Phospholipase D is involved in oxidative stress-induced migration of vascular smooth muscle cells via tyrosine phosphorylation and protein kinase C
Experimental & Molecular Medicine
;
: 103-109, 2004.
Article
in English
| WPRIM
| ID: wpr-37860
ABSTRACT
Oxidative stress has been implicated in mediation of vascular disorders. In the presence of vanadate, H2O2 induced tyrosine phosphorylation of PLD1, protein kinase C-a (PKC-a), and other unidentified proteins in rat vascular smooth muscle cells (VSMCs). Interestingly, PLD1 was found to be constitutively associated with PKC-a in VSMCs. Stimulation of the cells by H2O2 and vanadate showed a concentration-dependent tyrosine phosphorylation of the proteins in PLD1 immunoprecipitates and activation of PLD. Pretreatment of the cells with the protein tyrosine kinase inhibitor, genistein resulted in a dose-dependent inhibition of H2O2-induced PLD activation. PKC inhibitor and down-regulation of PKC abolished H2O2-stimulated PLD activation. The cells stimulated by oxidative stress (H2O2) caused increased cell migration. This effect was prevented by the pretreatment of cells with tyrosine kinase inhibitors, PKC inhibitors, and 1-butanol, but not 3-butanol. Taken together, these results suggest that PLD might be involved in oxidative stress-induced migration of VSMCs, possibly via tyrosine phosphorylation and PKC activation.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Phospholipase D
/
Phosphorylation
/
Vascular Diseases
/
Protein Kinase C
/
Protein-Tyrosine Kinases
/
Vanadates
/
Signal Transduction
/
Cell Movement
/
Cells, Cultured
/
Rats, Sprague-Dawley
Limits:
Animals
Language:
English
Journal:
Experimental & Molecular Medicine
Year:
2004
Type:
Article
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