Mass Spectrometry-Based Methods for Identifying Oxidized Proteins in Disease: Advances and Challenges

Biomolecules

Ivan Verrastro²  Sabah Pasha²  Karina Tveen Jensen²  Andrew R. Pitt²  Corinne M. Spickett¹  Michael Breitenbach² 

[1] School of Life and Health Sciences, Aston University, Aston Triangle, Birmingham, B4 7ET, UK;

关键词: oxidative post-translational modification;    inflammation;    cardiovascular disease;    protein carbonyls;    nitrotyrosine;    chlorotyrosine;    LC-MS/MS;    precursor ion scanning;    neutral loss scanning;    multiple reaction monitoring;   

DOI  :  10.3390/biom5020378

来源: mdpi

【 摘 要 】

Many inflammatory diseases have an oxidative aetiology, which leads to oxidative damage to biomolecules, including proteins. It is now increasingly recognized that oxidative post-translational modifications (oxPTMs) of proteins affect cell signalling and behaviour, and can contribute to pathology. Moreover, oxidized proteins have potential as biomarkers for inflammatory diseases. Although many assays for generic protein oxidation and breakdown products of protein oxidation are available, only advanced tandem mass spectrometry approaches have the power to localize specific oxPTMs in identified proteins. While much work has been carried out using untargeted or discovery mass spectrometry approaches, identification of oxPTMs in disease has benefitted from the development of sophisticated targeted or semi-targeted scanning routines, combined with chemical labeling and enrichment approaches. Nevertheless, many potential pitfalls exist which can result in incorrect identifications. This review explains the limitations, advantages and challenges of all of these approaches to detecting oxidatively modified proteins, and provides an update on recent literature in which they have been used to detect and quantify protein oxidation in disease.

【 授权许可】

CC BY   
© 2015 by the authors; licensee MDPI, Basel, Switzerland.