𝔖 Bobbio Scriptorium
✦   LIBER   ✦

A novel mutation in the β-protein coding region of the amyloid β-protein precursor (APP) gene

✍ Scribed by Milagros Balbín; Magnus Abrahamson; Lars Gustafson; Karin Nilsson; Arne Brun; Anders Grubb

Publisher
Springer
Year
1992
Tongue
English
Weight
329 KB
Volume
89
Category
Article
ISSN
0340-6717

No coin nor oath required. For personal study only.

✦ Synopsis

A novel mutation, a C to T transition at base pair 2124 in exon 17 of the amyloid beta-protein precursor (APP) gene, has been identified by direct sequencing of amplified DNA from two Alzheimer's disease (AD) patients. A simple oligonucleotide-hybridization procedure was developed to allow population studies of this DNA variation. The mutation, which is silent at the protein level, was present in 2 out of 12 investigated AD patients, in 1 out of 60 non-AD patients and in 1 out of 30 healthy individuals. The mutation can be used as a new marker for linkage studies involving the APP gene, although more comprehensive population studies are required to determine the status of the mutation as a possible risk factor for the development of AD.

📜 SIMILAR VOLUMES

Amyloid precursor protein mutation E682K
Amyloid precursor protein mutation E682K at the alternative β-secretase cleavage β′-site increases Aβ generation
✍ Lujia Zhou; Nathalie Brouwers; Iryna Benilova; Annelies Vandersteen; Marc Mercke 📂 Article 📅 2011 🏛 John Wiley and Sons 🌐 English ⚖ 820 KB

BACE1 cleaves the amyloid precursor protein (APP) at the b-cleavage site (Met 671 -Asp 672 ) to initiate the generation of amyloid peptide Ab. BACE1 is also known to cleave APP at a much less well-characterized b 0 -cleavage site (Tyr 681 -Glu 682 ). We describe here the identification of a novel AP

Intracellular trafficking of the β-secre
Intracellular trafficking of the β-secretase and processing of amyloid precursor protein
✍ Pei Zhi; Cheryl Chia; Paul A. Gleeson 📂 Article 📅 2011 🏛 John Wiley and Sons 🌐 English ⚖ 354 KB

The main component of the amyloid plaques found in the brains of those with Alzheimer's disease (AD) is a polymerized form of the b-amyloid peptide (Ab) and is considered to play a central role in the pathogenesis of this neurodegenerative disorder. Ab is derived from the proteolytic processing of t