309, 2001.
Artículo
en Inglés
| WPRIM
| ID: wpr-144612
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:
Disponible
Índice:
WPRIM (Pacífico Occidental)
Asunto principal:
Fosfolipasas de Tipo C
/
Fosfolipasa D
/
Fosforilación
/
Fosforilcolina
/
Solubilidad
/
Tionas
/
Tirosina
/
Hidrocarburos Aromáticos con Puentes
/
Células Tumorales Cultivadas
/
Agua
Tipo de estudio:
Estudio diagnóstico
Límite:
Animales
Idioma:
Inglés
Revista:
Experimental & Molecular Medicine
Año:
2001
Tipo del documento:
Artículo
Similares
MEDLINE
...
LILACS
LIS