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

被引:186
作者
Jarosz-Griffiths, Heledd H. [1 ]
Noble, Elizabeth [1 ]
Rushworth, Jo V. [2 ]
Hooper, Nigel M. [1 ]
机构
[1] Univ Manchester, Inst Brain Behav & Mental Hlth, Fac Med & Human Sci, Manchester M13 9PT, Lancs, England
[2] De Montfort Univ, Fac Hlth & Life Sci, Leicester LE1 9BH, Leics, England
基金
英国生物技术与生命科学研究理事会;
关键词
Alzheimer disease; amyloid; oligomer; prion; receptor; A-BETA OLIGOMERS; ALZHEIMERS-DISEASE BRAIN; SYNAPTIC PLASTICITY; APOLIPOPROTEIN-E; MEMORY IMPAIRMENT; CLEARANCE; PEPTIDE; FIBRILS; INHIBITION; PATHWAY;
D O I
10.1074/jbc.R115.702704
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:3174 / 3183
页数:10
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