D60-sensitive tyrosine phosphorylation is involved in Fas-mediated phospholipase D activation
Experimental & Molecular Medicine
; : 303-309, 2001.
Article
Dans En
| WPRIM
| ID: wpr-144612
Responsable en Bibliothèque :
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.
Texte intégral:
1
Indice:
WPRIM
Sujet Principal:
Type C Phospholipases
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Phospholipase D
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Phosphorylation
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Phosphoryl-choline
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Solubilité
/
Thiones
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Tyrosine
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Composés pontés
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Cellules cancéreuses en culture
/
Eau
Type d'étude:
Diagnostic_studies
Limites du sujet:
Animals
langue:
En
Texte intégral:
Experimental & Molecular Medicine
Année:
2001
Type:
Article