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Related Experiment Videos

Glycation impairs high-density lipoprotein function.

C C Hedrick1, S R Thorpe, M X Fu

  • 1Division of Cardiology, University of California School of Medicine, Los Angeles 90095-1679, USA.

Diabetologia
|April 18, 2000
PubMed
Summary
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Hyperglycaemic conditions impair high-density lipoprotein (HDL) function by increasing glycation and reducing paraoxonase activity. These HDL alterations may contribute to accelerated atherosclerosis in Type II diabetes.

Area of Science:

  • Biochemistry
  • Cardiovascular Research
  • Metabolic Disorders

Background:

  • High-density lipoprotein (HDL) plays a crucial role in reverse cholesterol transport and possesses anti-atherogenic properties.
  • Hyperglycaemia, a hallmark of diabetes, is associated with increased oxidative stress and protein glycation.
  • Dysfunctional HDL is implicated in the pathogenesis of atherosclerosis.

Purpose of the Study:

  • To investigate the in vitro effects of hyperglycaemic conditions on human high-density lipoprotein (HDL) functionality.
  • To assess the impact of glucose exposure on HDL's enzymatic activities and its ability to inhibit monocyte adhesion.
  • To explore the relationship between HDL dysfunction and paraoxonase activity in patients with Type II diabetes.

Main Methods:

Related Experiment Videos

  • Human HDL was incubated for one week under hyperglycaemic conditions (25 mmol/l glucose) or control conditions.
  • Glycation products (fructoselysine, N epsilon-(carboxymethyl)-lysine) and apolipoprotein concentrations were measured.
  • Paraoxonase enzymatic activity and HDL's ability to inhibit monocyte adhesion to endothelial cells were assessed.
  • Paraoxonase protein was directly glycated to evaluate its functional changes.

    • Main Results:

    • Incubation in glucose led to increased HDL glycation, a 65% reduction in paraoxonase activity, and impaired inhibition of monocyte adhesion.
    • Glycated HDL showed enhanced non-esterified fatty acid release mediated by hepatic lipase.
    • Direct glycation of paraoxonase protein reduced its activity by 40% and abolished its inhibitory effect on monocyte adhesion.
    • Patients with Type II diabetes and coronary artery disease exhibited a 40% reduction in paraoxonase activity.

    Conclusions:

    • Exposure of HDL to hyperglycaemic conditions in vitro induces functional alterations, including reduced paraoxonase activity and impaired anti-atherogenic properties.
    • These HDL dysfunctions, characterized by increased glycation and reduced paraoxonase activity, may contribute to the accelerated atherosclerosis observed in Type II diabetes.
    • The findings highlight the detrimental impact of hyperglycaemia on HDL functionality and its potential role in diabetic cardiovascular complications.