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Open AccessArticle

Proteomic Analysis Identifies an NADPH Oxidase 1 (Nox1)-Mediated Role for Actin-Related Protein 2/3 Complex Subunit 2 (ARPC2) in Promoting Smooth Muscle Cell Migration

1
Vascular Medicine Institute, 12th Floor BST, 200 Lothrop Street, University of Pittsburgh, PA 15261, USA
2
Department of Pharmacology & Chemical Biology, 13th Floor BST, 200 Lothrop Street, University of Pittsburgh, PA 15261, USA
*
Authors to whom correspondence should be addressed.
Current address: Instituto do Coração, Hospital Das Clinicas Faculdade De Medicina Da USP, Av. Eneas Carvalho Aguiar, 44. Vascular Biology Laboratory - 9th Floor, Anexo 2 Sao Paulo, Brazil.
Int. J. Mol. Sci. 2013, 14(10), 20220-20235; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms141020220
Received: 8 August 2013 / Revised: 28 August 2013 / Accepted: 16 September 2013 / Published: 11 October 2013
(This article belongs to the Special Issue Oxidative Stress in Cardiovascular Disease)
A variety of vascular pathologies, including hypertension, restenosis and atherosclerosis, are characterized by vascular smooth muscle cell (VSMC) hypertrophy and migration. NADPH oxidase 1 (Nox1) plays a pivotal role in these phenotypes via distinct downstream signaling. However, the mediators differentiating these distinct phenotypes and their precise role in vascular disease are still not clear. The present study was designed to identify novel targets of VSMC Nox1 signaling using 2D Differential In-Gel Electrophoresis and Mass Spectrometry (2D-DIGE/MS). VSMC treatment with scrambled (Scrmb) or Nox1 siRNA and incubation with the oxidant hydrogen peroxide (H2O2; 50 µM, 3 h) followed by 2D-DIGE/MS on cell lysates identified 10 target proteins. Among these proteins, actin-related protein 2/3 complex subunit 2 (ARPC2) with no previous link to Nox isozymes, H2O2, or other reactive oxygen species (ROS), was identified and postulated to play an intermediary role in VSMC migration. Western blot confirmed that Nox1 mediates H2O2-induced ARPC2 expression in VSMC. Treatment with a p38 MAPK inhibitor (SB203580) resulted in reduced ARPC2 expression in H2O2-treated VSMC. Additionally, wound-healing “scratch” assay confirmed that H2O2 stimulates VSMC migration via Nox1. Importantly, gene silencing of ARPC2 suppressed H2O2-stimulated VSMC migration. These results demonstrate for the first time that Nox1-mediated VSMC migration involves ARPC2 as a downstream signaling target. View Full-Text
Keywords: vascular smooth muscle cell; migration; NADPH oxidase; oxidative stress; ARPC2 vascular smooth muscle cell; migration; NADPH oxidase; oxidative stress; ARPC2
MDPI and ACS Style

Ghouleh, I.A.; Rodríguez, A.; Pagano, P.J.; Csányi, G. Proteomic Analysis Identifies an NADPH Oxidase 1 (Nox1)-Mediated Role for Actin-Related Protein 2/3 Complex Subunit 2 (ARPC2) in Promoting Smooth Muscle Cell Migration. Int. J. Mol. Sci. 2013, 14, 20220-20235. https://0-doi-org.brum.beds.ac.uk/10.3390/ijms141020220

AMA Style

Ghouleh IA, Rodríguez A, Pagano PJ, Csányi G. Proteomic Analysis Identifies an NADPH Oxidase 1 (Nox1)-Mediated Role for Actin-Related Protein 2/3 Complex Subunit 2 (ARPC2) in Promoting Smooth Muscle Cell Migration. International Journal of Molecular Sciences. 2013; 14(10):20220-20235. https://0-doi-org.brum.beds.ac.uk/10.3390/ijms141020220

Chicago/Turabian Style

Ghouleh, Imad A.; Rodríguez, Andrés; Pagano, Patrick J.; Csányi, Gábor. 2013. "Proteomic Analysis Identifies an NADPH Oxidase 1 (Nox1)-Mediated Role for Actin-Related Protein 2/3 Complex Subunit 2 (ARPC2) in Promoting Smooth Muscle Cell Migration" Int. J. Mol. Sci. 14, no. 10: 20220-20235. https://0-doi-org.brum.beds.ac.uk/10.3390/ijms141020220

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