Glycation of biomolecules leads to the formation of advanced glycation end products (AGEs) and is implicated in molecular mechanisms of human chronic diseases. We compared the glycation properties of D-ribose and methylglyoxal on human high-density lipoprotein (HDL). The increase in fluorescent AGEs in HDL samples treated with methylglyoxal confirms that HDLs are sensitive to glycation treatment. Our results demonstrated that even D-ribose glycates HDL as shown by changes induced by D-ribose on HDL apoprotein. Biochemical markers of lipid and protein oxidative damage were also evaluated. The increase in protein carbonyl contents and thiobarbituric acid reactive substances (TBARS) demonstrates a glyco-oxidative stress occurs in D-ribose treated HDL. In addition, HDL treated with D-ribose showed a significant decrease in the activity of the enzyme paraoxonase 1 and an increased HDL redox activity. These data demonstrate that D-ribose-induced glycation of HDL may impair lipoprotein functionality and may contribute to molecular mechanisms of dysmetabolic diseases.
Morresi et al. (Thu,) studied this question.