scholarly journals Free aminothiols, glutathione redox state and protein mixed disulphides in aging Drosophila melanogaster

2004 ◽  
Vol 382 (1) ◽  
pp. 131-136 ◽  
Author(s):  
Igor REBRIN ◽  
Anne-Cécile V. BAYNE ◽  
Robin J. MOCKETT ◽  
William C. ORR ◽  
Rajindar S. SOHAL
Keyword(s):  
Oxidative Stress ◽  
Drosophila Melanogaster ◽  
Life Expectancy ◽  
Ambient Temperature ◽  
Aging Process ◽  
Redox State ◽  
Cellular Redox ◽  
Ambient Temperatures ◽  
Glutathione Redox ◽  
Methionine Content

The main purpose of the present study was to test the hypothesis that the aging process is associated with a pro-oxidizing shift in the cellular redox state. The amounts of the redox-sensitive free aminothiols (glutathione, cysteine, Cys-Gly and methionine) and protein mixed disulphides were measured at different ages and ambient temperatures in Drosophila melanogaster. GSH/GSSG ratios decreased significantly with increasing age of the flies, due to an increase in GSSG content. Concentrations of Cys-Gly increased and methionine decreased with age. The amounts of protein mixed disulphides, measured as protein-cysteinyl, protein-Cys-Gly and protein-glutathionyl mixed disulphides, increased as a function of age. The pattern of changes in free aminothiol content, glutathione-redox state and protein mixed disulphides varied in proportion to the ambient temperature, which is inversely related to the life expectancy of the flies. Collectively, these results support the idea that the pro-oxidizing shift in the glutathione-redox state, the decrease in methionine content and increase in abundance of protein mixed disulphides are associated with the life expectancy of flies, and are indicative of enhanced oxidative stress during aging.

scholarly journals Reactive Oxygen Species-Mediated Control of Mitochondrial Biogenesis

2012 ◽  
Vol 2012 ◽  
pp. 1-8 ◽  
Author(s):  
Edgar D. Yoboue ◽  
Anne Devin
Keyword(s):  
Oxidative Stress ◽  
Mitochondrial Biogenesis ◽  
Redox State ◽  
Mitochondrial Genomes ◽  
Oxygen Species ◽  
Mitochondrial Content ◽  
Cellular Redox ◽  
High Importance ◽  
Complex Process ◽  
Long Time

Mitochondrial biogenesis is a complex process. It necessitates the contribution of both the nuclear and the mitochondrial genomes and therefore crosstalk between the nucleus and mitochondria. It is now well established that cellular mitochondrial content can vary according to a number of stimuli and physiological states in eukaryotes. The knowledge of the actors and signals regulating the mitochondrial biogenesis is thus of high importance. The cellular redox state has been considered for a long time as a key element in the regulation of various processes. In this paper, we report the involvement of the oxidative stress in the regulation of some actors of mitochondrial biogenesis.

scholarly journals Effect of glutathione redox state on Leydig cell susceptibility to acute oxidative stress

2010 ◽  
Vol 323 (2) ◽  
pp. 147-154 ◽  
Author(s):  
Haolin Chen ◽  
Liang Zhou ◽  
Chieh-Yin Lin ◽  
Matthew C. Beattie ◽  
June Liu ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Leydig Cell ◽  
Redox State ◽  
Glutathione Redox

Reassessing cellular glutathione homoeostasis: novel insights revealed by genetically encoded redox probes

2014 ◽  
Vol 42 (4) ◽  
pp. 979-984 ◽  
Author(s):  
Bruce Morgan
Keyword(s):  
Oxidative Stress ◽  
Small Molecule ◽  
Redox State ◽  
Eukaryotic Cell ◽  
Yeast Cells ◽  
Cellular Redox ◽  
Whole Cell ◽  
New Findings ◽  
Cytosolic Glutathione ◽  
Cellular Redox State

Glutathione is the most abundant small molecule thiol in nearly all eukaryotes. Whole-cell levels of oxidized (GSSG) and reduced (GSH) glutathione are variable and responsive to genetic and chemical manipulations, which has led to their relative levels being widely used as a marker of the ‘cellular redox state’ and to indicate the level of ‘oxidative stress’ experienced by cells, tissues and organisms. However, the applicability of glutathione as a marker for a generalized ‘cellular redox state’ is questionable, especially in the light of recent observations in yeast cells. In yeast, whole-cell GSSG changes are almost completely dependent upon the activity of an ABC-C (ATP-binding cassette-C) transporter, Ycf1 (yeast cadmium factor 1), which mediates sequestration of GSSG to the vacuole. In the absence of Ycf1 whole-cell GSSG content is strongly decreased and extremely robust to perturbation. These observations are consistent with highly specific redox-sensitive GFP probe-based measurements of the cytosolic glutathione pool and indicate that cytosolic GSSG reductive systems are easily able to reduce nearly all GSSG formed, even following treatment with large concentrations of oxidant. In the present paper, I discuss the consequences of these new findings for our understanding of glutathione homoeostasis in the eukaryotic cell.

Reactive oxygen species in cell signaling

2000 ◽  
Vol 279 (6) ◽  
pp. L1005-L1028 ◽  
Author(s):  
Victor J. Thannickal ◽  
Barry L. Fanburg
Keyword(s):  
Oxidative Stress ◽  
Reactive Oxygen Species ◽  
Signal Transduction ◽  
Plasma Membrane ◽  
Growth Factors ◽  
Redox State ◽  
Reactive Oxygen ◽  
Oxygen Species ◽  
Cellular Redox ◽  
By Products

Reactive oxygen species (ROS) are generated as by-products of cellular metabolism, primarily in the mitochondria. When cellular production of ROS overwhelms its antioxidant capacity, damage to cellular macromolecules such as lipids, protein, and DNA may ensue. Such a state of “oxidative stress” is thought to contribute to the pathogenesis of a number of human diseases including those of the lung. Recent studies have also implicated ROS that are generated by specialized plasma membrane oxidases in normal physiological signaling by growth factors and cytokines. In this review, we examine the evidence for ligand-induced generation of ROS, its cellular sources, and the signaling pathways that are activated. Emerging concepts on the mechanisms of signal transduction by ROS that involve alterations in cellular redox state and oxidative modifications of proteins are also discussed.

scholarly journals Lower Mitochondrial Proton Leak and Decreased Glutathione Redox in Primary Muscle Cells of Obese Diet-Resistant Versus Diet-Sensitive Humans

2014 ◽  
Vol 99 (11) ◽  
pp. 4223-4230 ◽  
Author(s):  
A. Brianne Thrush ◽  
Rui Zhang ◽  
William Chen ◽  
Erin L. Seifert ◽  
Jessica K. Quizi ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Weight Loss ◽  
Body Mass ◽  
Mitochondrial Function ◽  
Redox State ◽  
Proton Leak ◽  
Oxidized Glutathione ◽  
Muscle Biopsies ◽  
And Oxidative Stress ◽  
Glutathione Redox

Context: Weight loss success in response to energy restriction is highly variable. This may be due in part to differences in mitochondrial function and oxidative stress. Objective: The objective of the study was to determine whether mitochondrial function, content, and oxidative stress differ in well-matched obese individuals in the upper [obese diet sensitive (ODS)] vs lower quintiles [obese diet resistant (ODR)] for rate of weight loss. Design: Primary myotubes derived from muscle biopsies of individuals identified as ODS or ODR were studied. Setting: Compliant ODS and ODR females who completed in the Ottawa Hospital Weight Management Program and identified as ODS and ODR participated in this study. Patients or Other Participants: Eleven ODS and nine ODR weight-stable females matched for age, body mass, and body mass index participated in this study. Intervention: Vastus lateralis muscle biopsies were obtained and processed for muscle satellite cell isolation. Main Outcome Measures: Mitochondrial respiration, content, reactive oxygen species, and glutathione redox ratios were measured in the myotubes of ODS and ODR individuals. Results: Mitochondrial proton leak was increased in myotubes of ODS compared with ODR (P < .05). Reduced and oxidized glutathione was decreased in the myotubes of ODR vs ODS (P < .05), indicating a more oxidized glutathione redox state. There were no differences in myotube mitochondrial content, uncoupling protein 3, or adenine nucleotide translocase levels. Conclusions: Lower rate of mitochondrial proton leak in muscle is a cell autonomous phenomenon in ODR vs ODS individuals, and this is associated with a more oxidized glutathione redox state in ODR vs ODS myotubes. The muscle of ODR subjects may thus have a lower capacity to adapt to oxidative stress as compared with ODS.

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