Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 374, Issue 2, Pages 351-355Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2008.07.027
Keywords
JunB; ERK1/2; NADPH oxidase; NOX1; vascular smooth muscle cells
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NADPH oxidase is a major source of the superoxide produced in cardiovascular tissues. The expression of NOX1, a Catalytic Subunit of NADPH oxidase, is induced by various vasoactive factors, including angiotensin 11, prostaglandin (PG) F-2 alpha, and platelet-derived growth factor (PDGF). It was reported previously that the inducible expression of NOX1 is governed by the activating transcription factor-1 (ATF-1)-myocyte enhancer factor 213 (MEF2B) cascade downstream of phosphoinositide 3 (1113) kinase. It was also reported that extracellular signal-regulated kinase (ERK) 1/2 is involved in the expression of NOX1. To further clarify the factors involved in NOX1 induction downstream of ERK1/2, the promoter region of the NOX1 gene was analyzed. A consensus activator protein-1 (AP-1) site was found at -98/-92 in the 5'-flanking region of the rat NOX1 gene. The introduction Of Mutations at this site abolished PGF(2 alpha)-induced transcriptional activation in a luciferase assay. Electrophoresis mobility shift assays demonstrated that PGF(2 alpha) and PDGF augmented the binding of JunB to this sequence. PD98059, an inhibitor of MAPK/ERK kinase, suppressed the expression of JunB induced by PGF(2 alpha) or PDGF. These results suggest that the ERK1/2-JunB pathway is a key regulator of the inducible expression of the NOX1 gene in vascular smooth muscle cells. (C) 2008 Elsevier Inc. All rights reserved.
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