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Updated: May 28, 2026

Cell-free Biochemical Fluorometric Enzymatic Assay for High-throughput Measurement of Lipid Peroxidation in High Density Lipoprotein
Published on: October 12, 2017
D-Ribose Glycation of Human High-Density Lipoprotein: Structural and Functional Alterations
Camilla Morresi1, Valeria Di Tomaso2, Giovanni Ricci1
1Department of Life and Environmental Sciences, Polytechnic University of the Marche, 60131 Ancona, Italy.
Abstract:
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.
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