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- W99576416 abstract "The β-amyloid precursor protein (βAPP) is widely expressed in neurons and glial cells throughout the mammalian nervous system. APP is a large transmembrane glycoprotein having a single transmembrane domain, a large extracelluar N-terminus, and a short cytoplasmic C-terminus (Kang et al., 1987). This protein is very important as a source of amyloid β peptide (Aβ), a 40–42 amino acid peptide that forms senile plaques in Alzheimer’s disease (AD) patient brains. Senile plaques, along with neurofibrillary tangles, are the most characteristic pathological change in AD brains (Alzheimer, 1907). In normal physiological conditions, α-secretase cleaves βAPP between amino acids 16 and 17 of A. The α-secretase cleavage prevents release of amyloidogenic Aβ and yields secreted forms of APP (sAPPα), which are released into the extracellular fluid (Weidemann et al., 1989; Esch et al., 1990; Sisodia et al., 1990). An alternative cleavage of βAPP within the endosomal—lysosomal pathway at the N-terminus of Aβ results in release of intact Aβ and secreted forms of APP without the Aβ1–16 domain (sAPPβ) (Haass et al., 1992; Seubert et al., 1992; Shoji et al., 1992; Busciglio et al., 1993). Previous studies paid great attention to the production and the functions of Aβ, but a regulated release of sAPPα and sAPPβ seems to be equally important (Furukawa et al., 1996b)." @default.
- W99576416 created "2016-06-24" @default.
- W99576416 creator A5047776373 @default.
- W99576416 date "1998-01-01" @default.
- W99576416 modified "2023-09-27" @default.
- W99576416 title "Signaling by β-Amyloid Precursor Protein" @default.
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