Amyloid-β Receptors: The Good, the Bad, and the Prion Protein
| Autor: | Jo V. Rushworth, Nigel M. Hooper, Heledd H. Jarosz-Griffiths, Elizabeth Noble |
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| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Amyloid receptor Receptor for Advanced Glycation End Products Apoptosis Nerve Tissue Proteins Receptors Cell Surface Protein aggregation Biology Ligands Models Biological Protein Aggregation Pathological Receptors N-Methyl-D-Aspartate Biochemistry oligomer prion Protein Aggregates 03 medical and health sciences 0302 clinical medicine Alzheimer Disease medicine Animals Humans Protein Isoforms PrPC Proteins Molecular Targeted Therapy Receptor Molecular Biology Nootropic Agents Neurons Receptor Aggregation Amyloid beta-Peptides Neurotoxicity amyloid Minireviews Cell Biology medicine.disease Cell biology 030104 developmental biology Transcytosis Alzheimer's disease Signal transduction Low Density Lipoprotein Receptor-Related Protein-1 030217 neurology & neurosurgery Signal Transduction |
| Zdroj: | The Journal of Biological Chemistry |
| ISSN: | 0021-9258 |
| Popis: | Several different receptor proteins have been identified that bind monomeric, oligomeric, or fibrillar forms of amyloid-β (Aβ). "Good" receptors internalize Aβ or promote its transcytosis out of the brain, whereas "bad" receptors bind oligomeric forms of Aβ that are largely responsible for the synapticloss, memory impairments, and neurotoxicity that underlie Alzheimer disease. The prion protein both removes Aβ from the brain and transduces the toxic actions of Aβ. The clustering of distinct receptors in cell surface signaling platforms likely underlies the actions of distinct oligomeric species of Aβ. These Aβ receptor-signaling platforms provide opportunities for therapeutic intervention in Alzheimer disease. |
| Databáze: | OpenAIRE |
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