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Updated: Jul 20, 2026

Chemically-blocked Antibody Microarray for Multiplexed High-throughput Profiling of Specific Protein Glycosylation in Complex Samples
Published on: May 4, 2012
Glycated proteins in diabetes.
P J Beisswenger1, B S Szwergold, K T Yeo
1Department of Medicine (Endocrinology), Dartmouth Medical School, Dartmouth-Hitchcock Medical Center, Lebanon and Hanover, New Hampshire, USA.
Nonenzymatic glycation, a reaction between sugars and proteins, contributes to diabetic complications and aging. Measuring alpha-dicarbonyls and advanced glycation end-products (AGEs) may improve diabetes monitoring and complication prediction.
Area of Science:
- Biochemistry
- Gerontology
- Endocrinology
Background:
- Nonenzymatic glycation involves spontaneous reactions between reducing sugars and protein-bound amines.
- This process contributes to diabetic complications and age-related degenerative changes.
- Alpha-dicarbonyls are an additional source of glycation beyond monocarbonyl sugars.
Purpose of the Study:
- To highlight the role of nonenzymatic glycation and advanced glycation end-products (AGEs) in human health.
- To discuss the potential of measuring alpha-dicarbonyls and AGEs for improved diabetes management.
Main Methods:
- Review of existing literature on nonenzymatic glycation and AGE formation.
- Discussion of analytical methods for quantifying alpha-dicarbonyls and AGEs.
Main Results:
- Nonenzymatic glycation leads to the formation of irreversible advanced glycation end-products (AGEs).
- AGEs are implicated in the etiology of diabetic complications.
- Improved measurement techniques for alpha-dicarbonyls and AGEs are emerging.
Conclusions:
- Nonenzymatic glycation and AGEs are significant factors in diabetic complications and aging.
- Enhanced measurement of alpha-dicarbonyls and AGEs offers potential for future diabetes monitoring and complication prediction.
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