Seeded strain-like transmission of b-amyloid morphotypes in APP transgenic mice
نویسندگان
چکیده
Götz Heilbronner1,2, Yvonne S. Eisele1,2, Franziska Langer1,2, Stephan A. Kaeser1,2, Renata Novotny1,2,3, Amudha Nagarathinam1,2, Andreas Åslund4, Per Hammarström4, K. Peter R. Nilsson4 & Mathias Jucker1,2+ 1Department ofCellularNeurology,Hertie Institute forClinical BrainResearch,University ofTübingen, Tübingen,Germany, 2DZNE, German Center for Neurodegenerative Diseases, Tübingen, Germany, 3Graduate School of Cellular and Molecular Neuroscience, University of Tübingen, Tübingen, Germany, and 4Department of Chemistry, IFM, Linköping University, Linköping, Sweden
منابع مشابه
Seeded strain-like transmission of β-amyloid morphotypes in APP transgenic mice.
The polymorphic β-amyloid lesions present in individuals with Alzheimer's disease are collectively known as cerebral β-amyloidosis. Amyloid precursor protein (APP) transgenic mouse models similarly develop β-amyloid depositions that differ in morphology, binding of amyloid conformation-sensitive dyes, and Aβ40/Aβ42 peptide ratio. To determine the nature of such β-amyloid morphotypes, β-amyloid-...
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We have studied synaptic function in a transgenic mouse strain relevant to Alzheimer's disease (AD), overexpressing the 695 amino acid isoform of human amyloid precursor protein with K670N and M671L mutations (APP(695)SWE mice), which is associated with early-onset familial AD. Aged-transgenic mice had substantially elevated levels of Abeta (up to 22 micromol/gm) and displayed characteristic Ab...
متن کاملDeficits in synaptic transmission and learning in amyloid precursor protein (APP) transgenic mice require C-terminal cleavage of APP.
Synaptic dysfunction has been shown to be one of the earliest correlates of disease progression in animal models of Alzheimer's disease. Amyloid-beta protein (Abeta) is thought to play an important role in disease-related synaptic dysfunction, but the mechanism by which Abeta leads to synaptic dysfunction is not understood. Here we describe evidence that cleavage of APP in the C terminus may be...
متن کاملAging increased amyloid peptide and caused amyloid plaques in brain of old APP/V717I transgenic mice by a different mechanism than mutant presenilin1.
Aging of transgenic mice that overexpress the London mutant of amyloid precursor protein (APP/V717I) (Moechars et al., 1999a) was now demonstrated not to affect the normalized levels of alpha- or beta-cleaved secreted APP nor of the beta-C-terminal stubs. This indicated that aging did not markedly disturb either alpha- or beta-secretase cleavage of APP and failed to explain the origin of the ma...
متن کاملPii: S0531-5565(00)00149-2
In transgenic mice that overexpress mutant Amyloid Precursor Protein [V717I], or APP/London (APP/Lo) (1999a. Early phenotypic changes in transgenic mice that overexpress different mutants of Amyloid Precursor Protein in brain. J. Biol. Chem. 274, 6483±6492; 1999b. Premature death in transgenic mice that overexpress mutant Amyloid precursor protein is preceded by severe neurodegeneration and apo...
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تاریخ انتشار 2013