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1 Center for Cardiovascular Science, The Albany Medical College, Albany, NY, USA
2 Research Service, Stratton Veterans Affairs Medical Center, Albany, NY, USA; Center for Cardiovascular Science, The Albany Medical College, Albany, NY, USA
* To whom correspondence should be addressed. E-mail: jmurd{at}msn.com.
We tested the hypothesis that the NAD[P]H-oxidase dependent generation of superoxide anion (.O2-) mediates tumor necrosis factor-
(TNF) induced alterations in permeability of pulmonary microvessel endothelial monolayers (PMEM). The permeability of PMEM was assessed by the clearance rate of Evans blue labeled albumin. The NAD[P]H-oxidase sub-components, p47phox and p22phox, were assessed by immunofluorescent-microscopy and Western-immunoblot. The reactive oxygen species, .O2-, was measured by fluorescence of 6-carboxy-2',7'-dichlorodihydrofluorescein diacetate-di(acetoxymethyl ester) (C-H2DCFDA), 5-(and -6)-chloromethyl-2',7'-dichlorodihydrofluorescein diacetate-acetyl ester (CM-H2DCFDA) and dihydroethidium (DHE). TNF treatment (50 ng/ml for 4.0 hr) induced: (1) p47phox-translocation, (2) an increase in p22phox protein, (3) increased localization of p47phox with p22phox, (4) .O2- generation, and (5) increased permeability to albumin. p22phox-antisense oligonucleotide prevented the TNF-induced effect on p22phox , p47phox, .O2- and permeability. The scrambled-nonsense oligonucleotide had no effect. The TNF-induced increase in .O2- and permeability to albumin was also prevented by the .O2- scavenger Cu-Zn SOD (100 U/ml). The data indicates that activation of NAD[P]H-oxidase, via the generation of .O2-, mediates TNF-induced barrier dysfunction in PMEM.
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