Advanced glycation end-products (AGEs): involvement in aging and in neurodegenerative diseases.
Advanced glycation end-products (AGEs) are formed from the so-called Amadori products by rearrangement followed by other reactions giving rise to compounds bound irreversibly. The structure of some of them is shown and the mechanism of formation is described. Several AGE binding molecules (Receptors for AGE, RAGE) are known and it is thought that many of the effects caused by AGEs are mediated by RAGE. Some of these were shown to be toxic, and called TAGE. The mechanism of detoxification of glyoxal and methylglyoxal by the glyoxalase system is described and also the possibility to eliminate glycated proteins by deglycation enzymes. Compounds able to inhibit AGEs formation are also taken into consideration.
Grillo
M A
MA
Dipartimento di Medicina e Oncologia Sperimentale, Sezione di Biochimica, Università di Torino, Torino, Italy. mariaangelica.grillo@unito.it
Colombatto
S
S
D000375:Aging / Q000378:metabolism*; D000445:Aldehyde Oxidoreductases; D000818:Animals; D017127:Glycation End Products, Advanced / Q000378:metabolism*; D006037:Glyoxal / Q000378:metabolism / Q000633:toxicity; D006801:Humans; D011765:Pyruvaldehyde; D000067759:Receptor for Advanced Glycation End Products; D011971:Receptors, Immunologic / Q000378:metabolism*
D017127:Glycation End Products, Advanced; D000067759:Receptor for Advanced Glycation End Products; D011971:Receptors, Immunologic; D006037:Glyoxal; D011765:Pyruvaldehyde; D000445:Aldehyde Oxidoreductases