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- W2163444925 abstract "Background : In lithogenic bile, cholesterol‐rich vesicles rapidly aggregate and fuse to eventually form cholesterol crystals. This process is modulated by cholesterol crystallization effector substances. In this study, we developed a method for quantitative assessment of vesicle fusion and used it to partly characterize the mechanisms of action of cholesterol crystallization effector proteins. Methods : Cholesterol:phospholipid (1:1) liposomes were prepared and labelled with octadecyl rhodamine B chloride (R18). Fusion of these liposomes was detected by the increase of R18 fluorescence after incubation with various proteins, such as albumin, concanavalin‐A bound glycoprotein, immunoglobulins, apolipoprotein A‐I and apolipoprotein B (all at 100 μg/mL). Results : Fusion of cholesterol/phospholipid liposomes was increased by 16 and 14% in the presence of concanavalin‐A bound glycoprotein and immunoglobulins, respectively, and decreased by 21 and 9% after addition of apolipoprotein A‐I and apolipoprotein B, respectively. The effect of each protein on vesicle fusion was correlated with its hydrophobicity. Conclusions : These results suggest that nucleation effector proteins modulate the stability of vesicles and, thus, affect cholesterol crystallization. Such modulation is based upon protein–vesicle association, which defines the physico‐chemical metastability of vesicular cholesterol." @default.
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- W2163444925 date "1999-07-01" @default.
- W2163444925 modified "2023-10-16" @default.
- W2163444925 title "Influence of cholesterol crystallization effector proteins on vesicle fusion in supersaturated model bile" @default.
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- W2163444925 doi "https://doi.org/10.1046/j.1440-1746.1999.01933.x" @default.
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