Structural modifications of HDL and functional consequences

Ferretti, Gianna; Bacchetti, Tiziana; Nègre‐Salvayre, Anne; Salvayre, Robert; Dousset, N.; Curatola, G

doi:10.1016/j.atherosclerosis.2005.08.008

Cited by 151 publications

(105 citation statements)

References 66 publications

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“…Lipid peroxidation induces significant changes of physicochemical properties and functional activities of lipoproteins such as exchange processes between lipoproteins and membranes (33,34). We suggest that the compositional changes observed in HDL of patients could reflect in a reduced ability to stimulate efflux of hydroperoxides from ox-membranes and/or to accept lipid hydroperoxides from oxidized membranes.…”

Section: Discussionmentioning

confidence: 87%

HDL‐paraoxonase and Membrane Lipid Peroxidation: A Comparison Between Healthy and Obese Subjects

Ferretti

Bacchetti

Masciangelo

et al. 2010

Obesity

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High‐density lipoproteins (HDLs) play a key role in the protection against oxidative damage. The enzyme paraoxonase‐1 (PON1) associated at the surface of HDL modulates the antioxidant and anti‐inflammatory role of HDL. Previous studies have demonstrated a decrease of serum PON in obese patients. The aim of this study was to investigate whether modifications of PON1 activity reflect in a different ability to protect and/or repair biological membranes against oxidative damage. Thirty obese patients at different grades of obesity (BMI ranging from 30.4 to 64.0 kg/m2) and 62 age‐matched control subjects (BMI <25 kg/m2) were included in the study. The ability of HDL to protect membranes against oxidative damage was studied using erythrocyte membranes oxidized with 2,2‐azobis(2 amidinopropane)dihydrochloride (AAPH) (ox‐membrane). The membrane lipid hydroperoxide levels were evaluated after the incubation of ox‐membranes in the absence or in the presence of HDL of controls or obese patients. The results confirm that HDL exerts a protective effect against lipid peroxidation. The ability of HDL to repair erythrocyte membranes was positively correlated with HDL‐PON activity and negatively correlated with lipid hydroperoxide levels in HDL. These results suggest that PON modulates the HDL repairing ability. HDL from obese patients repaired less efficiently erythrocyte membranes against oxidative damage with respect to HDL from healthy subjects. A negative relationship has been established between BMI of obese patients and the protective effect of HDL. In conclusion, the decrease of HDL‐PON activity and the lower HDL protective action against membrane peroxidation in obese patients could contribute to accelerate the cellular oxidative damage and arteriosclerosis in obesity.

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Section: Discussionmentioning

confidence: 87%

HDL‐paraoxonase and Membrane Lipid Peroxidation: A Comparison Between Healthy and Obese Subjects

Ferretti

Bacchetti

Masciangelo

et al. 2010

Obesity

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“…(37,38) Differences in distribution and size of HDL-P have been related to CVD risk. (39)(40)(41)(42)(43)(44)(45)(46) Whether there is a unique important protective effect of size of HDL-P measured by NMR spectroscopy requires better assessment of the characteristics and metabolism by size of HDL-P. (39) Large rather than small LDL-P were more strongly related to risk of CHD death for MRFIT men with MetSyn, especially among men without morbid CV events in the first 6 years of the trial. Recent reports from the MESA (36) and the VA-HIT trial (35) have shown that markers of LDL-P rather than size may be a more important determinant of the risk of CHD.…”

Section: Discussionmentioning

confidence: 99%

Lipoprotein particles, insulin, adiponectin, C-reactive protein and risk of coronary heart disease among men with metabolic syndrome

et al. 2007

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We tested the hypotheses whether nuclear magnetic resonance (NMR) determined lipoprotein particles, insulin and adiponectin, and C-reactive protein (CRP) and white blood cell (WBC) count as markers of inflammation predicted risk of coronary heart disease (CHD) death among 428 men age 35-57 years with metabolic syndrome (MetSyn) in a matched case control study within the Multiple Risk Factor Intervention Trial.Blood samples collected at entry into the study and stored at −60° C were obtained from central storage for blood analyte analysis. 214 men with MetSyn who died of CHD were matched with 214 men with MetSyn who did not die of CHD during 18 years of follow-up. Cases were matched to controls on age, study group, number of factors present in the MetSyn, and presence or absence of a non-fatal CVD event during the trial. Mortality follow up was determined using the National Death Index.Higher levels of high density lipoprotein particles (HDL-P), especially medium-sized HDL-P, [hazard ratio (95% confidence interval) 0.45 (0.25-0.83, p<0.01), quartile 1 as compared to quartile 4], were associated with lower risk of CHD death. Low density lipoprotein (LDL) particles were not associated with increased risk of CHD. Elevated LDL cholesterol (LDL-C), smoking and WBC count were, but levels of adiponectin, insulin and CRP were not significantly related to CHD death. In multivariate models adjusting for smoking and LDL-C, medium HDL-P and WBC count remained independent predictors of CHD death.Number of HDL particles, especially medium-sized HDL particles and WBC count were independent predictors of CHD death among men with MetSyn.

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“…Spherical HDL particles contain cholesterol esters and result from free cholesterol-containing discoidal HDL particles after the LCAT action. 50 In spherical HDL, ApoA1 molecules envelope~80% of a total surface thereby underlining the major role of this apolipoprotein in stabilizing HDL structure and shape. 34 In the spheres, Silva et al 51 showed that ApoA1 maintains the double-belt arrangement such as in discoidal HDL.…”

Section: Apoa1 Structure In Discoidal Hdl Particlesmentioning

confidence: 99%

“…This leads to the transformation of discoidal HDL to spherical HDL. 50 Indeed, genetic deletion of LCAT in mice results in lowered concentrations of HDL spheres, although discoidal HDL levels are elevated. 63 Involvement of ApoA1 in RCT ApoA1 regulates RCT through interaction with ABCA1.…”

Section: Involvement Of Apoa1 In Cholesterol Esterificationmentioning

confidence: 99%