Effect of glycation on α-crystallin structure and chaperone-like function

The chaperone-like activity of α-crystallin is considered to play an important role in the maintenance of the transparency of the eye lens. However, in the case of aging and in diabetes, the chaperone function of α-crystallin is compromized, resulting in cataract formation. Several post-translational modifications, including non-enzymatic glycation, have been shown to affect the chaperone function of α-crystallin in aging and in diabetes. A vari-ety of agents have been identified as the predominant sources for the formation of AGEs (advanced glycation end-products) in vari-ous tissues, including the lens. Nevertheless, glycation of α-crys-tallin with various sugars has resulted in divergent results. In the present in vitro study, we have investigated the effect of glucose, fructose, G6P (glucose 6-phosphate) and MGO (methyl-glyoxal), which represent the major classes of glycating agents, on the structure and chaperone function of α-crystallin. Modificatio