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Search Results: Advanced glycation end products

Sugars serve as energy sources and building blocks for macromolecules, making them indispensable to living organisms. Yet, there is also a negative...


= Encyclopedia Article; = Research Update
Figure 1.Classical view of AGE formation. Reducing sugars such as glucose or fructose react spontaneously with lysine or arginine residues in proteins. Initially a reversible condensation product (Schiff base, for example, fructose-lysine) is formed (1). Subsequently, stabilization of the adduct and Maillard browning reactions (2) result in the formation of stable AGEs: some form protein-protein crosslinks, whereas others are protein adducts. MOLD, methylglyoxal-lysine dimer; GOLD, glyoxal-lysine dimer; CML, Ne-(carboxymethyl)lysine; CEL, Ne-(carboxyethyl)lysine.
Figure 2.Chemical structures of AGEs that have been identified in human tissue proteins.
Figure 3.Potential strategies for anti-AGE therapies. Strategies include (1) inhibition of Schiff-base formation (for example, by aminoguanidine, lysine, or arginine); (2) inhibition of subsequent AGE formation (for example, by aminoguanidine or pyridoxamine); (3) breaking of AGE crosslinks (for example, by PTB or ALT-711); or (4) modulation of cellular effects by blockade of the AGE-RAGE interaction.
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