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
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| ID: wpr-37860
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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.
Texte intégral:
1
Indice:
WPRIM
Sujet Principal:
Phospholipase D
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Phosphorylation
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Maladies vasculaires
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Protéine kinase C
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Protein-tyrosine kinases
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Vanadates
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Transduction du signal
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Mouvement cellulaire
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Cellules cultivées
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Rat Sprague-Dawley
Limites du sujet:
Animals
langue:
En
Texte intégral:
Experimental & Molecular Medicine
Année:
2004
Type:
Article