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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.
D-ribose causes glycation and oxidative stress in high-density lipoprotein (HDL), impairing its function. This glycation may contribute to dysmetabolic diseases.
Area of Science:
- Biochemistry
- Molecular Biology
- Metabolic Diseases
Background:
- Glycation of biomolecules forms advanced glycation end products (AGEs).
- AGEs are implicated in the molecular mechanisms of chronic human diseases.
- High-density lipoprotein (HDL) plays a crucial role in lipid metabolism and possesses protective functions.
Purpose of the Study:
- To compare the glycation properties of D-ribose and methylglyoxal on human HDL.
- To investigate the impact of D-ribose-induced glycation on HDL functionality.
- To explore the potential contribution of HDL glycation to dysmetabolic diseases.
Main Methods:
- Treatment of human HDL with D-ribose and methylglyoxal.
- Measurement of fluorescent AGEs formation.
- Assessment of HDL apoprotein modifications.
- Evaluation of biochemical markers for lipid and protein oxidative damage (protein carbonyls, TBARS).
- Assay of paraoxonase 1 activity and HDL redox activity.
Main Results:
- Methylglyoxal treatment increased fluorescent AGEs in HDL, confirming HDL's sensitivity to glycation.
- D-ribose also glycated HDL, inducing changes in HDL apoprotein.
- D-ribose treatment led to increased protein carbonyl content and TBARS, indicating glyco-oxidative stress.
- HDL treated with D-ribose exhibited decreased paraoxonase 1 activity and increased redox activity.
Conclusions:
- D-ribose induces glycation and glyco-oxidative stress in HDL.
- D-ribose-induced glycation impairs HDL functionality, including reduced paraoxonase 1 activity and increased redox activity.
- Impaired HDL functionality due to D-ribose glycation may contribute to the molecular mechanisms of dysmetabolic diseases.
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