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Amyloid- Receptors: The Good, the Bad, and the Prion Protein

期刊

JOURNAL OF BIOLOGICAL CHEMISTRY
卷 291, 期 7, 页码 3174-3183

出版社

AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.R115.702704

关键词

Alzheimer disease; amyloid; oligomer; prion; receptor

资金

  1. Alzheimer's Research UK [PG2013-12]
  2. Biotechnology and Biological Sciences Research Council
  3. Dr. Donald Dean Fund in Dementia Research
  4. University of Manchester
  5. Alzheimers Research UK [ARUK-PG2013-12] Funding Source: researchfish
  6. Biotechnology and Biological Sciences Research Council [1360639] Funding Source: researchfish
  7. MRC [MR/L023784/1, MR/L023784/2] Funding Source: UKRI

向作者/读者索取更多资源

Several different receptor proteins have been identified that bind monomeric, oligomeric, or fibrillar forms of amyloid- (A). Good receptors internalize A or promote its transcytosis out of the brain, whereas bad receptors bind oligomeric forms of A that are largely responsible for the synapticloss, memory impairments, and neurotoxicity that underlie Alzheimer disease. The prion protein both removes A from the brain and transduces the toxic actions of A. The clustering of distinct receptors in cell surface signaling platforms likely underlies the actions of distinct oligomeric species of A. These A receptor-signaling platforms provide opportunities for therapeutic intervention in Alzheimer disease.

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