Plasma Proteins Modified by Advanced Glycation End Products (AGEs) Reveal Site-specific Susceptibilities to Glycemic Control in Patients with Type 2 Diabetes
| Autor: | Uta Greifenhagen, Matthias Blüher, Ralf Hoffmann, Andrej Frolov |
|---|---|
| Rok vydání: | 2016 |
| Předmět: |
Glycation End Products
Advanced 0301 basic medicine medicine.medical_specialty Genomics and Proteomics Pilot Projects Type 2 diabetes Biochemistry 03 medical and health sciences Glycation Internal medicine Diabetes mellitus Amadori rearrangement medicine Humans Molecular Biology Glycemic 030102 biochemistry & molecular biology Chemistry Type 2 Diabetes Mellitus Blood Proteins Cell Biology Human serum albumin medicine.disease Blood proteins 030104 developmental biology Endocrinology Diabetes Mellitus Type 2 Protein Processing Post-Translational medicine.drug |
| Zdroj: | Journal of Biological Chemistry. 291:9610-9616 |
| ISSN: | 0021-9258 |
| DOI: | 10.1074/jbc.m115.702860 |
| Popis: | Protein glycation refers to the reversible reaction between aldoses (or ketoses) and amino groups yielding relatively stable Amadori (or Heyns) products. Consecutive oxidative cleavage reactions of these products or the reaction of amino groups with other reactive substances (e.g. α-dicarbonyls) yield advanced glycation end products (AGEs) that can alter the structures and functions of proteins. AGEs have been identified in all organisms, and their contents appear to rise with some diseases, such as diabetes and obesity. Here, we report a pilot study using highly sensitive and specific proteomics approach to identify and quantify AGE modification sites in plasma proteins by reversed phase HPLC mass spectrometry in tryptic plasma digests. In total, 19 AGE modification sites corresponding to 11 proteins were identified in patients with type 2 diabetes mellitus under poor glycemic control. The modification degrees of 15 modification sites did not differ among cohorts of normoglycemic lean or obese and type 2 diabetes mellitus patients under good and poor glycemic control. The contents of two amide-AGEs in human serum albumin and apolipoprotein A-II were significantly higher in patients with poor glycemic control, although the plasma levels of both proteins were similar among all plasma samples. These two modification sites might be useful to predict long term, AGE-related complications in diabetic patients, such as impaired vision, increased arterial stiffness, or decreased kidney function. |
| Databáze: | OpenAIRE |
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