Voltage-dependent Anion Channels Control the Release of the Superoxide Anion from Mitochondria to Cytosol

Han, Derick; Antunes, Fernando; Canali, Raffaella; Rettori, Daniel; Cadenas, Enrique

doi:10.1074/jbc.m210269200

Cited by 624 publications

(447 citation statements)

References 54 publications

(22 reference statements)

Supporting

Mentioning

426

Contrasting

Unclassified

Order By: Relevance

“…Furthermore, mitochondrial function requires redox homeostasis, which is mediated primarily by the voltage-dependent anion channel (VDAC; porin pore). The VDAC releases superoxide anion from the mitochondria to the cytosol and increases cytosolic ROS (Han et al, 2003). The elevated expression of cell rescue systems makes it easy to modify neutralizing ROS or repair oxidative damage (Fig.…”

Section: A B C Discussionmentioning

confidence: 99%

Saccharomyces cerevisiae KNU5377 Stress Response during High-Temperature Ethanol Fermentation

Kim

et al. 2013

Molecules and Cells

View full text Add to dashboard Cite

Section: A B C Discussionmentioning

confidence: 99%

Saccharomyces cerevisiae KNU5377 Stress Response during High-Temperature Ethanol Fermentation

Kim

et al. 2013

Molecules and Cells

View full text Add to dashboard Cite

“…However, it can cross membranes through anion channels including the inner membrane anion channel and the voltage‐dependent anion channels55, 87, 88 (Figure 4). Nonetheless, it has been argued that superoxide can be protonated at physiological pH to produce the hydroperoxyl radical, enabling the transfer of superoxide across biomembranes 89.…”

Section: Chemistry Of Reactive Oxygen and Nitrogen Species Produced Bmentioning

confidence: 99%

Redox homeostasis and age‐related deficits in neuromuscular integrity and function

Sakellariou

Lightfoot

Earl

et al. 2017

J cachexia sarcopenia muscle

View full text Add to dashboard Cite

Skeletal muscle is a major site of metabolic activity and is the most abundant tissue in the human body. Age‐related muscle atrophy (sarcopenia) and weakness, characterized by progressive loss of lean muscle mass and function, is a major contributor to morbidity and has a profound effect on the quality of life of older people. With a continuously growing older population (estimated 2 billion of people aged >60 by 2050), demand for medical and social care due to functional deficits, associated with neuromuscular ageing, will inevitably increase. Despite the importance of this ‘epidemic’ problem, the primary biochemical and molecular mechanisms underlying age‐related deficits in neuromuscular integrity and function have not been fully determined. Skeletal muscle generates reactive oxygen and nitrogen species (RONS) from a variety of subcellular sources, and age‐associated oxidative damage has been suggested to be a major factor contributing to the initiation and progression of muscle atrophy inherent with ageing. RONS can modulate a variety of intracellular signal transduction processes, and disruption of these events over time due to altered redox control has been proposed as an underlying mechanism of ageing. The role of oxidants in ageing has been extensively examined in different model organisms that have undergone genetic manipulations with inconsistent findings. Transgenic and knockout rodent studies have provided insight into the function of RONS regulatory systems in neuromuscular ageing. This review summarizes almost 30 years of research in the field of redox homeostasis and muscle ageing, providing a detailed discussion of the experimental approaches that have been undertaken in murine models to examine the role of redox regulation in age‐related muscle atrophy and weakness.

show abstract

“…Complex III (CIII), also a key site of ROS generation, [6,[10][11][12] has been shown to release superoxide to both sides of the inner mitochondrial membrane [10,[13][14][15] The sites of release of ROS suggest that the protein components most proximal to these sites may also be at risk for oxidative damage. Thus, the identification of oxidatively modified proteins of the ETC complexes may contribute to further understanding of the molecular mechanisms of mitochondrial dysfunction in aging and age-associated cardiomyocytes injury.…”

Section: Introductionmentioning

confidence: 99%

Age-related alterations in oxidatively damaged proteins of mouse heart mitochondrial electron transport chain complexes

Choksi

Papaconstantinou

2008

Free Radical Biology and Medicine

View full text Add to dashboard Cite

Mitochondrial generated ROS increases with age and is a major factor that damages proteins by oxidative modification. Accumulation of oxidatively damaged proteins has been implicated as a causal factor in the age-associated decline in tissue function. Mitochondrial electron transport chain (ETC) complexes I and III are the principle sites of ROS production, and oxidative modifications to their complex subunits inhibit their in vitro activity. We hypothesize that mitochondrial complex subunits may be primary targets for modification by ROS which may impair normal complex activity. This study of heart mitochondria from young, middle-aged and old mice reveals that there is an agerelated decline in complex I and V activities that correlate with increased oxidative modification to their subunits. The data also show a specificity for modifications of the ETC complex subunits, i.e., several proteins have more than one type of adduct. We postulate that the electron leakage from ETC complexes causes specific damage to their subunits and increased ROS generation as oxidative damage accumulates, leading to further mitochondrial dysfunction, a cyclical process that underlies the progressive decline in physiologic function of aged mouse heart.

show abstract

Voltage-dependent Anion Channels Control the Release of the Superoxide Anion from Mitochondria to Cytosol

Cited by 624 publications

References 54 publications

Saccharomyces cerevisiae KNU5377 Stress Response during High-Temperature Ethanol Fermentation

Saccharomyces cerevisiae KNU5377 Stress Response during High-Temperature Ethanol Fermentation

Redox homeostasis and age‐related deficits in neuromuscular integrity and function

Age-related alterations in oxidatively damaged proteins of mouse heart mitochondrial electron transport chain complexes

Contact Info

Product

Resources

About