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71.
Cellular oxidative stress results from the increased generation of reactive oxygen species and/or the dysfunction of the antioxidant systems. Most intracellular reactive oxygen species derive from superoxide radical although the majority of the biological effects of reactive oxygen species are mediated by hydrogen peroxide. In this contribution we overview the major cellular sites of reactive oxygen species production, with special emphasis in the mitochondrial pathways. Reactive oxygen species regulate signaling pathways involved in promoting survival and cell death, proliferation, metabolic regulation, the activation of the antioxidant response, the control of iron metabolism and Ca2 + signaling. The reversible oxidation of cysteines in transducers of reactive oxygen species is the primary mechanism of regulation of the activity of these proteins. Next, we present the mitochondrial H+-ATP synthase as a core hub in energy and cell death regulation, defining both the rate of energy metabolism and the reactive oxygen species-mediated cell death in response to chemotherapy. Two main mechanisms that affect the expression and activity of the H+-ATP synthase down-regulate oxidative phosphorylation in prevalent human carcinomas. In this context, we emphasize the prominent role played by the ATPase Inhibitory Factor 1 in human carcinogenesis as an inhibitor of the H+-ATP synthase activity and a mediator of cell survival. The ATPase Inhibitory Factor 1 promotes metabolic rewiring to an enhanced aerobic glycolysis and the subsequent production of mitochondrial reactive oxygen species. The generated reactive oxygen species are able to reprogram the nucleus to support tumor development by arresting cell death. Overall, we discuss the cross-talk between reactive oxygen species signaling and mitochondrial function that is crucial in determining the cellular fate. This article is part of a Special Issue entitled: 18th European Bioenergetic Conference. 相似文献
72.
Stefan Dröse Ulrich Brandt Ilka Wittig 《Biochimica et Biophysica Acta - Proteins and Proteomics》2014,1844(8):1344-1354
The respiratory chain of the inner mitochondrial membrane is a unique assembly of protein complexes that transfers the electrons of reducing equivalents extracted from foodstuff to molecular oxygen to generate a proton-motive force as the primary energy source for cellular ATP-synthesis. Recent evidence indicates that redox reactions are also involved in regulating mitochondrial function via redox-modification of specific cysteine-thiol groups in subunits of respiratory chain complexes. Vice versa the generation of reactive oxygen species (ROS) by respiratory chain complexes may have an impact on the mitochondrial redox balance through reversible and irreversible thiol-modification of specific target proteins involved in redox signaling, but also pathophysiological processes. Recent evidence indicates that thiol-based redox regulation of the respiratory chain activity and especially S-nitrosylation of complex I could be a strategy to prevent elevated ROS production, oxidative damage and tissue necrosis during ischemia–reperfusion injury. This review focuses on the thiol-based redox processes involving the respiratory chain as a source as well as a target, including a general overview on mitochondria as highly compartmentalized redox organelles and on methods to investigate the redox state of mitochondrial proteins. This article is part of a Special Issue entitled: Thiol-Based Redox Processes. 相似文献
73.
F. MINIBAYEVA O. KOLESNIKOV A. CHASOV R. P. BECKETT S. LÜTHJE N. VYLEGZHANINA F. BUCK & M. BÖTTGER 《Plant, cell & environment》2009,32(5):497-508
Production of reactive oxygen species (ROS) is a widely reported response of plants to wounding. However, the nature of enzymes responsible for ROS production and metabolism in the apoplast is still an open question. We identified and characterized the proteins responsible for the wound-induced production and detoxification of ROS in the apoplast of wheat roots ( Triticum aestivum L.). Compared to intact roots, excised roots and leachates derived from them produced twice the amount of superoxide (O2 •− ). Wounding also induced extracellular peroxidase (ECPOX) activity mainly caused by the release of soluble peroxidases with molecular masses of 37, 40 and 136 kD. Peptide mass analysis by electrospray ionization–quadrupole time-of-flight–tandem mass spectrometry (ESI–QTOF–MS/MS) following lectin affinity chromatography of leachates showed the presence of peroxidases in unbound (37 kD) and bound (40 kD) fractions. High sensitivity of O2 •− -producing activity to peroxidase inhibitors and production of O2 •− by purified peroxidases in vitro provided evidence for the involvement of ECPOXs in O2 •− production in the apoplast. Our results present new insights into the rapid response of roots to wounding. An important component of this response is mediated by peroxidases that are released from the cell surface into the apoplast where they can display both oxidative and peroxidative activities. 相似文献
74.
Heterologous expression and characterization of a proxidomal ascorbate peroxidase from <Emphasis Type="Italic">Populus tomentosa</Emphasis> 总被引:1,自引:0,他引:1
The present study reported for the first time, cloning, expression and characteristics of a Proxidomal APX gene (PpAPX) from
Populus tomentosa. The PpAPX gene encodes a protein of 287 amino acid residues with a calculated molecular mass of 31.58 kDa. The over-expressed
recombinant PpAPX protein showed high activity towards the substrates ascorbate aicd (ASA) and H2O2. At fixed ASA concentrations, the K
m and V
max values were 0.12 ± 0.01 mM and 23.4 ± 4.2 mmol/min mg for H2O2. And at fixed H2O2 concentrations, the K
m and V
max values were 0.53 ± 0.04 mM and 20.0 ± 2.3 mmol/min mg for ASA. 相似文献
75.
76.
Plants of Miscanthus sinensis (cv. Giganteus) were grown in hydroponics for three months in nutrient solution with 0, 2.2, 4.4 and 6.6 μM CdNO3. Growth parameters, catalase (CAT), guaiacol peroxidase (POD), ascorbate peroxidase (APX) and superoxide dismutase (SOD)
activities were analysed in leaves and roots collected after 1-and 3-month exposure. Dry biomass of all miscanthus organs
was affected by Cd concentration both after 1-and 3-month exposure. No visible symptoms of Cd toxicity were observed in shoots
and rhizomes of plants grown in presence of Cd. In contrast, roots became shorter and thicker and the whole root system more
dense and compact already after one month of treatment with 6.6 μM Cd. The lower Cd concentration increased the enzymes activities
after 3 months in leaves and only after 1-month in roots, while a decrease in activity was observed at higher Cd concentrations. 相似文献
77.
Studies on the superoxide anion production and peroxidase activity in potato leaf cell suspension exposed to salicylic acid 总被引:1,自引:0,他引:1
It is now widely accepted that salicylic acid (SA) signaling is mediated by reactive oxygen species (ROS) production. We have
studied the effect of SA on peroxidase activity and superoxide anion production in potato leaf cell suspension. The results
show that potato cells are insensitive to low concentrations of exogenous SA (< 1 mM) and the effect is observed at 1–5 mM
SA. The cells exposed to SA exhibit higher peroxidase activity and show different peroxidase pattern when analyzed on native
gels compared to the control. Superoxide anion production is enhanced after two hours of treatment and 2.5 mM SA gives the
highest value. The results suggest peroxidase-mediated detoxification of ROS elicited by SA. 相似文献
78.
Background
The term GSSG/GSH redox potential is frequently used to explain redox regulation and other biological processes.Scope of review
The relevance of the GSSG/GSH redox potential as driving force of biological processes is critically discussed. It is recalled that the concentration ratio of GSSG and GSH reflects little else than a steady state, which overwhelmingly results from fast enzymatic processes utilizing, degrading or regenerating GSH.Major conclusions
A biological GSSG/GSH redox potential, as calculated by the Nernst equation, is a deduced electrochemical parameter based on direct measurements of GSH and GSSG that are often complicated by poorly substantiated assumptions. It is considered irrelevant to the steering of any biological process. GSH-utilizing enzymes depend on the concentration of GSH, not on [GSH]2, as is predicted by the Nernst equation, and are typically not affected by GSSG. Regulatory processes involving oxidants and GSH are considered to make use of mechanistic principles known for thiol peroxidases which catalyze the oxidation of hydroperoxides by GSH by means of an enzyme substitution mechanism involving only bimolecular reaction steps.General significance
The negligibly small rate constants of related spontaneous reactions as compared with enzyme-catalyzed ones underscore the superiority of kinetic parameters over electrochemical or thermodynamic ones for an in-depth understanding of GSH-dependent biological phenomena. At best, the GSSG/GSH potential might be useful as an analytical tool to disclose disturbances in redox metabolism. This article is part of a Special Issue entitled Cellular Functions of Glutathione. 相似文献79.
Valentina Bosello-Travain Marcus Conrad Giorgio Cozza Alessandro Negro Silvia Quartesan Monica Rossetto Antonella Roveri Stefano Toppo Fulvio Ursini Mattia Zaccarin Matilde Maiorino 《Biochimica et Biophysica Acta (BBA)/General Subjects》2013
Background
Mammalian GPx7 is a monomeric glutathione peroxidase of the endoplasmic reticulum (ER), containing a Cys redox center (CysGPx). Although containing a peroxidatic Cys (CP) it lacks the resolving Cys (CR), that confers fast reactivity with thioredoxin (Trx) or related proteins to most other CysGPxs.Methods
Reducing substrate specificity and mechanism were addressed by steady-state kinetic analysis of wild type or mutated mouse GPx7. The enzymes were heterologously expressed as a synuclein fusion to overcome limited expression. Phospholipid hydroperoxide was the oxidizing substrate. Enzyme–substrate and protein–protein interaction were analyzed by molecular docking and surface plasmon resonance analysis.Results
Oxidation of the CP is fast (k+ 1 > 103 M− 1 s− 1), however the rate of reduction by GSH is slow (k′+ 2 = 12.6 M− 1 s− 1) even though molecular docking indicates a strong GSH–GPx7 interaction. Instead, the oxidized CP can be reduced at a fast rate by human protein disulfide isomerase (HsPDI) (k+ 1 > 103 M− 1 s− 1), but not by Trx. By surface plasmon resonance analysis, a KD = 5.2 μM was calculated for PDI–GPx7 complex. Participation of an alternative non-canonical CR in the peroxidatic reaction was ruled out. Specific activity measurements in the presence of physiological reducing substrate concentration, suggest substrate competition in vivo.Conclusions
GPx7 is an unusual CysGPx catalyzing the peroxidatic cycle by a one Cys mechanism in which GSH and PDI are alternative substrates.General significance
In the ER, the emerging physiological role of GPx7 is oxidation of PDI, modulated by the amount of GSH. 相似文献80.
In this paper an effort has been made to review the literature on the role of peroxidases in the remediation and treatment of a wide spectrum of aromatic pollutants. Peroxidases can catalyse degradation/transformation of polycyclic aromatic hydrocarbons, polychlorinated biphenyls, organochlorines, 2,4,6-trinitrotoluene, phenolic compounds and dyes. These enzymes are also capable of treating various types of recalcitrant aromatic compounds in the presence of redox mediators. Immobilised peroxidases from plant and fungal sources have been used for the remediation of such types of industrial pollutants on a large scale. 相似文献