Tyrosine oxidation products

Analysis and biological relevance

Cecilia R Giulivi, N. J. Traaseth, K. J A Davies

Research output: Contribution to journalArticle

141 Citations (Scopus)

Abstract

Dityrosine is found in several proteins as a product of UV irradiation, γ-irradiation, aging, exposure to oxygen free radicals, nitrogen dioxide, peroxynitrite, and lipid hydroperoxides. Interest of dityrosine in proteins is based on its potential as a specific marker for oxidatively damaged proteins and their selective proteolysis, hence it could be used as a marker for oxidative stress. Dityrosine is also the product of normal post-translational processes affecting specific structural proteins. Since post-translational modification of a given amino acid in a protein is equivalent to the substitution of that residue by an analogue, it has been proposed that the covalent modification of amino acids may serve as a "marking" step for protein degradation.

Original languageEnglish (US)
Pages (from-to)227-232
Number of pages6
JournalAmino Acids
Volume25
Issue number3-4
DOIs
StatePublished - Dec 2003
Externally publishedYes

Fingerprint

Tyrosine
Oxidation
Proteins
Proteolysis
Amino Acids
Nitrogen Dioxide
Peroxynitrous Acid
Irradiation
Lipid Peroxides
Post Translational Protein Processing
Oxidative stress
Free Radicals
Reactive Oxygen Species
Oxidative Stress
Substitution reactions
Aging of materials
Oxygen
Degradation
dityrosine

Keywords

  • Dityrosine
  • Oxidative stress
  • Oxygen free radicals
  • Protein damage
  • Proteolysis

ASJC Scopus subject areas

  • Clinical Biochemistry
  • Biochemistry
  • Endocrinology

Cite this

Tyrosine oxidation products : Analysis and biological relevance. / Giulivi, Cecilia R; Traaseth, N. J.; Davies, K. J A.

In: Amino Acids, Vol. 25, No. 3-4, 12.2003, p. 227-232.

Research output: Contribution to journalArticle

Giulivi, Cecilia R ; Traaseth, N. J. ; Davies, K. J A. / Tyrosine oxidation products : Analysis and biological relevance. In: Amino Acids. 2003 ; Vol. 25, No. 3-4. pp. 227-232.
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