scholarly journals Effects of prolonged angiotensin-converting enzyme inhibitor treatment on amyloid β-protein metabolism in mouse models of Alzheimer disease

2007 ◽  
Vol 26 (1) ◽  
pp. 273-281 ◽  
Author(s):  
Matthew L. Hemming ◽  
Dennis J. Selkoe ◽  
Wesley Farris
Keyword(s):  
Alzheimer Disease ◽  
Angiotensin Converting Enzyme ◽  
Mouse Models ◽  
Protein Metabolism ◽  
Enzyme Inhibitor ◽  
Amyloid Β ◽  
Amyloid Β Protein ◽  
Converting Enzyme ◽  
Β Protein ◽  
Inhibitor Treatment

scholarly journals Amyloid-β protein modulates the perivascular clearance of neuronal apolipoprotein E in mouse models of Alzheimer’s disease

2011 ◽  
Vol 118 (5) ◽  
pp. 699-712 ◽  
Author(s):  
Harshvardhan Rolyan ◽  
Ann Caroline Feike ◽  
Ajeet Rijal Upadhaya ◽  
Andreas Waha ◽  
Tom Van Dooren ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Apolipoprotein E ◽  
Mouse Models ◽  
Amyloid Β ◽  
Amyloid Β Protein ◽  
Β Protein

scholarly journals Isolation and Characterization of Patient-derived, Toxic, High Mass Amyloid β-Protein (Aβ) Assembly from Alzheimer Disease Brains

2009 ◽  
Vol 284 (47) ◽  
pp. 32895-32905 ◽  
Author(s):  
Akihiko Noguchi ◽  
Satoko Matsumura ◽  
Mari Dezawa ◽  
Mari Tada ◽  
Masako Yanazawa ◽  
...  
Keyword(s):  
Alzheimer Disease ◽  
Amyloid Β ◽  
High Mass ◽  
Amyloid Β Protein ◽  
Isolation And Characterization ◽  
Β Protein

scholarly journals The Tottori (D7N) and English (H6R) Familial Alzheimer Disease Mutations Accelerate Aβ Fibril Formation without Increasing Protofibril Formation

2006 ◽  
Vol 282 (7) ◽  
pp. 4916-4923 ◽  
Author(s):  
Yukiko Hori ◽  
Tadafumi Hashimoto ◽  
Yosuke Wakutani ◽  
Katsuya Urakami ◽  
Kenji Nakashima ◽  
...  
Keyword(s):  
Alzheimer Disease ◽  
Amyloid Fibril ◽  
Amyloid Β ◽  
Fibril Formation ◽  
Amyloid Β Protein ◽  
Protein Precursor ◽  
Amyloid Fibril Formation ◽  
Β Protein ◽  
Familial Alzheimer Disease ◽  
Aβ Production

A subset of Alzheimer disease cases is caused by autosomal dominant mutations in genes encoding the amyloid β-protein precursor or presenilins. Whereas some amyloid β-protein precursor mutations alter its metabolism through effects on Aβ production, the pathogenic effects of those that alter amino acid residues within the Aβ sequence are not fully understood. Here we examined the biophysical effects of two recently described intra-Aβ mutations linked to early-onset familial Alzheimer disease, the D7N Tottori-Japanese and H6R English mutations. Although these mutations do not affect Aβ production, synthetic Aβ(1-42) peptides carrying D7N or H6R substitutions show enhanced fibril formation. In vitro analysis using Aβ(1-40)-based mutant peptides reveal that D7N or H6R mutations do not accelerate the nucleation phase but selectively promote the elongation phase of amyloid fibril formation. Notably, the levels of protofibrils generated from D7N or H6R Aβ were markedly inhibited despite enhanced fibril formation. These N-terminal Aβ mutations may accelerate amyloid fibril formation by a unique mechanism causing structural changes of Aβ peptides, specifically promoting the elongation process of amyloid fibrils without increasing metastable intermediates.

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