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Journal ArticleDOI

S-Thiolation of human endothelial cell glyceraldehyde-3-phosphate dehydrogenase after hydrogen peroxide treatment

TLDR
It is shown that the post-translational modification of the cysteinyl thiols of glyceraldehyde-3-phosphate dehydrogenase accompanies an inhibition of the enzyme and that both events are simultaneously and rapidly reversed upon the removal of the oxidative stimulus.
Abstract
Exposure of human umbilical vein endothelial cells to oxidants such as hydrogen peroxide, tertbutyl hydroperoxide and diamide has been shown to induce oxidant-specific S-thiolation of cellular proteins. In this study one of the main S-thiolated proteins in hydrogen-peroxide-treated cells was identified as the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase. Additionally, we have shown that the post-translational modification of the cysteinyl thiols of glyceraldehyde-3-phosphate dehydrogenase accompanies an inhibition of the enzyme and that both events are simultaneously and rapidly reversed upon the removal of the oxidative stimulus.

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Citations
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Journal ArticleDOI

Analysis of glutathione: implication in redox and detoxification.

TL;DR: The present review proposes an analysis of the current knowledge about the methodologies for measuring glutathione in human biological samples and their feasibility as routine methods in clinical chemistry, and elucidates the fundamental role of glutATHione in pathophysiological conditions and its implication in redox and detoxification process.
Journal ArticleDOI

Redox regulation of nf-kappa b activation

TL;DR: Upstream kinase(s) and or phosphatase(S) prone to thiolation or oxidation of vicinal SH groups are at present considered the best candidates mediating the redox regulation of NF-kappaB.
Journal ArticleDOI

New insights into an old protein: the functional diversity of mammalian glyceraldehyde-3-phosphate dehydrogenase.

TL;DR: The mechanisms through which mammalian cells may utilize GAPDH amino acid sequences to provide new functions and to determine its intracellular localization are considered and the interrelationship between new GAPDh activities and its role in cell pathologies is addressed.
Journal ArticleDOI

Regulation of protein function by S-glutathiolation in response to oxidative and nitrosative stress.

TL;DR: A review of recent work supporting a role for S-glutathiolation in stress signalling pathways and in the adaptive cellular response to oxidative and nitrosative stress and the molecular mechanisms of protein regulation by oxidative andNitrosative thiol-group modifications are outlined.
Journal ArticleDOI

The diverse functions of GAPDH: views from different subcellular compartments

TL;DR: These multifunctional properties of GAPDH are reviewed, especially linking them to its oligomerization, posttranslational modification, and subcellular localization, and mechanistic descriptions of how S-nitrosylation ofGAPDH under oxidative stress may lead to cell death/dysfunction via nuclear translocation of GAPS, which is counteracted by a cytosolic GOSPEL.
References
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Journal ArticleDOI

Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.

TL;DR: A method has been devised for the electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets that results in quantitative transfer of ribosomal proteins from gels containing urea.
Book

Antibodies: A Laboratory Manual

Ed Harlow, +1 more
TL;DR: A second edition of Antibodies: A Laboratory Manual is being published in September 2013, Revised, extended and updated by Edward Greenfield of the Dana-Farber Cancer Center, the material has been recast with extensive new information and new chapters have been added.
Journal ArticleDOI

A simplification of the protein assay method of Lowry et al. which is more generally applicable

TL;DR: A simple method based on a linear log-log protein standard curve is presented to permit rapid and totally objective protein analysis using small programmable calculators.
Journal ArticleDOI

Mechanisms of oxidant-mediated cell injury. The glycolytic and mitochondrial pathways of ADP phosphorylation are major intracellular targets inactivated by hydrogen peroxide.

TL;DR: Both the estimated rates of ADP phosphorylation by glycolysis and mitochondria and the estimated rate of ATP hydrolysis by ongoing metabolism were utilized to model the approximate decline in intracellular ATP expected at 15-min exposure to various H2O2 concentrations.
Journal ArticleDOI

Methodologies for the application of monobromobimane to the simultaneous analysis of soluble and protein thiol components of biological systems

TL;DR: In this article, a series of simple methodologies for the determination of the redox status of low molecular weight and protein thiols in biological systems is described, based centrally upon the use of monobromobimane.
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