Nox4 overexpression activates reactive oxygen species and p38 MAPK in human endothelial cells
Research output: Contribution to journal › Research article › Contributed › peer-review
Contributors
Abstract
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 p22phox 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-β 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 p22phox. 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.
Details
Original language | English |
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Pages (from-to) | 355-360 |
Number of pages | 6 |
Journal | Biochemical and biophysical research communications |
Volume | 380 |
Issue number | 2 |
Publication status | Published - 6 Mar 2009 |
Peer-reviewed | Yes |
External IDs
PubMed | 19280689 |
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ORCID | /0000-0001-9360-9736/work/164198485 |
Keywords
ASJC Scopus subject areas
Keywords
- Endothelial cells, NADPH oxidase, Nox4, p38 MAPK, Reactive oxygen species