Editors' ChoiceNeuroscience

Amyloid Binding Partners

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Science Signaling  24 Sep 2013:
Vol. 6, Issue 294, pp. ec230
DOI: 10.1126/scisignal.2004744

β-Amyloid (Aβ) is critical to the pathology of Alzheimer's disease (AD), but its role in normal physiology remains unclear. Kim et al. (see the Perspective by Benilova and De Strooper) found that murine-paired immunoglobulin-like receptor B (PirB) and its human ortholog, leukocyte immunoglobulin-like receptor B2 (LilrB2), both bound to oligomerized Aβ. Early in mouse development, ocular dominance plasticity was affected by interactions between oligomeric Aβ and PirB. In hippocampal brain slices from a mouse model of AD, reductions in long-term potentiation induced by Aβ required PirB. Furthermore, the memory defects characteristic of a mouse model of AD were dependent on the function of PirB. Many binding partners for Aβ have been identified, and so the extent to which these findings can be exploited therapeutically remains unclear.

T. Kim, G. S. Vidal, M. Djurisic, C. M. William, M. E. Birnbaum, K. C. Garcia, B. T. Hyman, C. J. Shatz, 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). [Abstract] [Full Text]

I. Benilova, B. De Strooper, Promiscuous Alzheimer's amyloid: Yet another partner. Science 341, 1354–1355 (2013). [Abstract] [Full Text]

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