A prion-derived peptide can protect SH-SY۵Y neuroblestoma cells against Aβ۴۲ oligomer cytotoxicity without interaction between the twopeptides

Backgrounds: Alzheimer's disease (AD) is a prevalent and progressive neurodegenerativedisease. The cellular prion protein (PrPC) is a glycoprotein that mostly located at the outersurface of the cell membrane and can act as a high affinity receptor for oligomeric Aβ. Mutationin the PRNP gene can change the kinetics of PrP. In present study, neuroblastoma cells weretreated with Aβ۴۲ oligomers (ADDLs) with and without PrP۱۰۷-۱۲۰ and the level of viability of cellwas investigated. We also assessed the interaction between the two peptidesMaterials and Methods: Cell viability was assessed by MTT assay. To investigate theinteraction between PrP۱۰۷-۱۲۰ and Aβ۴۲ ADDLs, cells were cultured on glass coverslips then weretreated with various sample (Aβ۴۲ ADDLs, Aβ۴۲ ADDLs + labelled PrP۱۰۷-۱۲۰ and labelled PrP۱۰۷-۱۲۰). PrP۱۰۷-۱۲۰ was labelled with BODIPY TMR-X NHS Ester, Aβ۴۲ ADDLs with mousemonoclonal primary antibody ۶E۱۰ and secondary antibody, and the nuclei with the Hoechstdye. Cells were imaged using a TCS SP۸ confocal microscope.Results: The present study shows that cytotoxicity of Aβ۴۲ ADDLs was strongly reduced whenthe SH-SY۵Y neuroblastoma cells were treated with ADDLs in the presence of PrP۱۰۷-۱۲۰.Surprisingly, no apparent co-localization between PrP۱۰۷-۱۲۰ and ADDLs was seen in confocalmicroscopy images.Conclusion: These data suggest that viability of neuroblastoma cells exposed to ADDLs withPrP۱۰۷-۱۲۰ was increased compared to the cells treated with ADDLs alone, although PrP۱۰۷-۱۲۰ didnot show any interaction with ADDLs.

کلیدواژه ها:

Alzheimer's disease ، ADDLs ، Cellular prion peptide ، Receptor ، PRNP gene