Amyloid precursor protein, although partially detergent-insoluble in mouse cerebral cortex, behaves as an atypical lipid raft protein

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Amyloid precursor protein, although partially detergent-insoluble in mouse cerebral cortex, behaves as an atypical lipid raft protein.

Lipid rafts are regions of the plasma membrane that are enriched in cholesterol, glycosphingolipids and acylated proteins, and which have been proposed as sites for the proteolytic processing of the Alzheimer's amyloid precursor protein (APP). Lipid rafts can be isolated on the basis of their insolubility in Triton X-100 at 4 degrees C, with the resulting low-density, detergent-insoluble glycol...

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Amyloid Precursor Protein

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 -protein (A ), 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 identificatio...

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Amyloidprecursor protein (APP), a type I membrane protein, is physiologically processed by or -secretases that cleave APP N-terminal to the transmembrane region. Extracellular -cleavage of APP generates a large secreted N-terminal fragment, and a smaller cellular C-terminal fragment. Subsequent -secretase cleavage in the transmembrane region of the C-terminal fragment induces secretion of small...

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ژورنال

عنوان ژورنال: Biochemical Journal

سال: 1999

ISSN: 0264-6021,1470-8728

DOI: 10.1042/bj3440023