Influence of cholesterol crystallization effector proteins on vesicle fusion in supersaturated model bile
| Autor: | Yoshihiro Hattori, Goro Kajiyama, Gunji Yamashita, Susumu Tazuma |
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| Rok vydání: | 1999 |
| Předmět: |
Time Factors
Vesicle fusion Apolipoprotein B Phospholipid Immunoglobulins Membrane Fusion Models Biological Receptors Concanavalin A chemistry.chemical_compound Bile Humans Apolipoproteins B Fluorescent Dyes chemistry.chemical_classification Liposome Apolipoprotein A-I Hepatology biology Rhodamines Effector Cholesterol Vesicle Gastroenterology Proteins chemistry Biochemistry Liposomes biology.protein lipids (amino acids peptides and proteins) Crystallization Glycoprotein |
| Zdroj: | Journal of Gastroenterology and Hepatology. 14:669-674 |
| ISSN: | 1440-1746 0815-9319 |
| DOI: | 10.1046/j.1440-1746.1999.01933.x |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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