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Neurodegenerative disorders

A PIR-fect storm

Nature Reviews Neuroscience volume 14, page 741 (2013)Cite this article

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Amyloid-β oligomers impair synaptic plasticity in vitro and in vivo, and several receptors for amyloid-β may mediate this effect. The authors assessed whether PIRB might be one such receptor, because they had previously shown that mice lacking PIRB have enhanced ocular dominance plasticity, whereas this form of plasticity is reduced in the transgenic APP/PS1 mouse model of Alzheimer's disease.

The authors first showed that human amyloid-β oligomers, but not monomers, could bind to both PIRB-expressing cells and LILRB2-expressing cells with a high (nanomolar) affinity, and that this binding required the two most amino-terminal immunoglobulin domains of the receptors.

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References

  1. Kim, T. et al. Human LilrB2 is a β-amyloid receptor and its murine homolog PirB regulates synaptic plasticity in an Alzheimer's model. Science 341, 1399–1404 (2013)

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  1. Leonie Welberg
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Welberg, L. A PIR-fect storm. Nat Rev Neurosci 14, 741 (2013). https://doi.org/10.1038/nrn3616

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