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• W1979376945 endingPage "316" @default.
• W1979376945 startingPage "309" @default.
• W1979376945 abstract "Doppel (Dpl) protein is a paralog of the prion protein (PrP) that shares 25% sequence similarity with the C-terminus of PrP, a common N-glycosylation site and a C-terminal signal peptide for attachment of a glycosylphophatidyl inositol anchor. Whereas PrP (C) is highly expressed in the central nervous system (CNS), Dpl is detected mostly in testes and its ectopic expression in the CNS leads to ataxia as well as Purkinje and granule cell degeneration in the cerebellum. The mechanism through which Dpl induces neurotoxicity is still debated. In the present work, primary neuronal cultures derived from postnatal cerebellar granule cells of wild-type and PrP-knockout FVB mice were used in order to investigate the molecular events that occur upon exposure to Dpl. Treatment of cultured cerebellar neurons with recombinant Dpl produced apoptosis that could be prevented by PrP co-incubation. When primary neuronal cultures from Bax-deficient mice were incubated with Dpl, no apoptosis was observed, suggesting an important role of Bax in triggering neurodegeneration. Similarly, cell survival increased when recDpl-treated cells were incubated with an inhibitor of caspase-3, which mediates apoptosis in mammalian cells. Together, our findings raise the possibility that Bax and caspase-3 feature in Dpl-mediated apoptosis." @default.
• W1979376945 created "2016-06-24" @default.
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• W1979376945 date "2012-07-01" @default.
• W1979376945 modified "2023-10-02" @default.
• W1979376945 title "The role of Bax and caspase-3 in doppel-induced apoptosis of cerebellar granule cells" @default.
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• W1979376945 doi "https://doi.org/10.4161/pri.20026" @default.
• W1979376945 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3399532" @default.
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