Advanced glycation end products and diabetic complications
Varun Parkash Singh1, Anjana Bali1, Nirmal Singh1
1Department of Pharmaceutical Sciences and Drug Research, Punjabi University, Patiala-147002, India.
Summary
High blood sugar in diabetes causes protein glycation, forming advanced glycation end products (AGEs). These AGEs contribute to diabetic complications and aging by altering protein function and promoting disease pathways.
Area of Science:
- Biochemistry
- Molecular Biology
- Pathophysiology
Background:
- Hyperglycemia in diabetes mellitus leads to non-enzymatic glycation of plasma proteins.
- Protein glycation forms advanced glycation end products (AGEs), implicated in diabetic complications and other diseases.
Purpose of the Study:
- To review the glycation of plasma proteins and the formation of AGEs.
- To discuss the role of AGEs in the pathogenesis of diabetic complications.
Main Methods:
- Review of existing literature on protein glycation and AGEs.
- Discussion of AGEs' impact on protein structure and function.
- Exploration of AGEs' interaction with receptors like RAGE.
Main Results:
- Glycation disrupts protein conformation, enzymatic activity, and receptor function.
- AGEs cross-link proteins, lipids, and nucleic acids, contributing to disease.
- AGEs interact with RAGE, altering cellular signaling and inflammation.
Conclusions:
- Protein glycation and AGEs are key contributors to diabetic complications such as retinopathy, nephropathy, neuropathy, and cardiomyopathy.
- AGEs also play a role in aging and diseases like rheumatoid arthritis and osteoporosis.
- Understanding AGEs' mechanisms is crucial for developing therapeutic strategies against diabetic complications.
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