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• W2528698712 abstract "// Bin Wang 1,* , Lilu Lin 2,* , Haidong Wang 3 , Honglei Guo 2 , Yong Gu 2 and Wei Ding 2 1 Division of Nephrology, Huashan Hospital and Institute of Nephrology, Fudan University, Xuhui, Shanghai, P.R. China 2 Division of Nephrology, The Fifth People’s Hospital of Shanghai, Fudan University, Shanghai, P.R. China 3 College of Animal Science and Veterinary Medicine, Shanxi Agricultural University, Taigu, Shanxi, P.R. China * These authors have contributed equally to this work Correspondence to: Wei Ding, email: // Keywords : tubular cell, oxidative stress, endoplasmic reticulum stress, apoptosis, aldosterone, Pathology Section Received : June 30, 2016 Accepted : September 28, 2016 Published : October 06, 2016 Abstract The renin-angiotensin-aldosterone system (RAAS) is overactivated in patients with chronic kidney disease. Oxidative stress and endoplasmic reticulum stress (ERS) are two major mechanisms responsible for aldosterone-induced kidney injury. Cyclophilin (CYP) B is a chaperone protein that accelerates the rate of protein folding through its peptidyl-prolyl cis-trans isomerase (PPIase) activity. We report that overexpression of wild-type CYPB attenuated aldosterone-induced oxidative stress (evidenced by reduced production of reactive oxygen species and improved mitochondrial dysfunction), ERS (indicated by reduced expression of the ERS markers glucose-regulated protein 78 [GRP78] and C/-EBP homologous protein [CHOP]), and tubular cell apoptosis in comparison with aldosterone-induced human kidney-2 (HK-2) cells. The in vivo study also yielded similar results. Hence, CYPB performs a crucial function in protecting cells against aldosterone-induced oxidative stress, ERS, and tubular cell injury via its PPIase activity." @default.
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• W2528698712 date "2016-10-06" @default.
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• W2528698712 title "Overexpressed cyclophilin B suppresses aldosterone-induced proximal tubular cell injury both <i>in vitro</i> and <i>in vivo</i>" @default.
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• W2528698712 doi "https://doi.org/10.18632/oncotarget.12503" @default.
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