Title : Phospholipase D activation in endothelial cells is redox sensitive.

Pub. Date : 1999 Summer

PMID : 11228747






4 Functional Relationships(s)
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1 Previously, we have shown that ROS (hydrogen peroxide, fatty acid hydroperoxide, diperoxovanadate, and 4-hydroxynonenal) enhance protein tyrosine phosphorylation and activate phospholipase D (PLD) in bovine pulmonary artery endothelial cells (BPAECs). Reactive Oxygen Species glycosylphosphatidylinositol specific phospholipase D1 Homo sapiens
2 In the present study, our aim was to investigate the role of exogenous thiol agents on ROS-induced PLD activation in conjunction with the role of cellular thiols--glutathione (GSH) and protein thiols--on PLD activation and protein tyrosine phosphorylation. Reactive Oxygen Species glycosylphosphatidylinositol specific phospholipase D1 Homo sapiens
3 Pretreatment of BPAECs with N-acetyl-L-cysteine (NAC) or 2-mercaptopropionylglycine (MPG) blocked ROS-induced changes in intracellular GSH and PLD activation. Reactive Oxygen Species glycosylphosphatidylinositol specific phospholipase D1 Homo sapiens
4 These results support the hypothesis that modulation of thiol-redox status (cellular nonprotein and protein thiols) may contribute to the regulation of ROS-induced protein tyrosine phosphorylation and PLD activation in vascular endothelium. Reactive Oxygen Species glycosylphosphatidylinositol specific phospholipase D1 Homo sapiens