胆固醇结晶促进蛋白与囊泡的相互作用。
Interaction of cholesterol-crystallization-promoting proteins with vesicles.
作者信息
de Bruijn M A, Goldhoorn B G, Zijlstra A I, Tytgat G N, Groen A K
机构信息
Division of Gastrointestinal and Liver Diseases, Academic Medical Centre, Amsterdam, The Netherlands.
出版信息
Biochem J. 1995 Jan 1;305 ( Pt 1)(Pt 1):93-6. doi: 10.1042/bj3050093.
In this study, the interaction of mucin and concanavalin A-binding proteins isolated from human bile with cholesterol/phospholipid vesicles was investigated. Using resonance energy transfer assays originally developed by Struck, Hoekstra and Pagano [(1981) Biochemistry 20, 4093-4099], no significant protein-induced fusion or aggregation of vesicles was demonstrated. Instead of fusion, these proteins induced destabilization of cholesterol/phospholipid vesicles, as monitored by release of entrapped carboxyfluorescein. A good correlation (rho = 0.81) was obtained between the extent of leakage and the nucleation-promoting activity of the concanavalin A-binding proteins. We conclude that aggregation or fusion of cholesterol/phospholipid vesicles is not an obligatory step in cholesterol crystallization. Biliary protein-induced crystallization seems to be preceded by vesicle disruption.
在本研究中，对从人胆汁中分离出的粘蛋白和伴刀豆球蛋白A结合蛋白与胆固醇/磷脂囊泡之间的相互作用进行了研究。使用Struck、Hoekstra和Pagano最初开发的共振能量转移测定法[（1981年）《生物化学》20，4093 - 4099]，未证明蛋白质诱导的囊泡融合或聚集。这些蛋白质没有引起融合，而是诱导了胆固醇/磷脂囊泡的不稳定，这通过包封的羧基荧光素的释放来监测。伴刀豆球蛋白A结合蛋白的泄漏程度与成核促进活性之间获得了良好的相关性（rho = 0.81）。我们得出结论，胆固醇/磷脂囊泡的聚集或融合不是胆固醇结晶的必要步骤。胆汁蛋白诱导的结晶似乎先于囊泡破裂。
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