ArticleScientific reports2014
Site-2 protease responds to oxidative stress and regulates oxidative injury in mammalian cells.
Article in Scientific reports, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 11 citations in OpenAlex.
- Oxidative stress-alleviating strategies to improve recombinant protein production in CHO cells.Biotechnology and bioengineering · 2020Review
- MicroRNA-451a targets caveolin-1 in stomach cancer cells.International journal of clinical and experimental pathology · 2020Article
- Metformin inhibits lithocholic acid-induced interleukin 8 upregulation in colorectal cancer cells by suppressing ROS production and NF-kB activity.Scientific reports · 2019Article
- miR-122 Release in Exosomes Precedes Overt Tolvaptan-Induced Necrosis in a Primary Human Hepatocyte Micropatterned Coculture Model.Toxicological sciences : an official journal of the Society of Toxicology · 2018Article
- Regulation of Transcription Factors by Reactive Oxygen Species and Nitric Oxide in Vascular Physiology and Pathology.Antioxidants & redox signaling · 2017Review
- Targeted Deletion of a Plasmodium Site-2 Protease Impairs Life Cycle Progression in the Mammalian Host.PloS one · 2017Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Site-2 protease (S2P) is a membrane-embedded protease that site-specifically cleaves intramembrane transcription factors, a necessary step for their maturation. S2P is well known to regulate cholesterol biosynthesis and endoplasmic reticulum stress in mammalian cells. In this study, we hypothesized that S2P could be responsible for the regulation of cellular oxidative injury under oxidative stress. Wild type Chinese hamster ovary (WT CHO) cells and their mutant M19 cells with defective S2P gene were exposed to different oxidative stress conditions. Results showed that oxidative stress significantly up-regulated S2P expression in WT CHO cells. Notably, M19 cells had remarkably higher level of superoxide and elevated rates of cell death than WT CHO cells. The vulnerability to oxidative stress was reversed by the transfection of S2P gene but not rescued by exogenous supplement of cholesterol, oleate, and mevalonate, indicating that lack of S2P gene leads cells to be more vulnerable to oxidative stress. Furthermore, compared with WT CHO cells, M19 cells had higher nicotinamide adenine dinucleotide phosphate (NADPH) oxidase activity and lower paraoxonase-2 expression. Taken together, these results suggest that S2P can be a protease responding to oxidative stress and has the function of regulating cellular oxidative injury.
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