期刊
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
卷 484, 期 2, 页码 197-204出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2009.01.022
关键词
NADPH oxidase; Protein disulfide isomerase; Oxidative stress; Vascular smooth muscle cell; Nitric oxide; Nitrosothiol; Thiol oxidation; Oxidoreductases; Redox signaling; Chaperones
资金
- Fundacao de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP)
- Conselho Nacional de Pesquisa (CNPq)
- Instituto do Milenio Redoxoma (CNPq)
- Fundacao Zerbini
Mechanisms regulating NADPH oxidase remain open and include the redox chaperone protein disulfide isomerase (PDI). Here, we further investigated PDI effects on vascular NADPH oxidase. VSMC transfected with wild-type PDI (wt-PDI) OF PDI mutated in all four redox cysteines (mut-PDI) enhanced (2.5-fold) basal cellular ROS production and membrane NADPH oxidase activity, with 3-fold increase in Nox1, but not Nox4 mRNA. However, further ROS production, NADPH oxidase activity and Nox1 mRNA increase triggered by angiotensin-II (AngII) were totally lost with PDI overexpression, suggesting preemptive Nox1 activation in such cells. PDI overexpression increased Nox4 mRNA after AngII stimulus, although without parallel ROS increase. We also show that Nox inhibition by the nitric oxide donor GSNO is independent of PDI. PDI silencing decreased specifically Nox1 mRNA and protein, confirming that PDI may regulate Nox1 at transcriptional level in VSMC. Such data further strengthen the role of PDI as novel NADPH oxidase regulator. (C) 2009 Elsevier Inc. All rights reserved.
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