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- W2011465322 abstract "γ-Secretase is a widely expressed multisubunit enzyme complex which is involved in the pathogenesis of Alzheimer disease and hematopoietic malignancies through its aberrant processing of the amyloid precursor protein (APP) and Notch1, respectively. While γ-secretase has been extensively studied, there is a dearth of information surrounding the activity, composition, and function of γ-secretase expressed in distinct cellular populations. Here we show that endogenous γ-secretase complexes of hematopoietic origin are distinct from epithelial derived γ-secretase complexes. Hematopoietic γ-secretase has reduced activity for APP and Notch1 processing compared to epithelial γ-secretase. Characterization of the active complexes with small molecule affinity probes reveals that hematopoietic γ-secretase has an atypical subunit composition with significantly altered subunit stoichiometry. Furthermore, we demonstrate that these discrete complexes exhibit cell-line specific substrate selectivity suggesting a possible mechanism of substrate regulation. These data underscore the need for studying endogenous γ-secretase to fully understand of the biology of γ-secretase and its complexity as a molecular target for the development of disease therapeutics." @default.
- W2011465322 created "2016-06-24" @default.
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- W2011465322 date "2010-03-10" @default.
- W2011465322 modified "2023-10-16" @default.
- W2011465322 title "Characterization of an Atypical γ-Secretase Complex from Hematopoietic Origin" @default.
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- W2011465322 doi "https://doi.org/10.1021/bi901388t" @default.
- W2011465322 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2880330" @default.
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