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Rabbani, Naila and Thornalley, Paul J. (2016) Glycation of proteins. In: Griffiths, J. R. and Unwin, R. D. , (eds.) Analysis of Protein Post-Translational Modifications by Mass Spectrometry. Hoboken, NJ, USA: John Wiley & Sons, Inc., , pp. 307-332. ISBN 9781119045854
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Official URL: http://dx.doi.org/10.1002/9781119250906.ch8
Abstract
Protein glycation occurs predominantly on lysine, arginine, and N-terminal residues of proteins and usually at mean extents of 1–5% of protein sites.
Glycation adducts are predominantly glucose-derived fructosamine on lysine and N-terminal residues of proteins, methylglyoxal-derived hydroimidazolone on arginine residues, and N ε-carboxymethyl-lysine residues mainly derived from fructosamine oxidation.
Total glycation adducts of different types are quantified by stable isotopic dilution analysis liquid chromatography–tandem mass spectrometry (LC-MS/MS) multiple reaction monitoring (MRM).
Metabolism of glycated proteins is followed by LC-MS/MS of glycation-free adducts as minor components of the amino acid metabolome in plasma and urine.
Glycated proteins and sites of modification within them are identified and quantified by label-free and isotope-coded affinity tag (ICAT) high-resolution mass spectrometry.
Outstanding challenges are (i) avoiding compromise of analysis by formation, loss, and relocation of glycation adducts in preanalytic processing; (ii) limited 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 the prediction of protein glycation sites.
Protein glycation studies have important applications in clinical translation – particularly on studies of aging, obesity, diabetes, cardiovascular disease, renal failure, neurological disorders, and cancer. Future use in health screening, disease diagnosis and therapeutic monitoring, and drug and functional food development is expected.
| Item Type: | Book Item | ||||
|---|---|---|---|---|---|
| Divisions: | Faculty of Science, Engineering and Medicine > Research Centres > Warwick Systems Biology Centre Faculty of Science, Engineering and Medicine > Medicine > Warwick Medical School |
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| Publisher: | John Wiley & Sons, Inc., | ||||
| Place of Publication: | Hoboken, NJ, USA | ||||
| ISBN: | 9781119045854 | ||||
| Book Title: | Analysis of Protein Post-Translational Modifications by Mass Spectrometry | ||||
| Editor: | Griffiths, J. R. and Unwin, R. D. | ||||
| Official Date: | 18 October 2016 | ||||
| Dates: |
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| Page Range: | pp. 307-332 | ||||
| DOI: | 10.1002/9781119250906.ch8 | ||||
| Status: | Peer Reviewed | ||||
| Publication Status: | Published | ||||
| Access rights to Published version: | Restricted or Subscription Access | ||||
| Adapted As: | Rabbani, N. and Thornalley, P. J. (2016) Glycation of Proteins, in Analysis of Protein Post-Translational Modifications by Mass Spectrometry (eds J. R. Griffiths and R. D. Unwin), John Wiley & Sons, Inc., Hoboken, NJ, USA. doi: 10.1002/9781119250906.ch8 |
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