D60-sensitive tyrosine phosphorylation is involved in Fas-mediated phospholipase D activation
Experimental & Molecular Medicine
;
: 303-309, 2001.
Article
in English
| 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.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Type C Phospholipases
/
Phospholipase D
/
Phosphorylation
/
Phosphorylcholine
/
Solubility
/
Thiones
/
Tyrosine
/
Bridged-Ring Compounds
/
Tumor Cells, Cultured
/
Water
Type of study:
Diagnostic study
Limits:
Animals
Language:
English
Journal:
Experimental & Molecular Medicine
Year:
2001
Type:
Article
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