4.6 Review

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

Journal

JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 291, Issue 7, Pages 3174-3183

Publisher

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

Keywords

Alzheimer disease; amyloid; oligomer; prion; receptor

Funding

  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

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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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