GGA1 Acts as a Spatial Switch Altering Amyloid Precursor Protein Trafficking and Processing
نویسندگان
چکیده
منابع مشابه
GGA1 acts as a spatial switch altering amyloid precursor protein trafficking and processing.
The beta-amyloid (Abeta) precursor protein (APP) is cleaved sequentially by beta-site of APP-cleaving enzyme (BACE) and gamma-secretase to release the Abeta peptides that accumulate in plaques in Alzheimer's disease (AD). GGA1, a member of the Golgi-localized gamma-ear-containing ARF-binding (GGA) protein family, interacts with BACE and influences its subcellular distribution. We now report tha...
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Intracellular trafficking and proteolytic processing of amyloid precursor protein (APP) have been the focus of numerous investigations over the past two decades. APP is the precursor to the amyloid beta-protein (Abeta), the 38-43-amino acid residue peptide that is at the heart of the amyloid cascade hypothesis of Alzheimer disease (AD). Tremendous progress has been made since the initial identi...
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The amyloid precursor protein (APP) is implied both in cell growth and differentiation and in neurodegenerative processes in Alzheimer disease. Regulated proteolysis of APP generates biologically active fragments such as the neuroprotective secreted ectodomain sAPPalpha and the neurotoxic beta-amyloid peptide. Furthermore, it has been suggested that the intact transmembrane APP plays a signalin...
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Background: Amyloid precursor protein (APP) undergoes cleavage under physiological conditions, predominantly by αand γ-secretases, to form the nonpathogenic sAPPα and p3 fragments. By contrast, amyloid-beta (Aβ) is produced via proteolytic cleavage by βand γ-secretases. In Alzheimer’s disease (AD), APP is preferentially processed via the amyloidogenic pathway, producing large amounts of Aβ that...
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ژورنال
عنوان ژورنال: Journal of Neuroscience
سال: 2006
ISSN: 0270-6474,1529-2401
DOI: 10.1523/jneurosci.2290-06.2006