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Targeted mass spectrometry methods for detecting oxidative post-translational modifications.

Karina Tveen-Jensen1, Ana Reis2, Corinne M Spickett2

  • 1Aston University (Birmingham), Life and Health Sciences, United Kingdom..

Free Radical Biology & Medicine
|October 14, 2015
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Summary

A new mass spectrometry method accurately detects multiple oxidative protein modifications (oxPTMs) and oxidized lipids in human samples. This approach improves identification accuracy and reveals potential biomarkers for oxidative damage in aging and disease.

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Area of Science:

  • Biochemistry
  • Analytical Chemistry
  • Proteomics

Background:

  • Oxidative post-translational modifications (oxPTMs) regulate cellular behavior but are challenging to detect.
  • Traditional mass spectrometry (MS) database searching often fails to identify unexpected or multiple modifications.
  • Accurate detection of oxPTMs is crucial for understanding redox regulation and disease pathogenesis.

Purpose of the Study:

  • To develop and validate a novel data mining approach for accurate mass spectrometry instruments.
  • To enable the detection of multiple and unspecified oxidative modifications on proteins.
  • To identify novel oxidized lipid adducts and assess their potential as disease biomarkers.

Main Methods:

  • Generation of accurate mass extracted ion chromatograms (XIC) for specific reporter ions from LC-MS/MS data.
  • Utilized a high-resolution mass spectrometer (ABSciex 5600 Triple TOF) for data acquisition.
  • Tested the method on human plasma and LDL proteins, confirming findings with manual sequencing.

Main Results:

  • Successfully detected various oxPTMs (e.g., chlorotyrosine, nitrotyrosine, kynurenine) and oxidized phospholipid adducts.
  • Identified intact oxidized phosphatidylcholine adducts on LDL using a phosphocholine reporter ion (184.074Da/e).
  • Detected ApoB-100 with oxidized lipid adducts in healthy individuals and patients with chronic kidney disease.
  • The XIC method demonstrated a lower false positive rate and identified more modified peptides than standard database searching.
  • Enabled post-data collection searching for additional modifications and identification of multiple modifications on single peptides.

Conclusions:

  • The accurate mass XIC method is a powerful tool for sensitive and specific detection of oxPTMs and oxidized lipids.
  • Oxidized lipid adducts on ApoB-100 and oxPTMs on albumin are potential biomarkers for oxidative damage in aging and inflammatory diseases.
  • This approach overcomes limitations of traditional database searching, enhancing proteomic analysis of oxidative modifications.