Mass spectrometric determination of early and advanced glycation in biology

Naila Rabbani, Amal Ashour, Paul J Thornalley, Naila Rabbani, Amal Ashour, Paul J Thornalley

Abstract

Protein glycation in biological systems occurs predominantly on lysine, arginine and N-terminal residues of proteins. Major quantitative glycation adducts are found at mean extents of modification of 1-5 mol percent of proteins. These are glucose-derived fructosamine on lysine and N-terminal residues of proteins, methylglyoxal-derived hydroimidazolone on arginine residues and N(ε)-carboxymethyl-lysine residues mainly formed by the oxidative degradation of fructosamine. Total glycation adducts of different types are quantified by stable isotopic dilution analysis liquid chromatography-tandem mass spectrometry (LC-MS/MS) in multiple reaction monitoring mode. Metabolism of glycated proteins is followed by LC-MS/MS of glycation free adducts as minor components of the amino acid metabolome. Glycated proteins and sites of modification within them - amino acid residues modified by the glycating agent moiety - are identified and quantified by label-free and stable isotope labelling with amino acids in cell culture (SILAC) high resolution mass spectrometry. Sites of glycation by glucose and methylglyoxal in selected proteins are listed. Key issues in applying proteomics techniques to analysis of glycated proteins are: (i) avoiding compromise of analysis by formation, loss and relocation of glycation adducts in pre-analytic processing; (ii) specificity of immunoaffinity enrichment procedures, (iii) maximizing protein sequence coverage in mass spectrometric analysis for detection of glycation sites, and (iv) development of bioinformatics tools for prediction of protein glycation sites. Protein glycation studies have important applications in biology, ageing and translational medicine - particularly on studies of obesity, diabetes, cardiovascular disease, renal failure, neurological disorders and cancer. Mass spectrometric analysis of glycated proteins has yet to find widespread use clinically. Future use in health screening, disease diagnosis and therapeutic monitoring, and drug and functional food development is expected. A protocol for high resolution mass spectrometry proteomics of glycated proteins is given.

Keywords: Bioinformatics; Glucose; Glycation; Hydroimidazolone; Mass spectrometry; Methylglyoxal, fructosamine; Orbitrap; Proteomics.

Figures

Fig. 1
Fig. 1
Major protein glycation processes in physiological systems. (a) Early glycation. Formation of the Schiff’s base and fructosamine (Amadori product) of lysine residues. (b) Oxidative degradation of fructosyl-lysine to Nε-carboxymethyl-lysine (CML). Similar processes occur on N-terminal amino acid residues. (c) Glycation of arginine residues by methylglyoxal with formation of dihydroxyimidazolidine and hydroimidazolone MG-H1 residues. There are related structural isomers and similar adducts formed from glyoxal and 3-deoxyglucosone [, –5]
Fig. 2
Fig. 2
Activation of arginine residues in alpha-helix domains of proteins by neighbouring group interactions with basic and acidic amino acid residues. Figure reproduced with permission from [5]
Fig. 3
Fig. 3
Fragmentation of fructosamine and hydroimidazolone glycation adducts. (a) Fragmentation of fructosyl-lysine by CID leading to formation of oxonium, pyrylium, furylium and immonium ions. (b) and (c) fragmentation of hydroimidazolones formed by methylglyoxal and glyoxal to immonium ions in CID and HCD [, –99]

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