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Glycated proteins in diabetes
1Oxford Research Unit, Open University, England, UK.
British Journal of Biomedical Science
|March 21, 1998
Summary
Protein glycation by sugars like glucose and fructose forms harmful products linked to diabetic complications. Monitoring glycation in vivo is challenging, but antiglycation therapies offer potential benefits.
Area of Science:
- Biochemistry
- Molecular Biology
- Endocrinology
Background:
- Protein glycation is a non-enzymatic reaction involving sugars.
- Glucose and fructose are primary dietary sugars that can glycate proteins.
- Glycation products are implicated in the pathogenesis of diabetes mellitus.
Purpose of the Study:
- To discuss the effects of protein glycation by glucose and fructose.
- To emphasize glycation products found in diabetic subjects and prepared in vitro.
- To review molecular damage, diabetic complications, monitoring challenges, and antiglycation therapy.
Main Methods:
- Literature review of glycation effects and products.
- Analysis of molecular damage from Amadori products and advanced glycation end-products (AGEs).
- Critical evaluation of in vivo glycation monitoring and antiglycation strategies.
Main Results:
- Glycation by glucose and fructose produces Amadori products and AGEs.
- These products cause molecular damage linked to diabetic complications.
- In vivo glycation monitoring presents significant difficulties.
Conclusions:
- Protein glycation contributes to diabetic complications through molecular damage.
- Antiglycation therapies are a potential therapeutic avenue.
- Further research is needed for effective in vivo glycation monitoring and treatment.