Tyrosine nitration: Localisation,quantification, consequences for protein function and signal transduction |
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| Authors: | Stan A.B. Greenacre Harry Ischiropoulos |
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| Affiliation: | 1. Centre for Cardiovascular Biology and Medicine and Wolfson Centre for Age-related Disease, King's College London, New Hunt's House, Guy's Campus, London, SE1 1UL, UK;2. The Joseph Stokes Jr. Research Institute and Departments of Paediatrics, Biochemistry, and Biophysics, Children's Hospital of Philadelphia, Philadelphia, Pennsylvania, 19104, USA;3. University of Pennsylvania, School of Medicine, Philadelphia, Pennsylvania, 19104, USA |
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| Abstract: | The nitration of free tyrosine or protein tyrosine residues generates 3-nitrotyrosine the detection of which has been utilised as a footprint for the in vivo formation of peroxynitrite and other reactive nitrogen species. The detection of 3-nitrotyrosine by analytical and immunological techniques has established that tyrosine nitration occurs under physiological conditions and levels increase in most disease states. This review provides an updated, comprehensive and detailed summary of the tissue, cellular and specific protein localisation of 3-nitrotyrosine and its quantification. The potential consequences of nitration to protein function and the pathogenesis of disease are also examined together with the possible effects of protein nitration on signal transduction pathways and on the metabolism of proteins. |
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| Keywords: | 3-nitrotyrosine protein nitration peroxynitrite reactive nitrogen species |
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