Generation of aggregation prone N-terminally truncated amyloid β peptides by meprin β depends on the sequence specificity at the cleavage site
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- 作者：Caroline Schönherr ; Jessica Bien ; Simone Isbert…
- 关键词：Alzheimer’s Disease ; Meprin β ; Metalloprotease ; Amyloid precursor protein ; Amyloid β ; N ; terminal truncation ; APP mutations ; Protein ; protein interaction ; Cell surface protein
- 刊名：Molecular Neurodegeneration
- 出版年：2016
- 出版时间：December 2016
- 年：2016
- 卷：11
- 期：1
- 全文大小：1,784 KB
- 刊物主题：Neurosciences; Neurology; Molecular Medicine;
- 出版者：BioMed Central
- ISSN：1750-1326
文摘
Background The metalloprotease meprin β cleaves the Alzheimer’s Disease (AD) relevant amyloid precursor protein (APP) as a β-secretase reminiscent of BACE-1, however, predominantly generating N-terminally truncated Aβ2-x variants.