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Am J Physiol Lung Cell Mol Physiol 278: L1107-L1117, 2000;
1040-0605/00 $5.00
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Vol. 278, Issue 6, L1107-L1117, June 2000

Protein kinase C-alpha mediates endothelial barrier dysfunction induced by TNF-alpha

Thomas Ferro1, Paul Neumann2, Nancy Gertzberg2, Richard Clements2, and Arnold Johnson1,2

1 Research Service, Stratton Veterans Affairs Medical Center, and 2 Vascular Biology Research Group, Albany Medical College, Albany, New York 12208

We tested the hypothesis that protein kinase C-alpha (PKC-alpha ) mediates tumor necrosis factor-alpha (TNF-alpha )-induced alterations in permeability of pulmonary microvessel endothelial monolayers (PEM). The permeability of PEM was assessed by the clearance rate of Evans blue-labeled albumin. PEM lysates were analyzed for PKC-alpha mRNA (Northern cDNA blot), protein (Western immunoblot), and activity (translocation and phosphorylation of myristoylated arginine-rich C kinase substrate). Incubation of PEM with TNF-alpha (1,000 U/ml) for 4 h resulted in increases in 1) PKC-alpha protein, 2) cytoskeletal-associated PKC-alpha , 3) PKC-alpha activity, and 4) permeability to albumin. The TNF-alpha -induced increase in PKC-alpha protein, PKC-alpha activity, and permeability was prevented by a 4-h pretreatment with PKC-alpha antisense oligonucleotide but not by the scrambled nonsense oligonucleotide. The TNF-alpha -induced increase in permeability to albumin was prevented by myristoylated protein kinase C inhibitor (an inhibitor of PKC-alpha /beta , 100 µM) and calphostin (an inhibitor of the classic and novel PKC isotypes, 200 nM). The treatment with calphostin from 0.5 to 3.0 h after TNF-alpha still prevented barrier dysfunction induced by 4 h of TNF-alpha treatment. The data indicate that prolonged activation of PKC-alpha , maintained by a translation-dependent pool of PKC-alpha protein, mediates TNF-alpha -induced increases in endothelial permeability in PEM.

antisense; edema; messenger ribonucleic acid; transcription


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