Phospholipase D is activated and phosphorylated by casein kinase-II in human U87 astroglioma cells
Experimental & Molecular Medicine
;
: 55-62, 2006.
Artículo
en Inglés
| WPRIM
| ID: wpr-77901
ABSTRACT
Elevated expression of protein casein kinase II (CKII) stimulated basal phospholipase D (PLD) activity as well as PMA-induced PLD activation in human U87 astroglioma cells. Moreover, CKII-selective inhibitor, emodin and apigenin suppressed PMA-induced PLD activation in a dose-dependent manner as well as basal PLD activity, suggesting the involvement of CKII in the activation of both PLD1 and PLD2. CKII was associated with PLD1 and PLD2 in co-transfection experiments. Furthermore, CKII induced serine/threonine phosphorylation of PLD2 in vivo, and the multiple regions of PLD2 were phosphorylated by CKII in vitro kinase assay using glutathione S-transferase-PLD2 fusion protein fragments. Elevated expression of CKII or PLD increased cell proliferation but pretreatment of cells with 1-butanol suppressed CKII-induced cell proliferation. These results suggest that CKII is involved in proliferation of U87 cells at least in part, through stimulation of PLD activity.
Texto completo:
Disponible
Índice:
WPRIM (Pacífico Occidental)
Asunto principal:
Fosfolipasa D
/
Fosforilación
/
Astrocitoma
/
Proteínas Recombinantes de Fusión
/
Pruebas de Precipitina
/
Acetato de Tetradecanoilforbol
/
Cinética
/
Western Blotting
/
1-Butanol
/
Línea Celular Tumoral
Límite:
Humanos
Idioma:
Inglés
Revista:
Experimental & Molecular Medicine
Año:
2006
Tipo del documento:
Artículo
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