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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...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2012
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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. |
format | Online Article Text |
id | pubmed-6268088 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
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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