scholarly journals Post-Translational Modifications of Cytochrome c in Cell Life and Disease

2020 ◽  
Vol 21 (22) ◽  
pp. 8483
Author(s):  
Alejandra Guerra-Castellano ◽  
Inmaculada Márquez ◽  
Gonzalo Pérez-Mejías ◽  
Antonio Díaz-Quintana ◽  
Miguel A. De la Rosa ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Electron Transport Chain ◽  
Control Mechanism ◽  
Cell Metabolism ◽  
Post Translational Modifications ◽  
Life And Death ◽  
Cell Life ◽  
Transport Chain ◽  
Respiratory Electron Transport

Mitochondria are the powerhouses of the cell, whilst their malfunction is related to several human pathologies, including neurodegenerative diseases, cardiovascular diseases, and various types of cancer. In mitochondrial metabolism, cytochrome c is a small soluble heme protein that acts as an essential redox carrier in the respiratory electron transport chain. However, cytochrome c is likewise an essential protein in the cytoplasm acting as an activator of programmed cell death. Such a dual role of cytochrome c in cell life and death is indeed fine-regulated by a wide variety of protein post-translational modifications. In this work, we show how these modifications can alter cytochrome c structure and functionality, thus emerging as a control mechanism of cell metabolism but also as a key element in development and prevention of pathologies.

Double-edged sword in cells: chemical biology studies of the vital role of cytochrome c in the intrinsic pre-apoptotic mitochondria leakage pathway

RSC Advances ◽  
2015 ◽  
Vol 5 (36) ◽  
pp. 28258-28269 ◽  
Author(s):  
Zhi-Peng Wang ◽  
Xiao-Zhe Ding ◽  
Jun Wang ◽  
Yi-Ming Li
Keyword(s):  
Cell Death ◽  
Electron Transport ◽  
Cytochrome C ◽  
Electron Transport Chain ◽  
Chemical Biology ◽  
Vital Role ◽  
Mitochondrial Electron Transport Chain ◽  
Transport Chain ◽  
Cyt C

Besides functioning as an electron transporter in the mitochondrial electron transport chain, cytochrome c (cyt c) is also one of the determinants in the execution of cell death.

scholarly journals Effects of L-Malate on Mitochondrial Oxidoreductases in Liver of Aged Rats

2011 ◽  
pp. 329-336 ◽  
Author(s):  
J.-L. WU ◽  
Q.-P. WU ◽  
Y.-P. PENG ◽  
J.-M. ZHANG
Keyword(s):  
Electron Transport ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Electron Transport Chain ◽  
Nadh Dehydrogenase ◽  
Tricarboxylic Acid Cycle ◽  
Radical Scavenger ◽  
Aged Rats ◽  
Transport Chain ◽  
Nadh Cytochrome

Accumulation of oxidative damage has been implicated to be a major causative factor in the decline in physiological functions that occur during the aging process. The mitochondrial respiratory chain is a powerful source of reactive oxygen species (ROS), considered as the pathogenic agent of many diseases and aging. L-malate, a tricarboxylic acid cycle intermediate, plays an important role in transporting NADH from cytosol to mitochondria for energy production. Previous studies in our laboratory reported L-malate as a free radical scavenger in aged rats. In the present study we focused on the effect of L-malate on the activities of electron transport chain in young and aged rats. We found that mitochondrial membrane potential (MMP) and the activities of succinate dehydrogenase, NADH-cytochrome c oxidoreductase and cytochrome c oxidase in liver of aged rats were significantly decreased when compared to young control rats. Supplementation of L-malate to aged rats for 30 days slightly increased MMP and improved the activities of NADH-dehydrogenase, NADH-cytochrome c oxidoreductase and cytochrome c oxidase in liver of aged rats when compared with aged control rats. In young rats, L-malate administration increased only the activity of NADH-dehydrogenase. Our result suggested that L-malate could improve the activities of electron transport chain enzymes in aged rats

scholarly journals An overview of chagasic cardiomyopathy: pathogenic importance of oxidative stress

2005 ◽  
Vol 77 (4) ◽  
pp. 695-715 ◽  
Author(s):  
Michele A. Zacks ◽  
Jian-Jun Wen ◽  
Galina Vyatkina ◽  
Vandanajay Bhatia ◽  
Nisha Garg
Keyword(s):  
Oxidative Stress ◽  
Electron Transport Chain ◽  
Common Source ◽  
Oxygen Species ◽  
Pathogen Invasion ◽  
Immune Mediated ◽  
Transport Chain ◽  
Chagasic Cardiomyopathy ◽  
The Common

There is growing evidence to suggest that chagasic myocardia are exposed to sustained oxidative stress-induced injuries that may contribute to disease progression. Pathogen invasion- and replication-mediated cellular injuries and immune-mediated cytotoxic reactions are the common source of reactive oxygen species (ROS) in infectious etiologies. However, our understanding of the source and role of oxidative stress in chagasic cardiomyopathy (CCM) remains incomplete. In this review, we discuss the evidence for increased oxidative stress in chagasic disease, with emphasis on mitochondrial abnormalities, electron transport chain dysfunction and its role in sustaining oxidative stress in myocardium. We discuss the literature reporting the consequences of sustained oxidative stress in CCM pathogenesis.

scholarly journals Heme Oxygenase-1 Supports Mitochondrial Energy Production and Electron Transport Chain Activity in Cultured Lung Epithelial Cells

2020 ◽  
Vol 21 (18) ◽  
pp. 6941
Author(s):  
Jennifer F. Carr ◽  
David Garcia ◽  
Alejandro Scaffa ◽  
Abigail L. Peterson ◽  
Andrew J. Ghio ◽  
...  
Keyword(s):  
Electron Transport ◽  
Heme Oxygenase ◽  
Electron Transport Chain ◽  
Iron Concentration ◽  
Heme Iron ◽  
Lung Epithelial Cells ◽  
Heme Oxygenase 1 ◽  
Protective Effects ◽  
Transport Chain

Heme oxygenase-1 is induced by many cellular stressors and catalyzes the breakdown of heme to generate carbon monoxide and bilirubin, which confer cytoprotection. The role of HO-1 likely extends beyond the simple production of antioxidants, for example HO-1 activity has also been implicated in metabolism, but this function remains unclear. Here we used an HO-1 knockout lung cell line to further define the contribution of HO-1 to cellular metabolism. We found that knockout cells exhibit reduced growth and mitochondrial respiration, measured by oxygen consumption rate. Specifically, we found that HO-1 contributed to electron transport chain activity and utilization of certain mitochondrial fuels. Loss of HO-1 had no effect on intracellular non-heme iron concentration or on proteins whose levels and activities depend on available iron. We show that HO-1 supports essential functions of mitochondria, which highlights the protective effects of HO-1 in diverse pathologies and tissue types. Our results suggest that regulation of heme may be an equally significant role of HO-1.

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