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A Mass Spectrometry-Based Proteomics Approach for Global and High-Confidence Protein R-Methylation Analysis
Published on: April 28, 2022
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Comprehensive Quantification of Carboxymethyllysine-Modified Peptides in Human Plasma
Arvind M Korwar1, Qibin Zhang1,2
1Center for Translational Biomedical Research, University of North Carolina at Greensboro, North Carolina Research Campus, Kannapolis, North Carolina 28081, United States.
Journal of the American Society for Mass Spectrometry
|January 29, 2021
Summary
Researchers identified novel protein markers for diabetes management. Five specific N(ε)-Carboxymethyllysine (CML) modified peptides in plasma show potential as indicators for assessing glycemic control in Type 1 diabetes.
Area of Science:
- Biochemistry
- Proteomics
- Diabetes Research
Background:
- Prolonged hyperglycemia in diabetes mellitus leads to protein glycation.
- N(ε)-Carboxymethyllysine (CML) is a key advanced glycation end product formed via Amadori compound modified lysine (AML).
- Limited biochemical methods exist for comprehensive CML-peptide profiling.
Purpose of the Study:
- To develop a method for comprehensive quantification of CML-modified peptides.
- To identify potential biomarkers for glycemic control in Type 1 diabetes.
Main Methods:
- Utilized AML peptide sequence and modification site as a template library.
- Developed a parallel reaction monitoring (PRM) workflow.
- Quantified CML-modified peptides in plasma from Type 1 diabetic subjects with good and poor glycemic control.
Main Results:
- Successfully quantified 58 CML-modified peptides across 19 proteins.
- Identified 57 unique CML modification sites.
- Five specific CML peptides were significantly elevated in individuals with poor glycemic control (AUC ≥ 0.83).
Conclusions:
- The identified CML peptides show promise as indicators of glycemic control.
- These findings contribute to the development of novel biomarkers for Type 1 diabetes management.
