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Protein oxidation : role in signalling and detection by mass spectrometry

Spickett, C. M. and Pitt, Andrew. R. (2012) Protein oxidation : role in signalling and detection by mass spectrometry. Amino Acids, 42 (1). pp. 5-21. ISSN 0939-4451

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Abstract

Proteins can undergo a wide variety of oxidative post-translational modifications (oxPTM); while reversible modifications are thought to be relevant in physiological processes, non-reversible oxPTM may contribute to pathological situations and disease. The oxidant is also important in determining the type of oxPTM, such as oxidation, chlorination or nitration. The best characterized oxPTMs involved in signalling modulation are partial oxidations of cysteine to disulfide, glutathionylated or sulfenic acid forms that can be reversed by thiol reductants. Proline hydroxylation in HIF signalling is also quite well characterized, and there is increasing evidence that specific oxidations of methionine and tyrosine may have some biological roles. For some proteins regulated by cysteine oxidation, the residues and molecular mechanism involved have been extensively studied and are well understood, such as the protein tyrosine phosphatase PTP1B and MAP3 kinase ASK1, as well as transcription factor complex Keap1-Nrf2. The advances in understanding of the role oxPTMs in signalling have been facilitated by advances in analytical technology, in particular tandem mass spectrometry techniques. Combinations of peptide sequencing by collisionally induced dissociation and precursor ion scanning or neutral loss to select for specific oxPTMs have proved very useful for identifying oxidatively modified proteins and mapping the sites of oxidation. The development of specific labelling and enrichment procedures for S-nitrosylation or disulfide formation has proved invaluable, and there is ongoing work to establish analogous methods for detection of nitrotyrosine and other modifications.

Item type: Article
ID code: 40172
Keywords: s-nitrosylation sites, calmodulin-dependent activation, i-kappa-b, cysteine-sulfinic acid, cysteine oxidation, tyrosine-phosphatase 1b, nitrotyrosine, precursor ion scanning, oxidative stress, redox signalling, coden affini, collision-induced dissociation, Pharmacy and materia medica, Biochemistry, Organic Chemistry, Clinical Biochemistry
Subjects: Medicine > Pharmacy and materia medica
Department: Faculty of Science > Strathclyde Institute of Pharmacy and Biomedical Sciences
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Depositing user: Pure Administrator
Date Deposited: 22 Jun 2012 11:54
Last modified: 17 Oct 2014 05:10
URI: http://strathprints.strath.ac.uk/id/eprint/40172

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