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The aggregation or oligomerization of amyloid-β (Aβ) peptide is thought to be the primary causative event in the pathogenesis of Alzheimer's disease (AD). Considerable  in vitro  evidence indicates that the aggregation/oligomerization of Aβ is promoted in the presence of Zn; however, the functional role of Zn in AD pathogenesis is still not well clarified  in vivo . Zn is imported into the brain mainly through the solute-linked carrier ( Slc ) 39 family transporters. Using a genetically tractable  Drosophila  model, we found that the expression of  dZip1 , the orthologue of human  Slc39  family transporter  hZip1  in  Drosophila , was altered in the brains of Aβ42-expressing flies, and Zn homeostasis could be modulated by forcible  dZip1  expression changes. An array of phenotypes associated with Aβ expression could be modified by altering  dZip1  expression. Importantly, Aβ42 fibril deposits as well as its SDS-soluble form were dramatically reduced upon  dZip1  inhibition, resulting in less neurodegeneration, significantly improved cognitive performance, and prolonged lifespan of the Aβ42-transgenic flies. These findings suggest that zinc contributes significantly to the Aβ pathology, and manipulation of zinc transporters in AD brains may provide a novel therapeutic strategy.

Genetic Inhibition of Solute-Linked Carrier 39 Family Transporter 1 Ameliorates Aβ Pathology in a Drosophila Model of Alzheimer's Disease