Journal
MASS SPECTROMETRY REVIEWS
Volume 24, Issue 1, Pages 55-99Publisher
WILEY
DOI: 10.1002/mas.20006
Keywords
biological markers; mass spectrometry; methionine sulfoxide; nitrosothiols; nitrotyrosine; protein carbonylation; protein oxidation; proteomics; reactive nitrogen species; reactive oxygen species; S-glutathionylation; S-nitrosation
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Reactive oxygen species (ROS) and reactive nitrogen species (RNS) contribute to the pathogenesis and/or progression of several human diseases. Proteins are important molecular signposts of oxidative/nitrosative damage. However, it is generally unresolved whether the presence of oxidatively/nitrosatively modified proteins has a causal role or simply reflects secondary epiphenomena. Only direct identification and characterization of the modified protein(s) in a given pathophysiological condition can decipher the potential roles played by ROS/RNS-induced protein modifications. During the last few years, mass spectrometry (MS)-based technologies have contributed in a significant way to foster a better understanding of disease processes. The study of oxidative/nitrosative modifications, investigated by redox proteomics, is contributing to establish a relationship between pathological hallmarks of disease and protein structural and functional abnormalities. MS-based technologies promise a contribution in a new era of molecular medicine, especially in the discovery of diagnostic biomarkers of oxidative/nitrosative stress, enabling early detection of diseases. Indeed, identification and characterization of oxidatively/nitrosatively modified proteins in human diseases has just begun. (C) 2004 Wiley Periodicals, Inc.
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