期刊
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
卷 380, 期 2, 页码 355-360出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2009.01.107
关键词
Nox4; NADPH oxidase; Reactive oxygen species; p38 MAPK; Endothelial cells
资金
- German Federal Ministry of Education, Research (BMBF)
- University of Technology Dresden
- DFG SCHN [430/6-1]
- Medical Faculty of the University of Technology Dresden
Nicotine adenine dinucleotide phosphate (NADPH) oxidase (Nox) complexes are the main sources of reactive oxygen species (ROS) formation in the vessel wall. We have used DNA microarray, real-time PCR and Western blot to demonstrate that the subunit Nox4 is the major Nox isoform in primary human endothelial cells; we also found high levels of NADPH oxidase subunit p22(phox) expression. Nox4 was localized by laser scanning confocal microscopy within the cytoplasm of endothelial cells, Endothelial Nox4 overexpression enhanced Superoxide anion formation and phosphorylation of p38 MAPK Nox4 down-regulation by shRNA has in contrast to TGF-beta no effect on p38 MAPK phosphorylation. We conclude that Nox4 is the major Nox isoform in human endothelial cells, and forms an active complex with P22(phox). The Nox4-containing complex mediates formation of reactive oxygen species and p38 MAPK activation. This is a novel mechanism of redox-sensitive signaling in human endothelial cells. (C) 2009 Elsevier Inc. All rights reserved.
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