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Updated: May 7, 2026

Cell-free Biochemical Fluorometric Enzymatic Assay for High-throughput Measurement of Lipid Peroxidation in High Density Lipoprotein
Published on: October 12, 2017
Biomarkers associated with high-density lipoproteins in atherosclerotic kidney disease
1Lipid Research Group, Centre for Vascular Research, Level 3, Lowy Centre, The University of New South Wales, Sydney, NSW, 2052, Australia, k.rye@unsw.edu.au.
Insights
Non-enzymatic glycation of apolipoprotein A-I impairs high-density lipoprotein (HDL) function. This process compromises HDL
Area of Science:
- Cardiovascular Science
- Lipid Metabolism
- Protein Chemistry
Background:
- High-density lipoproteins (HDL) are crucial for cholesterol transport and cardiovascular health.
- Apolipoprotein A-I (apoA-I) is the primary protein in HDL, facilitating cholesterol removal and possessing antioxidant properties.
- Diabetes and renal disease are linked to impaired HDL function and increased cardiovascular risk.
Purpose of the Study:
- To review the impact of non-enzymatic glycation of apoA-I on HDL structure and function.
- To investigate how glycated apoA-I affects lecithin:cholesterol acyltransferase (LCAT) activity.
- To examine the consequences of apoA-I glycation on cholesterol efflux and HDL's anti-inflammatory/antioxidant properties.
Main Methods:
- Review of existing literature on HDL metabolism, apoA-I glycation, and cardiovascular disease.
- Analysis of studies investigating the effects of non-enzymatic glycation on LCAT activity.
- Examination of research on cholesterol efflux from macrophages mediated by HDL.
Main Results:
- Non-enzymatic glycation of apoA-I alters HDL particle formation and function.
- Glycation of apoA-I inhibits the LCAT reaction, hindering the conversion of discoidal to spherical HDL.
- Impaired cholesterol efflux and reduced anti-inflammatory/antioxidant properties of HDL are associated with glycated apoA-I.
Conclusions:
- Non-enzymatic glycation of apoA-I is a significant factor in the compromised cardioprotective functions of HDL observed in diabetes and renal disease.
- Understanding these mechanisms is vital for developing strategies to mitigate cardiovascular risk in these patient populations.
- Further research is needed to fully elucidate the complex interplay between glycation, HDL function, and cardiovascular outcomes.
Abstract:
High-density lipoproteins (HDL) originate as discoidal particles that are rapidly converted by lecithin:cholesterol acyltransferase (LCAT) into the spherical particles that predominate in normal human plasma. Spherical HDL consist of multiple populations of particles that vary widely in size, composition and function. Human population studies have established that high plasma HDL cholesterol levels are associated with a reduced incidence of cardiovascular disease. The mechanistic basis of this relationship is not well understood, but most likely involves a number of the cardioprotective functions of HDL. These include the ability of apolipoprotein (apo) A-I, the main apolipoprotein constituent of HDL, to remove cholesterol from macrophages in the artery wall. HDL also have antioxidant and anti-inflammatory properties that are potentially cardioprotective. Evidence that some of these beneficial properties are compromised in people with diabetes and renal disease is emerging. Persistently elevated plasma glucose levels in people with diabetes and poor glycemic control can lead to irreversible, non-enzymatic glycation of plasma proteins, including apoA-I. Non-enzymatically glycated proteins are also prevalent in people with diabetes and end-stage renal disease who are at high cardiovascular risk. Evidence that non-enzymatically glycated apoA-I inhibits the LCAT reaction and impairs some of the cardioprotective properties of HDL is also emerging. This review is concerned with how non-enzymatic glycation of apoA-I affects the ability of LCAT to convert discoidal HDL into spherical HDL, how it affects cholesterol efflux from macrophages and how it affects the anti-inflammatory and antioxidant properties of HDL.
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