App Structure, Dimerization and Processing
نویسندگان
چکیده
APP is a type I transmembrane protein. Its cleavage in the amyloidogenic pathway by βand γ-secretases produces the β-amyloid peptide (Aβ), the major constituent of senile plaques. In addition, the cleavage of the membrane-bound APP C-terminal fragments (CTFs) by γ-secretase releases the AICD (APP Intracellular Cterminal Domain), a soluble intracellular protein believed to control APP-dependent signal transduction and nuclear signalling. Together, this strongly supports the view that APP processing and APP function are interconnected and that the γ-secretase cleavage play a crucial role in the onset and progression of AD
منابع مشابه
Analysis by a highly sensitive split luciferase assay of the regions involved in APP dimerization and its impact on processing
Alzheimer's disease (AD) is a neurodegenerative disease that causes progressive loss of cognitive functions, leading to dementia. Two types of lesions are found in AD brains: neurofibrillary tangles and senile plaques. The latter are composed mainly of the β-amyloid peptide (Aβ) generated by amyloidogenic processing of the amyloid precursor protein (APP). Several studies have suggested that dim...
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The amyloid β precursor protein (APP) is a single-pass transmembrane glycoprotein that is ubiquitously expressed in many cell types, including neurons. Amyloidogenic processing of APP by β- and γ-secretases leads to the production of amyloid-β (Aβ) peptides that can oligomerize and aggregate into amyloid plaques, a characteristic hallmark of Alzheimer's disease (AD) brains. Multiple reports sug...
متن کاملAmyloidogenic processing but not amyloid precursor protein (APP) intracellular C-terminal domain production requires a precisely oriented APP dimer assembled by transmembrane GXXXG motifs.
The beta-amyloid peptide (Abeta) is the major constituent of the amyloid core of senile plaques found in the brain of patients with Alzheimer disease. Abeta is produced by the sequential cleavage of the amyloid precursor protein (APP) by beta- and gamma-secretases. Cleavage of APP by gamma-secretase also generates the APP intracellular C-terminal domain (AICD) peptide, which might be involved i...
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Processing of the amyloid precursor protein (APP) by beta- and gamma-secretases leads to the generation of amyloid-beta (Abeta) peptides with varying lengths. Particularly Abeta42 contributes to cytotoxicity and amyloid accumulation in Alzheimer's disease (AD). However, the precise molecular mechanism of Abeta42 generation has remained unclear. Here, we show that an amino-acid motif GxxxG withi...
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APP is a type I transmembrane protein. Its cleavage in the amyloidogenic pathway by βand γsecretases produces the β-amyloid peptide (Aβ), the major constituent of senile plaques. In addition, the cleavage of the membrane-bound APP C-terminal fragments (CTFs) by γ-secretase releases the AICD (APP Intracellular Cterminal Domain), a soluble intracellular protein believed to control APP-dependent s...
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