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Alzheimer's disease

The ins and outs of amyloid-β

Nature volume 389, pages 677–678 (1997)Cite this article

The devastating consequences of Alzheimer's disease — marked by extracellular senile plaques with fibrils of amyloid-β peptide (Aβ) and intraneuronal tangles of polymerized tau protein — are experienced by more and more elderly people in the Western world. The latest step towards understanding the underlying causes is reported by Yan et al.1 on page689 of this issue. They have identified a possible mechanism to explain how Aβ could damage neurons, and they show that Aβ interacts with a hitherto unknown endoplasmic-reticulum-associated binding protein, ERAB.

We already have compelling evidence that Aβ may be at the root of neurodegeneration: mutations have been found in three genes — the amyloid precursor-protein (APP) gene on chromosome 21, and the genes for presenilin 1 (PS1) and presenilin 2 (PS2) on chromosomes 14 and 1, respectively — that segregate with rare forms of early-onset autosomal-dominant familial Alzheimer's disease. These mutations result in increased production2 of the APP cleavage product Aβ42, which is a main constituent of plaques but is not found in the paired helical filaments of tangles3,4,5. Moreover, all of the mutations in the APP gene are within the Aβ region. So although Aβ seems to be implicated in neuropathogenesis and neurodegeneration, the missing link revolves around how it interferes with neuronal function and tangle formation.

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Figure 1: Yan et al.1 have identified an endoplasmic-reticulum (ER)-associated binding protein (ERAB) which binds to amyloid-β peptide (Aβ).

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Authors and Affiliations

  1. the ZMBH, University of Heidelberg, Im Neuenheimer Feld 282, D-69120, Heidelberg, Germany

    Konrad Beyreuther

  2. the Department of Pathology, the University of Melbourne, Parkville, 3025, Victoria, Australia

    Colin L. Masters

Authors
  1. Konrad Beyreuther
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  2. Colin L. Masters
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Beyreuther, K., Masters, C. The ins and outs of amyloid-β. Nature 389, 677–678 (1997). https://doi.org/10.1038/39479

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