Dependency of γ-secretase complex activity on the structural integrity of the bilayer.
Dependency of γ-secretase complex activity on the structural integrity of the bilayer.
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γ-分泌酶复合物活性对双层结构完整性的依赖性。
DOI：
10.1016/j.bbrc.2010.10.017
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发表时间：
2010
影响因子：
3.1
通讯作者：
Jap,BingK
中科院分区：
文献类型：
--
作者：
Zhou,Hua;Zhou,Shuxia;Walian,PeterJ;Jap,BingK
γ-分泌酶是一种膜蛋白复合体，与A-β多肽的产生有关，这些多肽在阿尔茨海默病中是致病的。我们用电子显微镜表征了γ-分泌酶复合体在各种洗涤剂增溶和重组条件下的活性，以及蛋白质脂质体的结构状态。我们发现γ分泌酶的活性高度依赖于膜双层的物理状态或完整性-部分增溶可能会增加活性，而完全增溶则会取消活性。当适当地重组到脂质双层环境中时，溶解良好的γ分泌酶的活性可以恢复到接近天然水平。
γ-secretase is a membrane protein complex associated with the production of Aβ peptides that are pathogenic in Alzheimer’s disease. We have characterized the activity of γ-secretase complexes under a variety of detergent solubilization and reconstitution conditions, and the structural state of proteoliposomes by electron microscopy. We found that γ-secretase activity is highly dependent on the physical state or integrity of the membrane bilayer – partial solubilization may increase activity while complete solubilization will abolish it. The activity of well-solubilized γ-secretase can be restored to near native levels when properly reconstituted into a lipid bilayer environment.