Cellular Energy Metabolism and Oxidative Stress

2015 ◽  
pp. 1-11
Author(s):  
Shujiang Cheng ◽  
Regina Hourigan ◽  
Zeenat Nabi ◽  
Laurence Du-Thumm
Keyword(s):  
Oxidative Stress ◽  
Energy Metabolism ◽  
Cellular Energy ◽  
Cellular Energy Metabolism ◽  
And Oxidative Stress

Cellular Energy Metabolism and Oxidative Stress

2016 ◽  
pp. 617-627
Author(s):  
Shujiang Cheng ◽  
Regina Hourigan ◽  
Zeenat Nabi ◽  
Laurence Du-Thumm
Keyword(s):  
Oxidative Stress ◽  
Energy Metabolism ◽  
Cellular Energy ◽  
Cellular Energy Metabolism ◽  
And Oxidative Stress

scholarly journals Discovery of a Redox Thiol Switch: Implications for Cellular Energy Metabolism

2020 ◽  
Vol 19 (5) ◽  
pp. 852-870 ◽  
Author(s):  
Xing-Huang Gao ◽  
Ling Li ◽  
Marc Parisien ◽  
Jing Wu ◽  
Ilya Bederman ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Energy Metabolism ◽  
Pancreatic Beta Cells ◽  
Large Scale ◽  
Protein S ◽  
Cysteine Residues ◽  
Cellular Energy ◽  
Cellular Energy Metabolism ◽  
Proteomics Approach ◽  
Thiol Switch

The redox-based modifications of cysteine residues in proteins regulate their function in many biological processes. The gas molecule H2S has been shown to persulfidate redox sensitive cysteine residues resulting in an H2S-modified proteome known as the sulfhydrome. Tandem Mass Tags (TMT) multiplexing strategies for large-scale proteomic analyses have become increasingly prevalent in detecting cysteine modifications. Here we developed a TMT-based proteomics approach for selectively trapping and tagging cysteine persulfides in the cellular proteomes. We revealed the natural protein sulfhydrome of two human cell lines, and identified insulin as a novel substrate in pancreatic beta cells. Moreover, we showed that under oxidative stress conditions, increased H2S can target enzymes involved in energy metabolism by switching specific cysteine modifications to persulfides. Specifically, we discovered a Redox Thiol Switch, from protein S-glutathioinylation to S-persulfidation (RTSGS). We propose that the RTSGS from S-glutathioinylation to S-persulfidation is a potential mechanism to fine tune cellular energy metabolism in response to different levels of oxidative stress.

scholarly journals MicroRNA-210 Modulates the Cellular Energy Metabolism Shift During H2O2-Induced Oxidative Stress by Repressing ISCU in H9c2 Cardiomyocytes

2017 ◽  
Vol 43 (1) ◽  
pp. 383-394 ◽  
Author(s):  
Wei Sun ◽  
Lei  Zhao ◽  
Xianjing  Song ◽  
Jichang  Zhang ◽  
Yue  Xing ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Energy Metabolism ◽  
Complex I ◽  
Cluster Assembly ◽  
Iron Sulfur Cluster ◽  
Myocardial Energy Metabolism ◽  
Cellular Energy ◽  
Atp Assay ◽  
Cellular Energy Metabolism ◽  
H9c2 Cardiomyocytes

Background/Aims: The myocardial energy metabolism shift is one of the most important pathological features of ischemic heart disease (IHD). Although several microRNAs (miRs) are involved in the regulation of myocardial energy metabolism, their exact effects and underlying mechanisms remain unclear. The aim of this study was to investigate whether microRNA(miR-210) regulates the energy metabolism shift during oxidative stress in H9c2 cardiomyocytes. Methods: Cell survival was analyzed via CCK assay. The energy metabolism shift was detected by lactate assay, ATP assay and RT2 profiler glucose metabolism PCR array. Protein and mRNA expression levels were determined by western blot and qPCR. We also used kits to detect the activity of Complex I, Sirt3 and the NAD+/NADH ratio. Results: We determined that miR-210 promoted the energy metabolism shift. The iron-sulfur cluster assembly protein (ISCU) was a target of miR-210. Additionally, we detected the activity of complex I and found that miR-210 inhibits mitochondrial respiration. Interestingly, miR-210 may also indirectly regulate SIRT3 by regulating ISCU. Conclusion: Our results confirm that miR-210 is essential and sufficient for modulating the cellular energy metabolism shift during H2O2-induced oxidative stress in H9c2 cardiomyocytes by targeting ISCU.

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