In vivo glycation of bovine lens crystallins

Abstract

To investigate the possible role of glycation in the aging of lens proteins, we used bovine lenses as a model. We studied crystallins isolated from prenatal bovine lenses, calf lenses and lenses from mature animals (up to 20 years old). The experiments show an increase in glycation levels with age in all crystallin fractions. Regarding the lysine content of the different crystallins, γ-crystallin showed relatively high levels of early glycation products. The results also revealed high levels of early glycation products for the HM material (containing mainly α-crystallin). In α-crystallin, αA-subunits were glycated to a higher extent compared with the αB-subunits. There is an age-related increase in advanced glycation products, measured as specific flourescence (excitation/emission wavelengths 370/440 nm), mainly present in the HM and α-crystallin fraction.