Oxidative stress enhanced the transforming growth factor-β2-induced epithelial-mesenchymal transition through chemokine ligand 1 on ARPE-19 cell.

Scientific Reports
I-Hui YangHsiu-Mei Huang

Abstract

Fibroblast-like transformation of retinal pigment epithelial (RPE) cells is a pathological feature of proliferative vitreoretinopathy (PVR) that may cause blindness. The effect of oxidative stress alone or together with transforming growth factor-beta 2 (TGF-β2) on epithelial-mesenchymal transformation (EMT) is not fully understood in RPE. TGF-β2 induced the upregulation EMT markers including α-smooth muscle actin (α-SMA), Snail, and Slug and downregulation of E-cadherin (E-cad) in ARPE-19 cells. Hydrogen peroxide (H2O2) not only upregulated α-SMA but also enhanced the effect of TGF-β2 on the expression of Snail and Slug. The CXCL family of cytokines could be the mediators of EMT induced by H2O2 and TGF-β2. H2O2 induced CXCL1, that upregulated α-SMA and fibronectin. Both SB225002, an inhibitor of CXCR2, and antioxidant N-acetylcysteine suppressed the TGF-β2-induced EMT in ARPE-19 cells. Taken together, the results suggest that oxidative stress enhanced TGF-β2-induced EMT through the possible autocrine effect of CXCL1 on CXCR2 in ARPE-19 cells.

References

Sep 9, 2000·Molecular Aspects of Medicine·G Poli
Oct 18, 2000·Survey of Ophthalmology·S BeattyM Boulton
Sep 13, 2001·Molecular Biology of the Cell·B HinzC Chaponnier
Nov 25, 2003·The Journal of Investigative Dermatology·Richard A F ClarkJean E Schwarzbauer
May 17, 2005·American Journal of Respiratory and Critical Care Medicine·Vuokko L KinnulaTim D Oury
Jan 7, 2006·The Journal of Investigative Dermatology·Randle M GallucciJames J Tomasek
Mar 28, 2006·Investigative Ophthalmology & Visual Science·David N ZacksAnand Swaroop
Sep 20, 2006·The Journal of Biological Chemistry·Liqiong GuiDenise C Hocking
May 26, 2007·The American Journal of Pathology·Boris HinzGiulio Gabbiani
Feb 15, 2008·Pediatric Nephrology : Journal of the International Pediatric Nephrology Association·Yukihiko KawasakiMitsuaki Hosoya
May 3, 2008·Genes & Development·Xiaoming ZhouStephen J Weiss
May 9, 2009·Genes to Cells : Devoted to Molecular & Cellular Mechanisms·Junko InumaruHideyuki Saya
Jun 3, 2009·The Journal of Clinical Investigation·Raghu Kalluri
Jun 3, 2009·The Journal of Clinical Investigation·Raghu Kalluri, Robert A Weinberg
Feb 24, 2011·Annals of Oncology : Official Journal of the European Society for Medical Oncology·W-L ChengK-H Lin
Sep 20, 2011·Fibrogenesis & Tissue Repair·Wing S To, Kim S Midwood
Dec 4, 2012·The Journal of Biological Chemistry·Manu JainNavdeep S Chandel
Dec 12, 2012·Biochimica Et Biophysica Acta·Paul ChereshDavid W Kamp
Apr 20, 2013·International Immunopharmacology·Xiao-Hua ShenGuo-Sheng Fu
Dec 21, 2013·Ocular Immunology and Inflammation·Chrysanthos SymeonidisEudoxia Diza
Feb 22, 2014·Nature Reviews. Molecular Cell Biology·Samy LamouilleRik Derynck
Mar 15, 2015·Clinical and Experimental Immunology·C SymeonidisS A Dimitrakos

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BETA
ELISA
PCR
electrophoresis

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SPSS

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