Exploring oxidative modifications of tyrosine: an update on mechanisms of formation, advances in analysis and biological consequences

C. Houée-Lévin, K. Bobrowski, L. Horakova, B. Karademir, C. Schöneich, M.J. Davies, C.M. Spickett

Research output: Contribution to journalArticle

Abstract

Protein oxidation is increasingly recognised as an important modulator of biochemical pathways controlling both physiological and pathological processes. While much attention has focused on cysteine modifications in reversible redox signalling, there is increasing evidence that other protein residues are oxidised in vivo with impact on cellular homeostasis and redox signalling pathways. A notable example is tyrosine, which can undergo a number of oxidative post-translational modifications to form 3-hydroxy-tyrosine, tyrosine crosslinks, 3-nitrotyrosine and halogenated tyrosine, with different effects on cellular functions. Tyrosine oxidation has been studied extensively in vitro, and this has generated detailed information about the molecular mechanisms that may occur in vivo. An important aspect of studying tyrosine oxidation both in vitro and in biological systems is the ability to monitor the formation of oxidised derivatives, which depends on a variety of analytical techniques. While antibody-dependent techniques such as ELISAs are commonly used, these have limitations, and more specific assays based on spectroscopic or spectrometric techniques are required to provide information on the exact residues modified and the nature of the modification. These approaches have helped understanding of the consequences of tyrosine oxidation in biological systems, especially its effects on cell signalling and cell dysfunction, linking to roles in disease. There is mounting evidence that tyrosine oxidation processes are important in vivo and can contribute to cellular pathology.

LanguageEnglish
Pages347-373
Number of pages27
JournalFree Radical Research
Volume49
Issue number4
Early online date27 Mar 2015
DOIs
Publication statusPublished - 2015

Fingerprint

Tyrosine
Oxidation
Biological systems
Oxidation-Reduction
Physiological Phenomena
Cell signaling
Pathologic Processes
Post Translational Protein Processing
Pathology
Cysteine
Mountings
Proteins
Modulators
Homeostasis
Enzyme-Linked Immunosorbent Assay
Assays
Derivatives
Antibodies

Bibliographical note

This is an Accepted Manuscript of an article published by Taylor & Francis in Free Radical Research on 27/3/15, available online: http://www.tandfonline.com/10.3109/10715762.2015.1007968

Funding: EPSRC (EP/I017887/1).

Keywords

  • antibody-dependent techniques
  • mass spectrometry
  • oxidising free radicals
  • Redox balance
  • time resolved techniques
  • tyrosine nitration
  • tyrosine oxidation

Cite this

Houée-Lévin, C. ; Bobrowski, K. ; Horakova, L. ; Karademir, B. ; Schöneich, C. ; Davies, M.J. ; Spickett, C.M. / Exploring oxidative modifications of tyrosine : an update on mechanisms of formation, advances in analysis and biological consequences. In: Free Radical Research. 2015 ; Vol. 49, No. 4. pp. 347-373.
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Exploring oxidative modifications of tyrosine : an update on mechanisms of formation, advances in analysis and biological consequences. / Houée-Lévin, C.; Bobrowski, K.; Horakova, L.; Karademir, B.; Schöneich, C.; Davies, M.J.; Spickett, C.M.

In: Free Radical Research, Vol. 49, No. 4, 2015, p. 347-373.

Research output: Contribution to journalArticle

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