Mass spectrometric evidence for the existence of distinct modifications of different proteins by 2(E),4(E)-decadienal

Chem Res Toxicol. 2010 Mar 15;23(3):467-73. doi: 10.1021/tx900379a.

Abstract

2(E),4(E)-Decadienal (DDE), a lipid peroxidation product, was found to covalently modify Lys residues of different proteins by different reactions using mass spectrometry (MALDI-TOF-MS and LC-ESI-MS). DDE mainly formed Lys Schiff base adducts with cytochrome c and ribonuclease A at 10 min, but these reversibly formed adducts almost disappeared after 24 h. In contrast, beta-lactoglobulin (beta-LG) was highly modified by DDE after 24 h. In addition to the Lys Schiff base adducts, DDE formed novel Lys pyridinium adducts as well as Cys Michael adducts with beta-LG.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Aldehydes / adverse effects*
  • Amino Acid Sequence
  • Cytochromes c / analysis
  • Cytochromes c / metabolism
  • Lactoglobulins / analysis
  • Lactoglobulins / metabolism
  • Mass Spectrometry*
  • Molecular Sequence Data
  • Proteins / analysis
  • Proteins / metabolism*
  • Ribonuclease, Pancreatic / analysis
  • Ribonuclease, Pancreatic / metabolism
  • Spectrometry, Mass, Electrospray Ionization
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

Substances

  • Aldehydes
  • Lactoglobulins
  • Proteins
  • 2,4-decadienal
  • Cytochromes c
  • Ribonuclease, Pancreatic