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Investigation of Non-Enzymatic Glycosylation of Human Serum Albumin Using Ion Trap-Time of Flight Mass Spectrometry

Non-enzymatic glycosylation or glycation involves covalent attachment of reducing sugar residues to proteins without enzyme participation. Glycation of glucose to human serum albumin in vivo is related to diabetes and many other diseases. We present an approach using liquid chromatography coupled to...

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Detalles Bibliográficos
Autores principales: Bai, Xue, Wang, Zhangjie, Huang, Chengcai, Wang, Zhe, Chi, Lianli
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6268088/
https://www.ncbi.nlm.nih.gov/pubmed/22832880
http://dx.doi.org/10.3390/molecules17088782
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author Bai, Xue
Wang, Zhangjie
Huang, Chengcai
Wang, Zhe
Chi, Lianli
author_facet Bai, Xue
Wang, Zhangjie
Huang, Chengcai
Wang, Zhe
Chi, Lianli
author_sort Bai, Xue
collection PubMed
description Non-enzymatic glycosylation or glycation involves covalent attachment of reducing sugar residues to proteins without enzyme participation. Glycation of glucose to human serum albumin in vivo is related to diabetes and many other diseases. We present an approach using liquid chromatography coupled to an electrospray ionization source of a hybrid ion trap-time of flight (IT-TOF-MS/MS) tandem mass spectrometer to identify the glycation sites on serum albumin from both a healthy person and a diabetic patient. The MetID software, which is commonly used for screening metabolites, is adapted for peptide fingerprinting based on both m/z values and isotopic distribution profiles. A total of 21 glycation sites from the healthy person and 16 glycation sites from the diabetic patient were identified successfully. We also demonstrate the use of matrix assisted laser desorption ionization-time of flight mass spectrometry to estimate the incorporation ratio of glucose to albumin during glycation. Results from this study show that the glycation in healthy person is more complicated than previously thought. Further analysis of incorporation ratio distribution may be necessary to accurately reflect the change of serum albumin glycation in diabetic patients.
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spelling pubmed-62680882018-12-12 Investigation of Non-Enzymatic Glycosylation of Human Serum Albumin Using Ion Trap-Time of Flight Mass Spectrometry Bai, Xue Wang, Zhangjie Huang, Chengcai Wang, Zhe Chi, Lianli Molecules Article Non-enzymatic glycosylation or glycation involves covalent attachment of reducing sugar residues to proteins without enzyme participation. Glycation of glucose to human serum albumin in vivo is related to diabetes and many other diseases. We present an approach using liquid chromatography coupled to an electrospray ionization source of a hybrid ion trap-time of flight (IT-TOF-MS/MS) tandem mass spectrometer to identify the glycation sites on serum albumin from both a healthy person and a diabetic patient. The MetID software, which is commonly used for screening metabolites, is adapted for peptide fingerprinting based on both m/z values and isotopic distribution profiles. A total of 21 glycation sites from the healthy person and 16 glycation sites from the diabetic patient were identified successfully. We also demonstrate the use of matrix assisted laser desorption ionization-time of flight mass spectrometry to estimate the incorporation ratio of glucose to albumin during glycation. Results from this study show that the glycation in healthy person is more complicated than previously thought. Further analysis of incorporation ratio distribution may be necessary to accurately reflect the change of serum albumin glycation in diabetic patients. MDPI 2012-07-25 /pmc/articles/PMC6268088/ /pubmed/22832880 http://dx.doi.org/10.3390/molecules17088782 Text en © 2012 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).
spellingShingle Article
Bai, Xue
Wang, Zhangjie
Huang, Chengcai
Wang, Zhe
Chi, Lianli
Investigation of Non-Enzymatic Glycosylation of Human Serum Albumin Using Ion Trap-Time of Flight Mass Spectrometry
title Investigation of Non-Enzymatic Glycosylation of Human Serum Albumin Using Ion Trap-Time of Flight Mass Spectrometry
title_full Investigation of Non-Enzymatic Glycosylation of Human Serum Albumin Using Ion Trap-Time of Flight Mass Spectrometry
title_fullStr Investigation of Non-Enzymatic Glycosylation of Human Serum Albumin Using Ion Trap-Time of Flight Mass Spectrometry
title_full_unstemmed Investigation of Non-Enzymatic Glycosylation of Human Serum Albumin Using Ion Trap-Time of Flight Mass Spectrometry
title_short Investigation of Non-Enzymatic Glycosylation of Human Serum Albumin Using Ion Trap-Time of Flight Mass Spectrometry
title_sort investigation of non-enzymatic glycosylation of human serum albumin using ion trap-time of flight mass spectrometry
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6268088/
https://www.ncbi.nlm.nih.gov/pubmed/22832880
http://dx.doi.org/10.3390/molecules17088782
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