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Interaction of cholesterol-crystallization-promoting proteins with vesicles
M A de Bruijn1, B G Goldhoorn, A I Zijlstra
1Division of Gastrointestinal and Liver Diseases, Academic Medical Centre, Amsterdam, The Netherlands.
The Biochemical Journal
|January 1, 1995
Summary
Bile proteins destabilize cholesterol vesicles, causing leakage rather than fusion or aggregation. This disruption, not fusion, appears to precede cholesterol crystallization in bile.
Area of Science:
- Biochemistry
- Molecular Biology
- Cell Biology
Background:
- Cholesterol crystallization in bile is a significant factor in gallstone formation.
- The precise mechanism by which biliary proteins influence cholesterol crystallization remains incompletely understood.
Purpose of the Study:
- To investigate the interaction of human biliary proteins with cholesterol/phospholipid vesicles.
- To determine if protein-induced vesicle fusion or aggregation is involved in cholesterol crystallization.
Main Methods:
- Utilized resonance energy transfer assays to monitor vesicle interactions.
- Assessed vesicle destabilization by measuring carboxyfluorescein leakage.
- Correlated vesicle leakage with nucleation-promoting activity of biliary proteins.
Main Results:
- No significant protein-induced fusion or aggregation of cholesterol/phospholipid vesicles was observed.
- Biliary proteins induced destabilization and leakage of entrapped molecules from vesicles.
- A strong positive correlation was found between vesicle leakage and nucleation-promoting activity.
Conclusions:
- Vesicle aggregation or fusion is not a necessary step preceding cholesterol crystallization.
- Biliary protein-induced cholesterol crystallization appears to be preceded by vesicle disruption.