The Carboxyl Termini of β-Amyloid Peptides 1-40 and 1-42 Are Generated by Distinct γ-Secretase Activities
نویسندگان
چکیده
منابع مشابه
Molecular mechanism of the intramembrane cleavage of the β-carboxyl terminal fragment of amyloid precursor protein by γ-secretase
Amyloid β-protein (Aβ) plays a central role in the pathogenesis of Alzheimer's disease, the most common age-associated neurodegenerative disorder. Aβ is generated through intramembrane proteolysis of the β-carboxyl terminal fragment (βCTF) of β-amyloid precursor protein (APP) by γ-secretase. The initial cleavage by γ-secretase occurs in the membrane/cytoplasm boundary of the βCTF, liberating th...
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Two main amyloid-β peptides of different length (Aβ40 and Aβ42) are involved in Alzheimer's disease. Their relative abundance is decisive for the severity of the disease and mixed oligomers may contribute to the toxic species. However, little is know about the extent of mixing. To study whether Aβ40 and Aβ42 co-aggregate, we used Fourier transform infrared spectroscopy in combination with 13C-l...
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Department of Chemistry Case Western Reserve University, Cleveland OH 44106, USA The amyloid b-peptide is the major protein constituent of neuritic plaques in Alzheimer's disease. The b-peptide varies slightly in length and exists in two predominant forms: (1) the shorter, 40 residue b-(1-40), found mainly in cerebrovascular amyloid; and (2) the longer, 42 residue b-(1-42), which is the major c...
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Alzheimer's disease (AD) is characterized pathologically by an abundance of extracellular neuritic plaques composed primarily of the 42-amino acid amyloid β peptide variant (Aβ42). In the majority of familial AD (FAD) cases, e.g., those harboring mutations in presenilin 1 (PS1), there is a relative increase in the levels of Aβ42 compared to the levels of Aβ40. We previously reported the charact...
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Amyloid β-protein (Aβ) is central to the pathology of Alzheimer's disease. A 5% difference in the primary structure of the two predominant alloforms, Aβ(1-40) and Aβ(1-42), results in distinct assembly pathways and toxicity properties. Discrete molecular dynamics (DMD) studies of Aβ(1-40) and Aβ(1-42) assembly resulted in alloform-specific oligomer size distributions consistent with experimenta...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1996
ISSN: 0021-9258
DOI: 10.1074/jbc.271.45.28655