D60-sensitive tyrosine phosphorylation is involved in Fas-mediated phospholipase D activation.
- Author:
Jong Gon KIM
1
;
In Cheol SHIN
;
Ki Sung LEE
;
Joong Soo HAN
Author Information
1. Institute of Biomedical Sciences and Department of Biochemistry, College of Medicine, Hanyang University, Seoul, Korea.
- Publication Type:Original Article ; Research Support, Non-U.S. Gov't
- Keywords:
Fas;
phospholipase D;
D609;
phosphatidylcholine-specific phospholipase C;
tyrosine phosphorylation;
protein kinase C;
A20 murine cells;
genistein
- MeSH:
Animal;
Antibodies, Monoclonal/immunology/*pharmacology;
Antigens, CD95/immunology/*metabolism;
Bridged Compounds/*pharmacology;
Cell Line;
Cross-Linking Reagents;
Dose-Response Relationship, Immunologic;
Enzyme Activation;
Genistein/pharmacology;
Hydrolysis;
Lymphoma/pathology;
Mice;
Phospholipase C/*antagonists & inhibitors;
Phospholipase D/*metabolism;
Phosphorylation;
Phosphorylcholine/metabolism;
Solubility;
Thiones/*pharmacology;
Tumor Cells, Cultured;
Tyrosine/*metabolism;
Water/chemistry
- From:Experimental & Molecular Medicine
2001;33(4):303-309
- CountryRepublic of Korea
- Language:English
-
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.
