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Am J Physiol Lung Cell Mol Physiol (July 26, 2002). doi:10.1152/ajplung.00123.2002
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Articles in PresS, published online ahead of print July 26, 2002
Am J Physiol Lung Cell Mol Physiol, 10.1152/ajplung.00123.2002
Submitted on April 25, 2002
Accepted on July 19, 2002

Hyperoxia-induced NAD[P]H oxidase activation and regulation by MAP kinases in human lung endothelial cells

Narasimham L. Parinandi1, Michael A. Kleinberg2, Peter V. Usatyuk1, Rhett J. Cummings1, Arjun Pennathur1, Arturo J. Cardounel1, Jay L. Zweier1, Joe G. N. Garcia1, and Viswanathan Natarajan1*

1 Department of Medicine, Johns Hopkins University School of Medicine, Baltimore, Maryland 21224, USA
2 Division of Infectitious Diseases, University of Maryland School of Medicine, Baltimore, Maryland 21201, USA

* To whom correspondence should be addressed. E-mail: vnataraj{at}mail.jhmi.edu.

As the exact mechanisms of generation of reactive oxygen species (ROS) during hyperoxia in vascular endothelium are not thoroughly understood, we investigated the role and mechanisms of regulation of NAD[P]H oxidase in hyperoxia-induced generation of ROS in human pulmonary artery endothelial cells (HPAECs). Exposure of HPAECs to hyperoxia (95% O2/5% CO2) for 1, 3, and 12 h increased the generation of O2-., hydroxyl radicals, H2O2 and total ROS. Diphenyleneiodonium (DPI) (100 µM) significantly inhibited where as rotenone (100 µM) and oxypurinol (100 µM) failed to inhibit hyperoxia-induced generation of ROS in HPAECs. Furthermore, hyperoxia enhanced NADPH- and NADH-dependent and SOD- and DPI-inhibitable generation of O2-. by intact cells as measured by lucigenin chemiluminescence. Immunohistocytochemistry and Western blotting revealed the presence of gp91, p67 phox, p22 phox and p47 phox subcomponents of NAD[P]H oxidase in HPAECs. Hyperoxia-induced generation of ROS was completely blocked in cells transfected with p22 phox antisense plasmid. Hyperoxia also activated p38 mitogen-activated protein kinase (p38 MAPK) and extracellular-regulated kinase (ERK) in HPAECs. Inhibition of p38 MAPK and MEK1/2 significantly attenuated the hyperoxia-induced generation of ROS in HPAECs, suggesting the involvement of p38 MAPK and ERK. The attenuation of hyperoxia-induced ROS generation in HPAECs infected with p38 MAP kinase dominant negative adenoviral constructs further supports the role of p38 MAP kinase. In summary, our results demonstrate a role for MAP kinases in the regulation of hyperoxia-induced activation of NAD[P]H oxidase in HPAECs.




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