Protein Glycation in Diabetes as Determined by Mass Spectrometry
Diabetes is a common endocrine disorder characterized by hyperglycemia leading to nonenzymatic glycation of proteins, responsible for chronic complications. The development of mass spectrometric techniques able to give highly specific and reliable results in proteome field is of wide interest for ph...
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| Format: | Article |
| Language: | English |
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Wiley
2013-01-01
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| Series: | International Journal of Endocrinology |
| Online Access: | http://dx.doi.org/10.1155/2013/412103 |
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| author | Annunziata Lapolla Laura Molin Pietro Traldi |
| author_facet | Annunziata Lapolla Laura Molin Pietro Traldi |
| author_sort | Annunziata Lapolla |
| collection | DOAJ |
| description | Diabetes is a common endocrine disorder characterized by hyperglycemia leading to nonenzymatic glycation of proteins, responsible for chronic complications. The development of mass spectrometric techniques able to give highly specific and reliable results in proteome field is of wide interest for physicians, giving them new tools to monitor the disease progression and the possible complications related to diabetes, as well as the effectiveness of therapeutic treatments. This paper reports and discusses some of the data pertaining protein glycation in diabetic subjects obtained by matrix-assisted laser desorption ionization (MALDI) mass spectrometry (MS). The preliminary studies carried out by in vitro protein glycation experiments show clear differences in molecular weight of glycated and unglycated proteins. Then, the attention was focused on plasma proteins human serum albumin (HSA) and immunoglobulin G (IgG). Enzymatic degradation products of in vitro glycated HSA were studied in order to simulate the in vivo enzymatic digestion of glycated species by the immunological system leading to the highly reactive advanced glycation end-products (AGEs) peptides. Further studies led to the evaluation of glycated Apo A-I and glycated haemoglobin levels. A different MALDI approach was employed for the identification of markers of disease in urine samples of healthy, diabetic, nephropathic, and diabetic-nephropathic subjects. |
| format | Article |
| id | doaj-art-4ae8905a8b0d4b119b1709a2f948533e |
| institution | Kabale University |
| issn | 1687-8337 1687-8345 |
| language | English |
| publishDate | 2013-01-01 |
| publisher | Wiley |
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| series | International Journal of Endocrinology |
| spelling | doaj-art-4ae8905a8b0d4b119b1709a2f948533e2025-02-03T05:59:19ZengWileyInternational Journal of Endocrinology1687-83371687-83452013-01-01201310.1155/2013/412103412103Protein Glycation in Diabetes as Determined by Mass SpectrometryAnnunziata Lapolla0Laura Molin1Pietro Traldi2Department of Medicine, Padova University, Via Giustiniani 2, I35100 Padova, ItalyNational Council of Researches, Institute of Molecular Sciences and Technologies, Corso Stati Uniti 4, I35127 Padova, ItalyNational Council of Researches, Institute of Molecular Sciences and Technologies, Corso Stati Uniti 4, I35127 Padova, ItalyDiabetes is a common endocrine disorder characterized by hyperglycemia leading to nonenzymatic glycation of proteins, responsible for chronic complications. The development of mass spectrometric techniques able to give highly specific and reliable results in proteome field is of wide interest for physicians, giving them new tools to monitor the disease progression and the possible complications related to diabetes, as well as the effectiveness of therapeutic treatments. This paper reports and discusses some of the data pertaining protein glycation in diabetic subjects obtained by matrix-assisted laser desorption ionization (MALDI) mass spectrometry (MS). The preliminary studies carried out by in vitro protein glycation experiments show clear differences in molecular weight of glycated and unglycated proteins. Then, the attention was focused on plasma proteins human serum albumin (HSA) and immunoglobulin G (IgG). Enzymatic degradation products of in vitro glycated HSA were studied in order to simulate the in vivo enzymatic digestion of glycated species by the immunological system leading to the highly reactive advanced glycation end-products (AGEs) peptides. Further studies led to the evaluation of glycated Apo A-I and glycated haemoglobin levels. A different MALDI approach was employed for the identification of markers of disease in urine samples of healthy, diabetic, nephropathic, and diabetic-nephropathic subjects.http://dx.doi.org/10.1155/2013/412103 |
| spellingShingle | Annunziata Lapolla Laura Molin Pietro Traldi Protein Glycation in Diabetes as Determined by Mass Spectrometry International Journal of Endocrinology |
| title | Protein Glycation in Diabetes as Determined by Mass Spectrometry |
| title_full | Protein Glycation in Diabetes as Determined by Mass Spectrometry |
| title_fullStr | Protein Glycation in Diabetes as Determined by Mass Spectrometry |
| title_full_unstemmed | Protein Glycation in Diabetes as Determined by Mass Spectrometry |
| title_short | Protein Glycation in Diabetes as Determined by Mass Spectrometry |
| title_sort | protein glycation in diabetes as determined by mass spectrometry |
| url | http://dx.doi.org/10.1155/2013/412103 |
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