The functional γ-secretase inhibitor prevents production of amyloid β 1–34 in human and murine cell lines
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2019, Journal of Neuroscience MethodsAre N- And C-terminally truncated A β species key pathological triggers in Alzheimer's disease?
2018, Journal of Biological ChemistryAstrocytes and microglia but not neurons preferentially generate N-terminally truncated Aβ peptides
2015, Neurobiology of DiseaseCitation Excerpt :Additionally an association between Aβ NpE-x and hyperphosphorylated tau was demonstrated in human brain tissue and the severity of AD neuropathology correlated with frontal NpE-Aβ load, indicating a potential role of this N-terminal truncated Aβ for the initiation and progress of AD (Mandler et al., 2014). In cell culture supernatant, CSF, and blood plasma, the most abundant Aβ peptide variant is Aβ 1-40 (Wang et al., 1996; Vandermeeren et al., 2001; Esselmann et al., 2004; Maler et al., 2007; Haussmann et al., 2013). CSF predominantly contains Aβ peptides that begin at Asp1; in human blood plasma, a high proportion of N-terminally modified Aβ peptides has been detected (Lewczuk et al., 2004; Maler et al., 2007).
Study on Aβ34 biology and detection in transgenic mice brains
2014, Neurobiology of AgingCitation Excerpt :Interestingly, the latter cleavage was enhanced by BACE1 overexpression and prevented by selective γ-secretase inhibitors. This indicates that Aβ34 production by BACE1 was strictly dependent upon prior generation of Aβ by γ-secretase, in agreement with the observation that Aβ34 species cannot be produced directly from C99 (Fluhrer et al., 2003; Shi et al., 2003; Vandermeeren, et al., 2001). Despite previous observation of Aβ1-34 peptide in vitro and in vivo (Fluhrer et al., 2003; Maddalena et al., 2004; Shi et al., 2003; Vandermeeren et al., 2001; Wang et al., 1996), the function and fate of such a species as well as its impact on AD pathogenesis remains unknown.
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