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• W2040141850 abstract "Abstract Oxysterols, derived either from cholesterol autoxidation in vitro or through lipoprotein peroxidation in vivo are biologically active compounds implicated in the pathogenesis of atherosclerosis. Using 25-hydroxycholesterol (25OHC) as a model and radiolabeled 25OHC to trace mass, in this study we examined the transport of oxysterols in human serum. In contrast to cholesterol, which is associated exclusively with serum lipoproteins, 55 to 75% of 25OHC added to serum in vitro was associated with the lipoprotein-deficient fraction of serum (LPDS, density > 1.21 g/mL) over a wide concentration range. Upon sequential gel filtration, ion-exchange chromatography, and nondenaturing polyacrylamide gel electrophoresis, 25OHC added to LPDS eluted in a single peak corresponding to a protein peak of molecular weight about 67 kD. Immunoprecipitation of serum albumin from LPDS also precipitated 25OHC. 25OHC added to albumin-depleted LPDS did not associate with any of the remaining serum proteins, suggesting that albumin is the sole protein with which 25OHC associates to any significant extent in LPDS. Bovine serum albumin (BSA) was used to characterize the association of 25OHC with albumin. Other oxysterols, including 19-hydroxycholesterol, 7β-hydroxycholesterol, and 7-ketocholesterol, effectively competed with 25OHC for association with BSA, suggesting that they also associate with albumin in serum. The association of 25OHC with albumin in serum is selective but of low affinity as calculated from Scatchard analysis. However, given the high concentration of albumin in serum a significant amount of serum oxysterols may be delivered to or removed from various tissues via albumin." @default.
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• W2040141850 date "1995-11-01" @default.
• W2040141850 modified "2023-09-27" @default.
• W2040141850 title "Distribution of oxysterols in human serum: Characterization of 25-hydroxycholesterol association with serum albumin" @default.
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• W2040141850 doi "https://doi.org/10.1016/0955-2863(95)00122-g" @default.
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