scholarly journals Reactive Oxygen Species Signaling through Regulation of Protein Tyrosine Phosphorylation in Endothelial Cells

1998 ◽  
Vol 106 ◽  
pp. 1205 ◽  
Author(s):  
Viswanathan Natarajan ◽  
William M. Scribner ◽  
Mohammed Al-Hassani ◽  
Suryanarayana Vepa
Keyword(s):  
Reactive Oxygen Species ◽  
Endothelial Cells ◽  
Tyrosine Phosphorylation ◽  
Reactive Oxygen ◽  
Oxygen Species ◽  
Protein Tyrosine Phosphorylation ◽  
Protein Tyrosine ◽  
Reactive Oxygen Species Signaling

scholarly journals Reactive oxygen species mediate phorbol ester-regulated tyrosine phosphorylation and phospholipase A2 activation: potentiation by vanadate

1993 ◽  
Vol 295 (3) ◽  
pp. 879-888 ◽  
Author(s):  
U Zor ◽  
E Ferber ◽  
P Gergely ◽  
K Szücs ◽  
V Dombrádi ◽  
...  
Keyword(s):  
Reactive Oxygen Species ◽  
Protein Kinase ◽  
Phospholipase A2 ◽  
Tyrosine Phosphorylation ◽  
Phorbol Ester ◽  
Cellular Protein ◽  
Oxygen Species ◽  
Protein Tyrosine Phosphorylation ◽  
Protein Tyrosine ◽  
Ros Formation

We have previously shown that vanadate potentiates the activating effect of phorbol ester (TPA) on cellular phospholipase A2 (PLA2) in a pathway dependent on the formation of reactive oxygen species (ROS). Here we evaluate the chain of enzymes (protein kinases and phosphatases) that participate in this process. Treatment of macrophages with vanadate plus TPA led to activation of protein kinase C (PKC) and NADPH oxidase (O2- generation in intact cells), massive cellular protein tyrosine phosphorylation, suppression of protein tyrosine phosphatase (PTP) activity and a sustained activation of protein tyrosine kinase (PTK) and myelin basic protein kinase activity (the latter three enzyme activities were assessed in cell lysates). Inhibition of ROS formation by diphenyleneiodonium (DPI) prevented PTP inhibition, PTK activation and protein tyrosine phosphorylation by vanadate plus TPA. Vanadate plus H2O2 mimicked the effect of vanadate plus TPA on PKC activation, cellular protein tyrosine phosphorylation, PTP and PTK, but their effects were resistant to DPI. Suppression of PKC activity (down-regulation; selective inhibitors) prevented the above-mentioned effects of vanadate plus TPA, but not of vanadate plus H2O2. Collectively, the results show that ROS formation induced by TPA in association with vanadate is essential in the modulation of protein tyrosine phosphorylation and PLA2 activity.

Reactive oxygen species induce reversible PECAM-1 tyrosine phosphorylation and SHP-2 binding

2003 ◽  
Vol 285 (6) ◽  
pp. H2336-H2344 ◽  
Author(s):  
Matthias Maas ◽  
Ronggang Wang ◽  
Cathy Paddock ◽  
Srigiridhar Kotamraju ◽  
Balaraman Kalyanaraman ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Reactive Oxygen Species ◽  
Tyrosine Phosphorylation ◽  
Tyrosine Phosphatase ◽  
Reactive Oxygen ◽  
Protein Tyrosine Phosphatases ◽  
Sh2 Domain ◽  
Oxygen Species ◽  
Protein Tyrosine ◽  
High Concentrations

Platelet endothelial cell adhesion molecule-1 (PECAM-1, CD31) functions to control the activation and survival of the cells on which it is expressed. Many of the regulatory functions of PECAM-1 are dependent on its tyrosine phosphorylation and subsequent recruitment of the Src homology (SH2) domain containing protein tyrosine phosphatase SHP-2. The recent demonstration that PECAM-1 tyrosine phosphorylation occurs in cells exposed to the reactive oxygen species hydrogen peroxide (H2O2) suggested that this form of oxidative stress may also support PECAM-1/SHP-2 complex formation. In the present study, we show that PECAM-1 tyrosine phosphorylation in response to exposure of cells to H2O2 is reversible, involves a shift in the balance between kinase and phosphatase activities, and supports binding of SHP-2 and recruitment of this phosphatase to cell-cell borders. We speculate, however, that the unique ability of H2O2 to reversibly oxidize the reactive site cysteine residues of protein tyrosine phosphatases may result in transient inactivation of the SHP-2 that is bound to PECAM-1 under these conditions. Finally, we provide evidence that PECAM-1 tyrosine phosphorylation and SHP-2 binding in endothelial cells requires exposure to an “oxidative burst” of H2O2, but that exposure of these cells to sufficiently high concentrations of H2O2 for a sufficiently long period of time abrogates binding of SHP-2 to tyrosine-phosphorylated PECAM-1. These findings support a role for PECAM-1 as a sensor of oxidative stress, perhaps most importantly during the process of inflammation.

Reactive oxygen species activate focal adhesion kinase, paxillin and P130CAS tyrosine phosphorylation in endothelial cells

1998 ◽  
Vol 25 (9) ◽  
pp. 1021-1032 ◽  
Author(s):  
Alexia Gozin ◽  
Elisabeth Franzini ◽  
Valérie Andrieu ◽  
Lydie Da Costa ◽  
Emmanuelle Rollet-Labelle ◽  
...  
Keyword(s):  
Reactive Oxygen Species ◽  
Endothelial Cells ◽  
Focal Adhesion Kinase ◽  
Tyrosine Phosphorylation ◽  
Focal Adhesion ◽  
Reactive Oxygen ◽  
Oxygen Species

scholarly journals Src-mediated Tyrosine Phosphorylation of p47phoxin Hyperoxia-induced Activation of NADPH Oxidase and Generation of Reactive Oxygen Species in Lung Endothelial Cells

2005 ◽  
Vol 280 (21) ◽  
pp. 20700-20711 ◽  
Author(s):  
Ashis K. Chowdhury ◽  
Tonya Watkins ◽  
Narasimham L. Parinandi ◽  
Bahman Saatian ◽  
Michael E. Kleinberg ◽  
...  
Keyword(s):  
Reactive Oxygen Species ◽  
Endothelial Cells ◽  
Nadph Oxidase ◽  
Tyrosine Phosphorylation ◽  
Reactive Oxygen ◽  
Oxygen Species ◽  
Lung Endothelial Cells
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