Oxidative modification of serum proteins in multiple sclerosis

Neurochem Int. 2013 Nov;63(5):507-16. doi: 10.1016/j.neuint.2013.08.009. Epub 2013 Sep 12.

Abstract

Multiple sclerosis (MS) has been demonstrated to involve oxidative stress and augmented glycoxidation. In this study, several markers of protein oxidative damage and glycoxidation have been compared in 14 relapsing remittent in MS (RRMS) patients without immunomodifying treatment, 10 patients in clinical relapse, and clinically stable patient groups treated with interferon β 1a (18) , β 1b (19) and glatiramer acetate (GA; 6) in relation to healthy subjects (12). The glycophore content was increased in RRSM patients without treatment and in patients treated with GA. The level of advanced protein oxidation products (AOPP) was increased in RRSM patients without treatment and in patients with clinical relapse. The level of protein carbonyls was elevated in RRSM patients without treatment and in patients treated with interferon β 1b. The levels of dityrosine level and N'-formylkynureine were elevated in RRSM patients without treatment while serum protein thiol groups were decreased in RRSM patients in clinical relapse as well as RRMS patients treated with interferon β 1a. Several markers of protein modification showed correlation with the C-reactive protein level and white blood cell count, suggesting that oxidative protein modifications are linked to the inflammatory processes in MS. Results of this study confirm the occurrence of protein oxidative and glycoxidative damage in MS and show that spectrophotometric and fluorimetric markers of this damage, especially the AOPP level, may be useful in monitoring oxidative stress in the course of therapy of MS.

Keywords: AOPP; Glycoxidation; Inflammation; Multiple sclerosis; Oxidative stress; Protein oxidation.

MeSH terms

  • Adult
  • Blood Proteins / metabolism*
  • Female
  • Humans
  • Male
  • Middle Aged
  • Multiple Sclerosis / blood*
  • Oxidation-Reduction

Substances

  • Blood Proteins