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Redox Activation Of Mitochondrial Intermembrane Space Cu,Zn-superoxide Dismutase.

P. Iñarrea, H. Moini, D. Rettori, Derick Han, Jesús I. Martínez, Inés García, E. Fernández-Vizarra, M. Iturralde, E. Cadenas
Published 2005 · Chemistry, Medicine

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The localization of Cu,Zn-superoxide dismutase in the mitochondrial intermembrane space suggests a functional relationship with superoxide anion (O2*-) released into this compartment. The present study was aimed at examining the functionality of Cu,Zn-superoxide dismutase and elucidating the molecular basis for its activation in the intermembrane space. Intact rat liver mitochondria neither scavenged nor dismutated externally generated O2*-, unless the mitochondrial outer membrane was disrupted selectively by digitonin. The activation of the intermembrane space Cu,Zn-superoxide dismutase following the disruption of mitochondrial outer membrane was largely inhibited by bacitracin, an inhibitor of protein disulphide-isomerase. Thiol alkylating agents, such as N-methylmaleimide or iodoacetamide, decreased intermembrane space Cu,Zn-superoxide dismutase activation during, but not after, disruption of the outer membrane. This inhibitory effect was overcome by exposing mitochondria to low micromolar concentrations of H2O2 before disruption of the outer membrane in the presence of the alkylating agents. Moreover, H2O2 treatment alone enabled intact mitochondria to scavenge externally generated O2*-. These findings suggest that intermembrane space Cu,Zn-superoxide dismutase is inactive in intact mitochondria and that an oxidative modification of its critical thiol groups is necessary for its activation.
This paper references
Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein).
J. McCord (1969)
Superoxide dismutase: improved assays and an assay applicable to acrylamide gels.
C. Beauchamp (1971)
Mitochondrial superoxide simutase. Site of synthesis and intramitochondrial localization.
R. Weisiger (1973)
Intracellular localization of superoxide dismutase and its relation to the distribution and mechanism of hydrogen peroxide-producting enzymes.
G. Rotilio (1973)
Superoxide dismutase. Organelle specificity.
R. Weisiger (1973)
Superoxide dismutase in the anaerobic flagellates, Tritrichomonas foetus and Monocercomonas sp.
D. Lindmark (1974)
Mitochondrial production of superoxide anions and its relationship to the antimycin insensitive respiration
A. Boveris (1975)
Subcellular localization of superoxide dismutase in rat liver.
C. Peeters-Joris (1975)
Polarographic assay and intracellular distribution of superoxide dismutase in rat liver.
D. D. Tyler (1975)
A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding.
M. M. Bradford (1976)
Production of superoxide radicals and hydrogen peroxide by NADH-ubiquinone reductase and ubiquinol-cytochrome c reductase from beef-heart mitochondria.
E. Cadenas (1977)
Bacitracin: an inhibitor of the insulin degrading activity of glutathione-insulin transhydrogenase.
R. Roth (1981)
A quantitative fluorimetric assay for the determination of oxidant production by polymorphonuclear leukocytes: its use in the simultaneous fluorimetric assay of cellular activation processes.
P. Hyslop (1984)
Localization of a sulphate-activating system within Euglena mitochondria.
T. Saidha (1985)
Localization of a sulphateactivating system within
T. Saidha (1985)
Oxidation of cyanide to the cyanyl radical by peroxidase/H2O2 systems as determined by spin trapping.
S. Moreno (1988)
Molecular cloning of rat liver sulfite oxidase. Expression of a eukaryotic Mo-pterin-containing enzyme in Escherichia coli.
R. M. Garrett (1994)
A comparative study of EPR spin trapping and cytochrome c reduction techniques for the measurement of superoxide anions.
S. Sanders (1994)
Molecular cloning of rat liver sulfite oxidase: expression of a eukaryotic Mo-pterin-containing enzyme
R. M. Garrett (1994)
Application of the aconitase method to the assay of superoxide in the mitochondrial matrices of cultured cells: effects of oxygen, redox cycling agent, TNF-α, IL-1, LPS and inhibitors of respiration
P. R. Gardner (1995)
Relation between the activities reducing disulfides and the protection against membrane permeability transition in rat liver mitochondria.
J. Wudarczyk (1996)
Continuous assay for acid phosphatase using phenyl phosphate.
E. Luchter-Wasylewska (1996)
Spectrophotometric assay for superoxide dismutase based on tetrazolium salt 3'--1--(phenylamino)-carbonyl--3, 4-tetrazolium]-bis(4-methoxy-6-nitro)benzenesulfonic acid hydrate reduction by xanthine-xanthine oxidase.
H. Ukeda (1997)
SP-22 is a thioredoxin-dependent peroxide reductase in mitochondria.
S. Watabe (1997)
The Copper Chaperone for Superoxide Dismutase*
V. Culotta (1997)
Cellular sources and steady-state levels of reactive oxygen species
A. Boveris (1997)
Interferon Regulatory Factor 3 and CREB-Binding Protein/p300 Are Subunits of Double-Stranded RNA-Activated Transcription Factor DRAF1
Brian K. Weaver (1998)
Purification of mitochondrial thioredoxin reductase and its involvement in the redox regulation of membrane permeability.
M. P. Rigobello (1998)
Disruption of the outer mitochondrial membrane as a result of large amplitude swelling: the impact of irreversible permeability transition
P. Petit (1998)
Mammalian Peroxiredoxin Isoforms Can Reduce Hydrogen Peroxide Generated in Response to Growth Factors and Tumor Necrosis Factor-α*
S. W. Kang (1998)
The protein disulphide-isomerase family: unravelling a string of folds.
D. Ferrari (1999)
[Xanthine oxidase].
Y. Hidaka (1999)
In vivo formation of Cu,Zn superoxide dismutase disulfide bond in Escherichia coli
A. Battistoni (1999)
Mitochondrial free radical generation, oxidative stress, and aging.
E. Cadenas (2000)
Identification of a New Type of Mammalian Peroxiredoxin That Forms an Intramolecular Disulfide as a Reaction Intermediate*
M. S. Seo (2000)
Alkylation kinetics of proteins in preparation for two‐dimensional maps: A matrix assisted laser desorption/ionization‐mass spectrometry investigation
M. Galvani (2001)
Subcellular Distribution of Superoxide Dismutases (SOD) in Rat Liver
A. Okado-Matsumoto (2001)
NADH Oxidase Activity of Mitochondrial Apoptosis-inducing Factor*
M. D. Miramar (2001)
Mitochondrial respiratory chain-dependent generation of superoxide anion and its release into the intermembrane space.
D. Han (2001)
Distribution of protein disulphide isomerase in rat liver mitochondria.
M. P. Rigobello (2001)
A fraction of yeast Cu,Zn-superoxide dismutase and its metallochaperone, CCS, localize to the intermembrane space of mitochondria. A physiological role for SOD1 in guarding against mitochondrial oxidative damage.
L. Sturtz (2001)
Purification and determination of activity of mitochondrial cyanide-sensitive superoxide dismutase in rat tissue extract.
P. Iñarrea (2002)
A Comparative Study on the Hydroperoxide and Thiol Specificity of the Glutathione Peroxidase Family and Selenoprotein P*
G. Takebe (2002)
Free radicals in the physiological control of cell function.
W. Dröge (2002)
Formation and transfer of disulphide bonds in living cells
C. Sevier (2002)
dismutases (SOD) in rat liver: Cu,Zn-SOD in mitochondria
L. A. Sturtz (2002)
Voltage-dependent Anion Channels Control the Release of the Superoxide Anion from Mitochondria to Cytosol*
D. Han (2003)
Structure, mechanism and regulation of peroxiredoxins.
Z. Wood (2003)
Factors Controlling the Uptake of Yeast Copper/Zinc Superoxide Dismutase into Mitochondria*
L. S. Field (2003)
Peroxiredoxin Evolution and the Regulation of Hydrogen Peroxide Signaling
Z. Wood (2003)
Reversible Oxidation of the Active Site Cysteine of Peroxiredoxins to Cysteine Sulfinic Acid
H. A. Woo (2003)
On the compartmentalization of catalase, fatty acyl-CoA oxidase and urate oxidase in mammalian livers, and the influence of clofibrate treatment on this microlocalization
A. Hemsley (2004)

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Chynna N. Broxton (2016)
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Sensing hypoxia by mitochondria : a unifying hypothesis involving S-nitrosation
UllrichVolker (2014)
Mechanisms of mutant SOD1 induced mitochondrial toxicity in amyotrophic lateral sclerosis
Piia Vehviläinen (2014)
Over-expressed copper/zinc superoxide dismutase localizes to mitochondria in neurons inhibiting the angiotensin II-mediated increase in mitochondrial superoxide☆
Shumin Li (2013)
Eficiência no uso de água e de potássio no cultivo e na produção do morangueiro
Edilson Ramos Gomes (2013)
Mitochondrial metabolism of reactive oxygen species.
P. Venditti (2013)
Principles in redox signaling: from chemistry to functional significance.
A. Bindoli (2013)
Integrated free radical sensor systems for investigation of cellular models of disease
S. Boulton (2012)
Schisandrin B as a Hormetic Agent for Preventing Age-Related Neurodegenerative Diseases
Philip Y. Lam (2012)
Mutant Cu/Zn-Superoxide Dismutase Induced Mitochondrial Dysfunction in Amyotrophic Lateral Sclerosis
J. Koistinaho (2012)
Models of Mitochondrial Oxidative Stress
E. Cadenas (2011)
Mitochondrial protein tyrosine nitration
L. Castro (2011)
Mitochondrial Cu,Zn-Superoxide Dismutase Mediates Pulmonary Fibrosis by Augmenting H2O2 Generation*
C. He (2011)
Superoxide dismutase deficiency enhances superoxide levels in brain tissues during oxygenation and hypoxia‐reoxygenation
T. Sasaki (2011)
Melatonin and steroid hormones activate intermembrane Cu,Zn-superoxide dismutase by means of mitochondrial cytochrome P450.
P. Iñarrea (2011)
Are Mitochondria a Source , a Sink , or a Target of ROS ?
A. Starkov (2010)
Mitochondrial potassium channels and reactive oxygen species
D. Malińska (2010)
The Sod2 mutant mouse as a model for oxidative stress: a functional proteomics perspective.
Yie Hou Lee (2010)
Atividade peroxidásica da enzima superóxido dismutase 1 humana: produção do radical carbonato, dimerização covalente da enzima e implicações para a esclerose lateral amiotrófica
D. B. Medinas (2010)
Asymmetric superoxide release inside and outside the mitochondria in skeletal muscle under conditions of aging and disuse.
X. Xu (2010)
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