Red Wine Inhibits the Cell-Mediated Oxidation of LDL and HDL

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Red Wine Inhibits the Cell-Mediated Oxidation of LDL and HDL

Vincent A. Rifici, PhD, Elias M. Stephan, MD, Stephen H. Schneider, MD and Avedis K. Khachadurian, MD

Department of Medicine, Robert Wood Johnson Medical School, University of Medicine and Dentistry of New Jersey, New Brunswick, New Jersey

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Fig. 1. Effects of red wine, white wine and ethanol (equivalent to 0.2 mg/mL ethanol) on LDL oxidation. LDL (0.2 mg protein/mL) was incubated with and without cells in 6 well plates (500,000 cells/well) for 16 h at 37°C in serum-free DMEM containing 2 µM copper. (A) Change in absorbance at 234 nm ( ${Delta}$ A234) is expressed relative to unmodified LDL. (B) TBARS are expressed as nmoles malondialdehyde (MDA) equivalents/mg LDL protein. (C) percent decrease in TNBS reactivity relative to the unmodified LDL (0%). The mean absorbance of the unmodified LDL (50 µg) at 340 nm = 0.164 ± 0.005. Results are means ± SEM of four experiments done in triplicate. Red wine vs. control, white wine and ethanol (A), p < 0.0001; (B), p < 0.0001; (C), p < 0.0006. RW = red wine; WW = white wine; EtOH = ethanol.

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Fig. 2. Concentration-dependent effect of red wine and white wine on cell mediated oxidation of LDL. Incubation conditions were as described in the legend to Fig. 1 except for incubation in 24-well plates (200,000 cells/well). The mean TBARS production by the cell control (represented as 100%) = 15.1 ± 2.4 nmoles MDA/mg LDL protein. The points are the means ± SEM of four determinations done in triplicate. Red wine vs. white wine in the range of 0.05–0.5 mg EtOH/mL, p < 0.001, at 1.0 mg/mL, NS. RW = red wine; WW = white wine.

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Fig. 3. Time course of LDL oxidation. Incubation conditions were as described in the legend to Fig. 1 except for incubation in 24-well plates (200,000 cells/well). (A) Change in absorbance at 234 nm ( ${Delta}$ A234) is expressed relative to unmodified LDL. (B) TBARS are expressed as nmoles MDA equivalents/mg LDL protein. Results are from one duplicate experiment. RW = red wine; WW = white wine.

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Fig. 4. Effects of red wine, white wine and ethanol (equivalent to 0.2 mg/mL ethanol) on HDL oxidation. HDL (0.5 mg protein/mL) was incubated with and without cells in 6 well plates (500,000 cells/well) for 24 h at 37°C in serum-free DMEM containing 5 µM copper. (A) Change in absorbance at 234 nm ( ${Delta}$ A234) is expressed relative to unmodified HDL. Results are means ± SEM of four experiments done in triplicate. (B) TBARS are expressed as nmoles malondialdehyde equivalents/mg HDL protein. (C) % decrease in TNBS reactivity relative to the unmodified HDL (0%). The mean absorbance of the unmodified HDL (50 µg) at 340 nm = 0.243 ± 0.040. Red wine media vs. control, white wine and ethanol (A) p < 0.0001; (B), p < 0.0001; (C) p < 0.007. RW = red wine; WW = white wine; EtOH = ethanol.

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Fig. 5. TBARS production from HDL oxidation at various concentrations of red and white wines. The incubation conditions were as described in the legend for Fig. 4 except for incubation in 24-well plates (200,000 cells/well). The mean TBARS production by the cell control (represented as 100%) = 9.7 ± 0.7 nmoles MDA/mg HDL protein. The results are the means ± SEM of four determinations done in duplicate. Red wine vs. white wine in the range of 0.05–0.5 mg EtOH/mL, p < 0.007, at 1.0 mg EtOH/mL, p = 0.0534 RW = red wine; WW = white wine.