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Oxidative stress, an imbalance toward the pro-oxidant side of the pro-oxidant/antioxidant homeostasis, occurs in several human diseases. Among these diseases are those in which high levels of protein carbonyl (CO) groups have been observed, including Alzheimer's disease (AD), rheumatoid arthritis, diabetes, sepsis, chronic renal failure, and respiratory(More)
Oxidative/nitrosative stress, a pervasive condition of increased amounts of reactive oxygen/nitrogen species, is now recognized to be a prominent feature of many acute and chronic diseases and even of the normal aging process. However, definitive evidence for this association has often been lacking because of recognized shortcomings with biomarkers and/or(More)
Oxidative modifications of enzymes and structural proteins play a significant role in the aetiology and/or progression of several human diseases. Protein carbonyl content is the most general and well-used biomarker of severe oxidative protein damage. Human diseases associated with protein carbonylation include Alzheimer's disease, chronic lung disease,(More)
Protein S-glutathionylation, the reversible formation of mixed disulfides between glutathione and low-pKa cysteinyl residues, not only is a cellular response to mild oxidative/nitrosative stress, but also occurs under basal (physiological) conditions. S-glutathionylation has now emerged as a potential mechanism for dynamic, posttranslational regulation of a(More)
Actin is the major constituent of the cytoskeleton of almost all the eukaryotic cells. In vitro experiments have indicated that oxidant-stressed nonmuscle mammalian cells undergo remarkable changes in their morphology and in the structure of the actin cytoskeleton, often resulting in plasma membrane blebbing. Although the microfilament network is one of the(More)
Haemoglobins bearing reactive sulfhydryl groups have been shown to be able to interplay with glutathione in some detoxification processes. Blood from different mouse strains commonly used as experimental animal models, i.e., C57, DBA and ICR, was treated with oxidants with the aim of evaluating: (i) the involvement of protein SH groups in oxido-reductive(More)
S-Glutathionylation is the specific post-translational modification of protein cysteine residues by the addition of the tripeptide glutathione, the most abundant and important low-molecular-mass thiol within most cell types. Protein S-glutathionylation is promoted by oxidative or nitrosative stress but also occurs in unstressed cells. It can serve to(More)
Many proteins, including actin, are targets for S-glutathionylation, the reversible formation of mixed disulphides between protein cysteinyl thiol groups and glutathione (GSH) that can be induced in cells by oxidative stress. Proposed mechanisms of protein S-glutathionylation follow mainly two distinct pathways. One route involves the initial oxidative(More)
Plasma low molecular mass thiols are represented by glutathione, cysteine, cysteinylglycine and homocysteine. The physiological mechanisms responsible for maintaining the homeostasis of these compounds in the intracellular and extracellular spaces have not been fully clarified. Erythrocytes possess the enzymatic machinery to synthesize glutathione and an(More)
The measurement of glutathione is a challenging task in that, during sample manipulation, a large percentage of this compound can be artificially oxidized. Here a high-performance liquid chromatography (HPLC) method to measure reduced glutathione in blood, based on the analysis of its conjugate with N-ethylmaleimide, has been developed and validated. The(More)