Alzheimer's disease untangled

Fiona Crawford, Alison Goate

Research output: Contribution to journalReview articlepeer-review

16 Scopus citations

Abstract

The last year has seen major advances in the study of Alzheimer's disease (AD).† Four mutations involving amino acid substitutions in axons 16 and 17 of the amyloid precursor protein (APP) gene, have been identified which co‐segregate with the disease in some families multiply affected by early onset Alzheimer's disease. These mutations are strongly suggestive of a causative role for the amyloid preursor protein in Alzheimer's disease. Despite their rarity, these mutations are important because they represent the first known cause of Alzheimer's disease. Processing of APP must be central to the pathogenesis of the disease although the precise effects of these amino acid substitutions are not understood. Work is now being undertaken to characterise the processing pathways of APP and to identify other causes of AD. The development of models of AD using the APP mutations offers the possibility of identifying drug targets and developing more effective treatments than are presently available.

Original languageEnglish
Pages (from-to)727-734
Number of pages8
JournalBioEssays
Volume14
Issue number11
DOIs
StatePublished - Nov 1992
Externally publishedYes

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