Protein glycation, diabetes, and aging.

Area of Science:

• Biochemistry
• Food Chemistry
• Gerontology

Background:

• The Maillard reaction, or advanced glycation, involves biological amines and reducing sugars, creating complex adducts.
• Advanced glycation endproducts (AGEs) form in vivo, contributing to diabetes complications and aging by crosslinking proteins like collagen.
• Vascular collagen AGEs lead to detrimental effects including plaque formation and reduced elasticity.

Purpose of the Study:

• To investigate the role of AGEs in aging and diabetes complications.
• To develop inhibitors of AGE formation and crosslinking.

Main Methods:

• Introduction of aminoguanidine hydrochloride as an inhibitor of AGE formation.
• Development of agents like DPTC to break AGE protein-protein crosslinks.
• Testing DPTC in aged animals to assess its effect on vascular compliance.

Main Results:

• Aminoguanidine has shown effectiveness in slowing diabetes and aging complications in animal and human studies.
• DPTC has demonstrated the ability to revert vascular compliance indices in aged animals.
• Human clinical trials for DPTC are currently in progress.

Conclusions:

• AGEs are significant contributors to the pathology of aging and diabetes.
• Inhibiting AGE formation and breaking existing AGE crosslinks are viable therapeutic strategies.
• Further research and clinical trials are warranted to validate these therapeutic approaches.