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dc.contributor.authorO'Donnell, Amanda Raeen_US
dc.date.accessioned2016-03-01T14:52:54Z
dc.date.available2016-03-01T14:52:54Z
dc.date.issued2014
dc.identifier.urihttps://hdl.handle.net/2144/14661
dc.description.abstractAlzheimer's disease is a neurodegenerative disease characterized by plaques of amyloid-beta protein (Aβ) and neurofibrillary tangles of the microtubule-associated protein tau. Plaques contain several variants of Aβ, including full-length Aβ1-40 and Aβ1-42, and N-terminally truncated and cyclized pyroglutamate-3 (pE3) Aβ. In particular, pE3 Aβ has been shown to be extremely toxic and resistant to degradation. Microglia are phagocytic cells in the brain that have been shown to take up and degrade Aβ. The purpose of this study is to compare the uptake and degradation of three different Aβ variants: Aβ1-40, Aβ3-40, and AβpE3-40 using both primary murine microglia and N9 microglia, a murine microglial cell line. The three techniques used to discern the differences in uptake and degradation are fluorescence-activated cell sorting, immunofluorescence, and Western blot. According to these techniques, primary microglia and N9 microglia take up and degrade the three Aβ variants differently. Overall, N9 cells appear to prefer to take up and degradeAβ1-40, whereas primary microglia prefer to take up AβpE3-40 and degrade Aβ1-40.en_US
dc.language.isoen_US
dc.subjectNeurosciencesen_US
dc.titleIn vitro uptake of different N-terminal variants of the beta-amyloid peptide by murine microgliaen_US
dc.typeThesis/Dissertationen_US
dc.date.updated2016-01-22T18:57:10Z
etd.degree.nameMaster of Scienceen_US
etd.degree.levelmastersen_US
etd.degree.disciplineMedical Sciencesen_US
etd.degree.grantorBoston Universityen_US


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