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Am J Physiol Cell Physiol 281: C1064-C1075, 2001;
0363-6143/01 $5.00
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Vol. 281, Issue 3, C1064-C1075, September 2001

SPECIAL COMMUNICATION
Peroxynitrite causes endothelial cell monolayer barrier dysfunction

James L. Knepler Jr., Loui N. Taher, Mahesh P. Gupta, Carolyn Patterson, Fred Pavalko, Michael D. Ober, and C. Michael Hart

Departments of Medicine and Physiology, Richard L. Roudebush Veterans Affairs and Indiana University Medical Centers, Indianapolis, Indiana 46202

Nitric oxide (·NO) attenuates hydrogen peroxide (H2O2)-mediated barrier dysfunction in cultured porcine pulmonary artery endothelial cells (PAEC) (Gupta MP, Ober MD, Patterson C, Al-Hassani M, Natarajan V, and Hart, CM. Am J Physiol Lung Cell Mol Physiol 280: L116-L126, 2001). However, ·NO rapidly combines with superoxide (O<UP><SUB>2</SUB><SUP>−</SUP></UP>) to form the powerful oxidant peroxynitrite (ONOO-), which we hypothesized would cause PAEC monolayer barrier dysfunction. To test this hypothesis, we treated PAEC with ONOO- (500 µM) or 3-morpholinosydnonimine hydrochloride (SIN-1; 1-500 µM). SIN-1-mediated ONOO- formation was confirmed by monitoring the oxidation of dihydrorhodamine 123 to rhodamine. Both ONOO- and SIN-1 increased albumin clearance (P < 0.05) in the absence of cytotoxicity and altered the architecture of the cytoskeletal proteins actin and beta -catenin as detected by immunofluorescent confocal imaging. ONOO--induced barrier dysfunction was partially reversible and was attenuated by cysteine. Both ONOO- and SIN-1 nitrated tyrosine residues, including those on beta -catenin and actin, and oxidized proteins in PAEC. The introduction of actin treated with ONOO- into PAEC monolayers via liposomes also resulted in barrier dysfunction. These results indicate that ONOO- directly alters endothelial cytoskeletal proteins, leading to barrier dysfunction.

nitrotyrosine; actin; catenin


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