Analysis by a highly sensitive split luciferase assay of the regions involved in APP dimerization and its impact on processing
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- 作者：Marie Decocka ; Laetitia El Haylania ; Serena Stangaa ; Ilse Dewachtera ; Jean-Noë ; l Octavea ; Steven O. Smithb ; Stefan N. Constantinescuc ; Pascal Kienlen-Camparda ; pascal.kienlen-campard@uclouvain.be" class="auth_mail" title="E-mail the corresponding author
- 关键词：Aβ ; β-amyloid peptide ; AD ; Alzheimer&rsquo ; s disease ; APP ; amyloid precursor protein ; AICD ; APP intracellular domain ; sAPPα ; soluble APPα ; sAPPβ ; soluble APPβ ; CHO ; chinese hamster ovary ; CTF ; C-terminal fragment ; DAPT ; N-[N-(3 ; 5-difluorophenacetyl)-l-alanyl]-S-phenylglycine t-butyl ester ; DTT ; dithiothreitol ; ECL ; enzymatic chemi-luminescence ; ECLIA ; electro-chemiluminescence immuno-assay ; FBS ; fetal bovine serum ; FRET ; fluorescence resonance energy transfer ; KPI ; Kunitz-type protease inhibitor
- 刊名：FEBS Open Bio
- 出版年：2015
- 出版时间：2015
- 年：2015
- 卷：5
- 期：Complete
- 页码：763-773
- 全文大小：2234 K
文摘
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Amyloid precursor protein (APP) dimerizes more than its C-terminal fragments in cells.
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Mutations of membrane GXXXG motifs affect Aβ production but not APP dimerization.
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Deletion of the APP intracellular domain increases APP dimerization.