Comprehensive Identification of Glycated Peptides and Their Glycation Motifs in Plasma and Erythrocytes of Control and Diabetic Subjects
Nonenzymatic glycation of proteins sets the stage for formation of advanced glycation end-products and development of chronic complications of diabetes. In this report, we extended our previous methods on proteomics analysis of glycated proteins to comprehensively identify glycated proteins in contr...
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| Published in | Journal of proteome research Vol. 10; no. 7; pp. 3076 - 3088 |
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| Main Authors | , , , , , , , , |
| Format | Journal Article |
| Language | English |
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American Chemical Society
01.07.2011
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| Abstract | Nonenzymatic glycation of proteins sets the stage for formation of advanced glycation end-products and development of chronic complications of diabetes. In this report, we extended our previous methods on proteomics analysis of glycated proteins to comprehensively identify glycated proteins in control and diabetic human plasma and erythrocytes. Using immunodepletion, enrichment, and fractionation strategies, we identified 7749 unique glycated peptides, corresponding to 3742 unique glycated proteins. Semiquantitative comparisons showed that glycation levels of a number of proteins were significantly increased in diabetes and that erythrocyte proteins were more extensively glycated than plasma proteins. A glycation motif analysis revealed that some amino acids were favored more than others in the protein primary structures in the vicinity of the glycation sites in both sample types. The glycated peptides and corresponding proteins reported here provide a foundation for potential identification of novel markers for diabetes, hyperglycemia, and diabetic complications in future studies. |
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| AbstractList | Nonenzymatic glycation of proteins sets the stage for formation of advanced glycation end-products and development of chronic complications of diabetes. In this report, we extended our previous methods on proteomics analysis of glycated proteins to comprehensively identify glycated proteins in control and diabetic human plasma and erythrocytes. Using immunodepletion, enrichment, and fractionation strategies, we identified 7749 unique glycated peptides, corresponding to 3742 unique glycated proteins. Semiquantitative comparisons showed that glycation levels of a number of proteins were significantly increased in diabetes and that erythrocyte proteins were more extensively glycated than plasma proteins. A glycation motif analysis revealed that some amino acids were favored more than others in the protein primary structures in the vicinity of the glycation sites in both sample types. The glycated peptides and corresponding proteins reported here provide a foundation for potential identification of novel markers for diabetes, hyperglycemia, and diabetic complications in future studies. Non-enzymatic glycation of proteins is implicated in diabetes mellitus and its related complications. In this report, we extend our previous development and refinement of proteomics-based methods for the analysis of non-enzymatically glycated proteins to comprehensively identify glycated proteins in normal and diabetic human plasma and erythrocytes. Using immunodepletion, enrichment, and fractionation strategies, we identified 7749 unique glycated peptides, corresponding to 3742 unique glycated proteins. Semi-quantitative comparisons revealed a number of proteins with glycation levels significantly increased in diabetes relative to control samples and that erythrocyte proteins are more extensively glycated than plasma proteins. A glycation motif analysis revealed amino acids that are favored more than others in the protein primary structures in the vicinity of the glycation sites in both sample types. The glycated peptides and corresponding proteins reported here provide a foundation for the potential identification of novel markers for diabetes, glycemia, or diabetic complications. Nonenzymatic glycation of proteins sets the stage for formation of advanced glycation end-products and development of chronic complications of diabetes. In this report, we extended our previous methods on proteomics analysis of glycated proteins to comprehensively identify glycated proteins in control and diabetic human plasma and erythrocytes. Using immunodepletion, enrichment, and fractionation strategies, we identified 7749 unique glycated peptides, corresponding to 3742 unique glycated proteins. Semiquantitative comparisons showed that glycation levels of a number of proteins were significantly increased in diabetes and that erythrocyte proteins were more extensively glycated than plasma proteins. A glycation motif analysis revealed that some amino acids were favored more than others in the protein primary structures in the vicinity of the glycation sites in both sample types. The glycated peptides and corresponding proteins reported here provide a foundation for potential identification of novel markers for diabetes, hyperglycemia, and diabetic complications in future studies.Nonenzymatic glycation of proteins sets the stage for formation of advanced glycation end-products and development of chronic complications of diabetes. In this report, we extended our previous methods on proteomics analysis of glycated proteins to comprehensively identify glycated proteins in control and diabetic human plasma and erythrocytes. Using immunodepletion, enrichment, and fractionation strategies, we identified 7749 unique glycated peptides, corresponding to 3742 unique glycated proteins. Semiquantitative comparisons showed that glycation levels of a number of proteins were significantly increased in diabetes and that erythrocyte proteins were more extensively glycated than plasma proteins. A glycation motif analysis revealed that some amino acids were favored more than others in the protein primary structures in the vicinity of the glycation sites in both sample types. The glycated peptides and corresponding proteins reported here provide a foundation for potential identification of novel markers for diabetes, hyperglycemia, and diabetic complications in future studies. Non-enzymatic glycation of proteins sets the stage for formation of advanced glycation end-products and development of chronic complications of diabetes. In this report, we extended our previous methods on proteomics analysis of glycated proteins to comprehensively identify glycated proteins in control and diabetic human plasma and erythrocytes. Using immunodepletion, enrichment, and fractionation strategies, we identified 7749 unique glycated peptides, corresponding to 3742 unique glycated proteins. Semi-quantitative comparisons showed that glycation levels of a number of proteins were significantly increased in diabetes and that erythrocyte proteins were more extensively glycated than plasma proteins. A glycation motif analysis revealed that some amino acids were favored more than others in the protein primary structures in the vicinity of the glycation sites in both sample types. The glycated peptides and corresponding proteins reported here provide a foundation for potential identification of novel markers for diabetes, hyperglycemia, and diabetic complications in future studies. |
| Author | Monroe, Matthew E Petyuk, Vladislav A Schepmoes, Athena A Gritsenko, Marina A Meng, Da Metz, Thomas O Clauss, Therese R. W Zhang, Qibin Smith, Richard D |
| AuthorAffiliation | Pacific Northwest National Laboratory |
| AuthorAffiliation_xml | – name: Pacific Northwest National Laboratory |
| Author_xml | – sequence: 1 givenname: Qibin surname: Zhang fullname: Zhang, Qibin – sequence: 2 givenname: Matthew E surname: Monroe fullname: Monroe, Matthew E – sequence: 3 givenname: Athena A surname: Schepmoes fullname: Schepmoes, Athena A – sequence: 4 givenname: Therese R. W surname: Clauss fullname: Clauss, Therese R. W – sequence: 5 givenname: Marina A surname: Gritsenko fullname: Gritsenko, Marina A – sequence: 6 givenname: Da surname: Meng fullname: Meng, Da – sequence: 7 givenname: Vladislav A surname: Petyuk fullname: Petyuk, Vladislav A – sequence: 8 givenname: Richard D surname: Smith fullname: Smith, Richard D – sequence: 9 givenname: Thomas O surname: Metz fullname: Metz, Thomas O email: thomas.metz@pnl.gov |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/21612289$$D View this record in MEDLINE/PubMed https://www.osti.gov/biblio/1020630$$D View this record in Osti.gov |
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| Keywords | boronate affinity chromatography electron transfer dissociation type 2 diabetes mellitus Amadori compound nonenzymatic glycation plasma glycation motif erythrocyte red blood cell |
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| Snippet | Nonenzymatic glycation of proteins sets the stage for formation of advanced glycation end-products and development of chronic complications of diabetes. In... Non-enzymatic glycation of proteins is implicated in diabetes mellitus and its related complications. In this report, we extend our previous development and... Non-enzymatic glycation of proteins sets the stage for formation of advanced glycation end-products and development of chronic complications of diabetes. In... |
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| SubjectTerms | 60 APPLIED LIFE SCIENCES Amadori compound Amino Acid Motifs AMINO ACIDS BASIC BIOLOGICAL SCIENCES Biomarkers - blood Biomarkers - chemistry Blood Proteins - analysis Blood Proteins - chemistry boronate affinity chromatography Chromatography, Affinity Chromatography, High Pressure Liquid Diabetes Complications - blood Diabetes Complications - physiopathology DIABETES MELLITUS Diabetes Mellitus, Type 2 - blood Diabetes Mellitus, Type 2 - physiopathology electron transfer dissociation Environmental Molecular Sciences Laboratory erythrocyte ERYTHROCYTES Erythrocytes - chemistry FRACTIONATION Glycation End Products, Advanced - blood Glycation End Products, Advanced - chemistry glycation motif Glycopeptides - blood Glycopeptides - chemistry Glycosylation Humans Hyperglycemia - blood Hyperglycemia - physiopathology Molecular Sequence Data nonenzymatic glycation Peptide Fragments - blood Peptide Fragments - chemistry PEPTIDES PLASMA Plasma - chemistry PROTEINS Proteomics - methods red blood cell Tandem Mass Spectrometry Trypsin - metabolism type 2 diabetes mellitus |
| Title | Comprehensive Identification of Glycated Peptides and Their Glycation Motifs in Plasma and Erythrocytes of Control and Diabetic Subjects |
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