维登二醇 - A抑制胆固醇酯与其转运蛋白的结合。
Wiedendiol-A inhibits cholesteryl ester binding to its transfer protein.
作者信息
Wang S, Clemmons A, Chackalamannil S, Coval S J, Sybertz E, Burrier R
机构信息
Department of CNS/CV Biological Research, Schering-Plough Research Institute, Kenilworth, NJ 07033, USA.
出版信息
Zhongguo Yao Li Xue Bao. 1998 Sep;19(5):408-12.
AIM
To study the wiedendiol-A (W-A) inhibition mechanism of plasma cholesteryl ester (CE) transfer protein (CETP) on the transfer of CE.
METHODS
Using gel filtration method.
RESULTS
W-A at 30 mumol.L-1 inhibited association of CE with CETP by 76% and CETP transfer activity by 81%. In addition, W-A enhanced binding of TP2, a monoclonal antibody with a CETP C-terminal epitope which is involved in CE binding, to CETP, suggesting a W-A-induced conformational change at the epitope for increased TP2 binding. When CETP activity was measured by varying high-density lipoproteins (HDL) concentration, the apparent Vmax of CE transfer was inhibited by 74% and 83% in the presence of W-A at 14 and 25 mumol.L-1, respectively, while the apparent K(m) of HDL for CETP did not change.
CONCLUSION
W-A action is mediated through interaction between W-A and CETP, but not through those between W-A and lipoproteins.
目的
研究维登二醇-A（W-A）对血浆胆固醇酯（CE）转移蛋白（CETP）介导的CE转移的抑制机制。
方法
采用凝胶过滤法。
结果
30μmol·L-1的W-A可使CE与CETP的结合减少76%，CETP的转移活性降低81%。此外，W-A增强了TP2（一种针对CETP C末端表位的单克隆抗体，该表位参与CE结合）与CETP的结合，提示W-A诱导了表位的构象变化，从而增加了TP2的结合。当通过改变高密度脂蛋白（HDL）浓度来测定CETP活性时，在14μmol·L-1和25μmol·L-1的W-A存在下，CE转移的表观Vmax分别被抑制了74%和83%，而HDL对CETP的表观K(m)未发生变化。
结论
W-A的作用是通过W-A与CETP之间的相互作用介导的，而非通过W-A与脂蛋白之间的相互作用。
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