Literature DB >> 18309110

AP-1-dependent transcriptional regulation of NADPH oxidase in human aortic smooth muscle cells: role of p22phox subunit.

Adrian Manea1, Simona A Manea, Anca V Gafencu, Monica Raicu, Maya Simionescu.   

Abstract

OBJECTIVE: NADPH oxidase (NADPHox) is the major source of reactive oxygen species in vascular diseases; the mechanisms of enzyme activation are not completely elucidated. AP-1 controls the expression of many genes linked to vascular smooth muscle cells (SMCs) dysfunction. In this study we searched for the role of AP-1 in the regulation of NADPHox expression and function in human aortic SMCs exposed to proinflammatory conditions. METHODS AND
RESULTS: Cultured SMCs were exposed to either angiotensin II (Ang II) or tumor necrosis factor (TNF)-alpha. The lucigenin-enhanced chemiluminescence assay and real-time polymerase chain reaction analysis revealed that AP-1 and mitogen-activated protein kinase inhibitors reduced both Ang II or TNF-alpha-dependent upregulation of NADPHox activity and mRNA expression (NOX1, NOX4, p67(phox), p47(phox), p22(phox)). Inhibitors of AP-1 significantly diminished the Ang II or TNF-alpha-stimulated p22(phox) promoter activity and protein level. Transient overexpression of c-Jun/c-Fos upregulated p22(phox) promoter activity. Transcription factor pull-down assay and chromatin immunoprecipitation demonstrated the physical interaction of c-Jun protein with predicted AP-1-binding sites in the p22(phox) gene promoter.
CONCLUSIONS: In SMCs exposed to Ang II or TNF-alpha, inhibition of AP-1-related pathways reduces NADPHox expression and the O(2)(-) production. The physical interaction of AP-1 with p22(phox) gene promoter facilitates NADPHox regulation.

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Year:  2008        PMID: 18309110     DOI: 10.1161/ATVBAHA.108.163592

Source DB:  PubMed          Journal:  Arterioscler Thromb Vasc Biol        ISSN: 1079-5642            Impact factor:   8.311


  32 in total

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4.  Thioredoxin-interacting protein mediates high glucose-induced reactive oxygen species generation by mitochondria and the NADPH oxidase, Nox4, in mesangial cells.

Authors:  Anu Shah; Ling Xia; Howard Goldberg; Ken W Lee; Susan E Quaggin; I George Fantus
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Review 5.  Oxidative stress and hepatic Nox proteins in chronic hepatitis C and hepatocellular carcinoma.

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6.  Increased p22(phox)/Nox4 expression is involved in remodeling through hydrogen peroxide signaling in experimental persistent pulmonary hypertension of the newborn.

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Review 7.  NADPH oxidases and angiotensin II receptor signaling.

Authors:  Abel Martin Garrido; Kathy K Griendling
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Review 8.  Oxidative stress as a mediator of cardiovascular disease.

Authors:  Maqsood M Elahi; Yu Xiang Kong; Bashir M Matata
Journal:  Oxid Med Cell Longev       Date:  2009 Nov-Dec       Impact factor: 6.543

9.  Distinct roles of Nox1 and Nox4 in basal and angiotensin II-stimulated superoxide and hydrogen peroxide production.

Authors:  Sergey I Dikalov; Anna E Dikalova; Alfiya T Bikineyeva; Harald H H W Schmidt; David G Harrison; Kathy K Griendling
Journal:  Free Radic Biol Med       Date:  2008-08-16       Impact factor: 7.376

10.  Peroxiredoxin 6 (Prdx6) supports NADPH oxidase1 (Nox1)-based superoxide generation and cell migration.

Authors:  Jaeyul Kwon; Aibing Wang; Devin J Burke; Howard E Boudreau; Kristen J Lekstrom; Agnieszka Korzeniowska; Ryuichi Sugamata; Yong-Soo Kim; Liang Yi; Ilker Ersoy; Stefan Jaeger; Kannappan Palaniappan; Daniel R Ambruso; Sharon H Jackson; Thomas L Leto
Journal:  Free Radic Biol Med       Date:  2016-04-14       Impact factor: 7.376

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