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Abstract
Advanced glycation end products (AGEs) is a causative factor of various chronic diseases, including chronic kidney disease and atherosclerosis. AGE inhibitors, such as aminoguanidine and pyridoxamine, have the therapeutic activities for reversing the increase in AGEs burden. This study evaluated the inhibitory effects of aucubin on the formation of methylglyoxal (MGO)-modified AGEs in vitro. We also determined the potential activity of aucubin in reducing the AGEs burden in the kidney, blood vessel, heart, and retina of exogenously MGO-injected rats. Aucubin inhibited the formation of MGO-modified AGE-bovine serum albumin (IC50 = 0.57 ± 0.04 mmol/L) and its cross-links to collagen (IC50 = 0.55 ± 0.02 mmol/L) in a dose-dependent manner. In addition, aucubin directly trapped MGO (IC50 = 0.22 ± 0.01 mmol/L) in vitro. In exogenous MGO-injected rats, aucubin suppressed the formation of circulating AGEs and its accumulation in various tissues. These activities of aucubin on the MGO-derived AGEs in vitro and in vivo showed its pharmacological potential for inhibiting AGEs-related various chronic diseases.
Highlights
The advanced glycation end products (AGEs) are generated in the human body and affect the structure and function of proteins
Oxidative stress is further fueled by excessive reactive oxygen stress (ROS) generation from glucose autoxidation and the nonenzymatic, covalent attachment of glucose molecules to circulating proteins that result in the formation of AGEs [8,9,10]
The formation of AGEs is an irreversible reaction and AGEs can form cross-links with proteins resulting in disturbed biochemical reactions, AGEs are implicated in pathogenic processes of various age-related diseases [11]
Summary
The advanced glycation end products (AGEs) are generated in the human body and affect the structure and function of proteins. This process was first introduced by Louis-Camille Maillard in. The formation of AGEs is an irreversible reaction and AGEs can form cross-links with proteins resulting in disturbed biochemical reactions, AGEs are implicated in pathogenic processes of various age-related diseases [11]. Matrix proteins such as collagen are properly cross-linked with AGEs in conditions like diabetes and aging [12,13]
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