Dextran sulfate sodium inhibits amyloid-β oligomer binding to cellular prion protein

Takahiro Aimi, Koichiro Suzuki, Tatsuya Hoshino, Tohru Mizushima

Research output: Contribution to journalArticlepeer-review

9 Citations (Scopus)


Amyloid-β peptide (Aβ), especially its oligomeric form, is believed to play an important role in the pathogenesis of Alzheimer's disease (AD). To this end, the binding of Aβ oligomer to cellular prion protein (PrPC) plays an important role in synaptic dysfunction in a mouse model of AD. Here, we have screened for compounds that inhibit Aβ oligomer binding to PrPC from medicines already used clinically (Mizushima Approved Medicine Library 1), and identified dextran sulfate sodium (DSS) as a candidate. In a cell-free assay, DSS inhibited Aβ oligomer binding to PrPC but not to ephrin receptor B2, another endogenous receptor for Aβ oligomers, suggesting that the drug's action is specific to the binding of Aβ oligomer to PrPC. Dextran on the other hand did not affect this binding. DSS also suppressed Aβ oligomer binding to cells expressing PrPC but not to control cells. Furthermore, while incubation of mouse hippocampal slices with Aβ oligomers inhibited the induction of long-term potentiation, simultaneous treatment with DSS restored the long-term potentiation. As DSS has already been approved for use in patients with hypertriglyceridemia, and its safety in humans has been confirmed, we propose further analysis of this drug as a candidate for AD treatment.

Original languageEnglish
Pages (from-to)611-617
Number of pages7
JournalJournal of Neurochemistry
Issue number4
Publication statusPublished - 2015 Aug 1


  • Alzheimer's disease
  • amyloid beta
  • cellular prion protein
  • dextran sulfate sodium

ASJC Scopus subject areas

  • Biochemistry
  • Cellular and Molecular Neuroscience


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