Nonenzymatic glycosylation of protein does not increase with age in normal human lenses

Abstract

Nonenzymatic glycosylation or glycation is a posttranslational modification of proteins which has been implicated in the aging of lens proteins and the development of senile and diabetic cataracts. The extent of glycation of normal human lens proteins was measured by reduction of the protein with [3H]NaBH4, acid hydrolysis and quantitation of radioactive hexitol-amino acids by phenylboronic acid (PBA) affinity chromatography. Hexitollysine (HL) accounted for greater than or equal to 90% of total radioactivity recovered as hexitol-amino acids (HAA). In lenses in the age range (1-79) years (n = 26) there was no significant age-dependent increase in glycation of lens proteins (p greater than .10). The average extent of glycation was 2.3 +/- 0.3 mmol glycated lysine/mol lysine, or approximately 0.8 nmol hexitollysine/mg lens protein. These results indicate that the extent of glycation of lysine residues in lens proteins is comparable to that of lysine residues in soluble proteins, such as hemoglobin and albumin, and that the extent of glycation of lens proteins does not increase with age. Thus, glycation, per se, is not an age-dependent chemical modification of human lens protein.