Regular ArticleSublethal Concentrations of Prion Peptide PrP106–126 or the Amyloid Beta Peptide of Alzheimer's Disease Activates Expression of Proapoptotic Markers in Primary Cortical Neurons
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Stereospecific interactions are necessary for Alzheimer disease amyloid-β toxicity
2011, Neurobiology of AgingA role for p53 in the β-amyloid-mediated regulation of the lysosomal system
2010, Neurobiology of AgingCitation Excerpt :While the 1–42 fibrillar form of Aβ is the most abundant in the AD senile plaque, the 1–40 peptide also has the proclivity to form fibrils and is present in the senile plaque, although to a lesser extent than the 1–42 species (Iwatsubo et al., 1994). In support of the hypothesis that Aβ deposition drives the neurodegenerative process, both Aβ1–40 and Aβ1–42 have been shown to induce neuronal apoptosis in vitro (Troy et al., 2000; White et al., 2001). Several mechanisms for Aβ-mediated neurotoxicity have been proposed, including activation of the proteases, caspase-3 (Uetsuki et al., 1999), caspase-2 (Troy et al., 2000), caspase 4 (Hitami et al., 2004), caspase-12 (Nakagawa et al., 2000) and the Ca2+-activated protease, calpain (Boland and Campbell, 2003).
Microcebus murinus retina: A new model to assess prion-related neurotoxicity in primates
2010, Neurobiology of DiseaseCitation Excerpt :After 15 days, 80 µM of human PrP106–126, or its scrambled form, was added to the culture medium for 10 days. The 80 µM concentration was selected as it has been described as the lowest toxic concentration in primary neuronal cultures (White et al., 2001). Culture solutions and PrP peptides were changed every 3–4 days.
Increased oxidation, glycoxidation, and lipoxidation of brain proteins in prion disease
2008, Free Radical Biology and MedicinePotential therapeutic targets of huperzine A for Alzheimer's disease and vascular dementia
2008, Chemico-Biological InteractionsCitation Excerpt :Other than oxidative stress, apoptosis is also believed to be an important contributor to the progression of AD and mediating Aβ neurotoxicity. There is considerable evidence showing that Aβ can activate intracellular apoptosis pathways [39,40], since application of Aβ to cells could up-regulate apoptotic relative protein Caspase-3 [41] and annexin [42], and eventually causes apoptosis [43]. The cellular commitment to apoptosis is regulated by the Bcl-2 family of proteins.
Fibrillar prion peptide PrP(106-126) treatment induces Dab1 phosphorylation and impairs APP processing and Aβ production in cortical neurons
2008, Neurobiology of DiseaseCitation Excerpt :Thus, prion protein fragments (i.e., PrP(106–126)) that aggregate and interact with the plasma membrane have been used as models of prion neurotoxicity, although they cannot be considered an equivalent of PrPres in other functions such as replication or infectivity (i.e., Kourie, 2001). Indeed, prolonged exposure of primary cortical cultures (e.g., Gavin et al., 2005; White et al., 2001) or cell lines (Perez et al., 2003; Thellung et al., 2002) to PrP(106–126) activates intracellular proapoptotic caspases, which leads to cell death. However, although Aβ and PrP(106–126) peptides may generate neurotoxic products in affected cells (Forloni, 1996), little is known about crosstalk between APP processing and prion-mediated intracellular responses.
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