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- W2127133072 abstract "The interaction of high-density lipoproteins (HDL) with adipocytes is important in the regulation of cellular cholesterol flux. To study the mechanisms of HDL binding and cellular processing, we incubated adipocytes isolated from epididymal and perirenal adipose tissue of male Wistar rats (300 g) with HDL 1 (1.07–1.10 g/mL) and HDL 2 (1.10–1.14 g/mL) fractions separated from rat plasma by gradient ultracentrifugation. Freshly isolated adipocytes were incubated with 125 I-labeled HDL for 2 h at 37 °C to determine cell-associated uptake and degradation. Adipocytes from both fat regions showed significant cell-associated HDL 1 and HDL 2 uptake and very high medium degradation (2- to 6-fold higher than uptake). To assess 125 I-labeled HDL binding independent of cellular metabolism, we purified adipocyte plasma membranes from isolated adipocytes and used them in binding assays. Binding of HDL 1 and HDL 2 in the membrane system was 85–95% specific, sensitive to high NaCl concentrations, and abolished by pronase treatment. In contrast to HDL 2 binding, the maximum HDL 1 binding to perirenal plasma membranes was significantly higher than its binding to epididymal membranes (7.2 ± 1.3 vs. 4.4 ± 0.2 μg/mg, n = 6, p < 0.05). This increment in HDL 1 binding to perirenal membranes represented an EDTA- sensitive, calcium-dependent component. These results indicate that HDL binding to adipocyte plasma membranes depends on both adipose tissue region and HDL subtype. The membrane binding characteristics, taken together with the cellular uptake results, suggest that adipocytes bind and metabolize HDL and that this interaction may involve a protein receptor." @default.
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- W2127133072 date "1988-09-01" @default.
- W2127133072 modified "2023-09-25" @default.
- W2127133072 title "Characterization of high-density lipoprotein binding to rat adipocytes and adipocyte plasma membranes" @default.
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- W2127133072 doi "https://doi.org/10.1139/o88-113" @default.
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