Role of Protein -SH Groups in Redox Homeostasis— The Erythrocyte as a Model System

Simplicio, P. Di; Cacace, Marcello G.; Lusini, Lorenzo; Giannerini, Fabiola; Giustarini, Daniela; Rossi, Ranieri

doi:10.1006/abbi.1998.0694

Cited by 113 publications

(67 citation statements)

References 25 publications

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“…3,4) Thiol contains a sulfhydryl (-SH) group and plays a critical role in the prevention of oxidative stress in cells and its level can be altered during proliferation or apoptosis at the cellular level. 28,29) As primary targets of oxygen radicals, the -SH groups of sulfur containing amino acids such as cysteine and methionine in proteins are oxidized and return to reversible disulfide bonds. The structural and functional alterations in cell proteins begin after loss of these thiol groups.…”

Section: Discussionmentioning

confidence: 99%

The Role of Thiol/Disulphide Homeostasis in Anthracycline Associated Cardiac Toxicity

et al. 2017

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SummaryThe aim of the present study was to evaluate whether the baseline thiol/disulfide state can predict the occurrence of anthracycline induced cardiac toxicity. A total of 186 cancer patients receiving anthracycline (doxorubicin)-based chemotherapy were enrolled. All patients underwent 2-dimensional (2D) speckle tracking echocardiography (STE) to determine their left ventricular ejection fraction (LVEF) and blood samples for measuring thiol forms were obtained before treatment and 4 weeks after completion of the chemotherapy. The mean dose of doxorubicin exposure was 255 ± 39.2 mg/m 2 . Baseline native thiol was found to be lower whereas baseline disulfide and the disulfide/total thiol ratio were found to be higher in patients who had a decrease in LVEF after anthracycline therapy. Also, the amount of decrease in LVEF was well correlated with the delta value of the thiol forms. Logistic regression analysis revealed that changes in BNP and global longitudinal strain (GLS), baseline level of native thiol, disulfide, and the disulfide/total thiol ratio were strong predictors for a decrease in LVEF.The thiol/disulfide pathway may be a factor for predicting chemotherapy-induced cardiac toxicity as one of the oxidative stress mechanisms. (Int Heart J 2017; 58: 69-72)

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Section: Discussionmentioning

confidence: 99%

The Role of Thiol/Disulphide Homeostasis in Anthracycline Associated Cardiac Toxicity

et al. 2017

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“…Endogenous thiol levels can be altered as a result of oxidation by free oxygen radicals and can return to reversible disulphide bonds. 28,29 Although some studies have investigated thiol levels in depression, to our knowledge, no studies have extensively investigated dynamic thiol disulphide homeostasis, including not only thiol levels, but also disulphide levels, in women with major depression. In our study, plasma thiol/disulphide levels were determined by a novel method developed by Erel and Neşe-lioğlu.…”

Section: Anadolu Psikiyatri Derg 2018; 19(2):135-142mentioning

confidence: 99%

Dynamic thiol/disulphide homeostasis as a novel oxidative stress marker in women with major depressive disorder

Baykan¹,

Durmaz²,

Baykan³

et al. 2018

Anadolu Psikiyatri Derg

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“…Second, GSSG glutathionylates hemoglobin with a pseudofirst-order rate constant of Ϸ0.1 s Ϫ1 (with respect to GSSG) (31). In vivo, hemoglobin glutathionylation is probably substantially faster owing to catalysis by glutaredoxin (32).…”

Section: Requirement For Low Gssg Concentrations Is Capable Of Mediatmentioning

confidence: 99%

Evolution of enzymes in a series is driven by dissimilar functional demands

Salvador

Savageau

2006

Proc. Natl. Acad. Sci. U.S.A.

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That distinct enzyme activities in an unbranched metabolic pathway are evolutionarily tuned to a single functional requirement is a pervasive assumption. Here we test this assumption by examining the activities of two consecutively acting enzymes in human erythrocytes with an approach to quantitative evolutionary design that avoids the above-mentioned assumption. We previously found that avoidance of NADPH depletion during the pulses of oxidative load to which erythrocytes are normally exposed is the main functional requirement mediating selection for high glucose-6-phosphate dehydrogenase activity. In the present study, we find that, in contrast, the maintenance of oxidized glutathione at low concentrations is the main functional requirement mediating selection for high glutathione reductase activity. The results in this case show that, contrary to the assumption of a single functional requirement, natural selection for the normal activities of the distinct enzymes in the pathway is mediated by different requirements. On the other hand, the results agree with the more general principles that underlie our approach. Namely, that (i) the values of biochemical parameters evolve so as to fulfill the various performance requirements that are relevant to achieve high fitness, and (ii) these performance requirements can be inferred from quantitative systems theory considerations, informed by knowledge of specific aspects of the biochemistry, physiology, genetics, and ecology of the organism.human erythrocytes ͉ oxidative stress ͉ safety factors ͉ quantitative evolutionary design ͉ systems biology A lthough numerous mutations can drastically change the values of biochemical parameters such as enzyme activities, these values are often narrowly distributed in natural populations. This outcome owes largely to the interplay between constraints imposed by physicochemical laws and natural selection for good performance of the organism's biochemical circuits. The strength of natural selection in shaping the design of living organisms at the molecular level (1) is just beginning to be appreciated. In humans, natural selection is strong enough to almost prevent fixation of mutations that decrease fitness by Ͼ0.002%. Furthermore, Ͼ70% of the amino acid-changing mutations are selected against (2, 3). In the many organisms that have larger effective populations, even smaller fitness differentials can drive natural selection. Understanding the quantitative design for biochemical parameters that has been achieved through natural selection (i.e., the qualitative and quantitative functional requirements that mediate their evolutionary tuning) is a goal of systems biology with far-reaching implications. Such understanding would provide valuable insight regarding physiological as well as evolutionary adaptation (4, 5) and guidance for metabolic engineering (6). However, this type of understanding for parameters such as enzyme activities remains limited.The assumption that the distinct enzyme activities in a metabolic pathway are evolutio...

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Role of Protein -SH Groups in Redox Homeostasis— The Erythrocyte as a Model System

Cited by 113 publications

References 25 publications

The Role of Thiol/Disulphide Homeostasis in Anthracycline Associated Cardiac Toxicity

The Role of Thiol/Disulphide Homeostasis in Anthracycline Associated Cardiac Toxicity

Dynamic thiol/disulphide homeostasis as a novel oxidative stress marker in women with major depressive disorder

Evolution of enzymes in a series is driven by dissimilar functional demands

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