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mediates TNF-
-induced ICAM-1 gene
transcription in endothelial cells
Department of Pharmacology, University of Illinois College of Medicine, Chicago, Illinois 60612
We addressed the role of
protein kinase C (PKC) isozymes in mediating tumor necrosis factor-
(TNF-)-induced oxidant generation in endothelial cells, a
requirement for nuclear factor-
B (NF-B) activation and
intercellular adhesion molecule-1 (ICAM-1) gene transcription.
Depletion of the conventional (c) and novel (n) PKC isozymes following
24 h exposure of human pulmonary artery endothelial (HPAE) cells
with the phorbol ester, phorbol 12-myristate 13-acetate (500 nM),
failed to prevent TNF--induced oxidant generation. In contrast,
inhibition of PKC-
synthesis by the antisense oligonucleotide prevented the oxidant generation following the TNF- stimulation. We
observed that PKC- also induced the TNF--induced NF-B binding to the ICAM-1 promoter and the resultant ICAM-1 gene transcription. We
showed that expression of the dominant negative mutant of PKC- prevented the TNF--induced ICAM-1 promoter activity, whereas overexpression of the wild-type PKC- augmented the response. These
data imply a critical role for the PKC- isozyme in regulating TNF--induced oxidant generation and in signaling the activation of
NF-B and ICAM-1 transcription in endothelial cells.
protein kinase C isoforms; oxidants; nuclear factor-B; intercellular adhesion molecule-1; endothelium
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