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000154287 0247_ $$2doi$$a10.1111/nan.12637
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000154287 037__ $$aDZNE-2021-00141
000154287 041__ $$aEnglish
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000154287 1001_ $$aZampar, S.$$b0
000154287 245__ $$aN-terminal heterogeneity of parenchymal and vascular amyloid-β deposits in Alzheimer's disease.
000154287 260__ $$aOxford [u.a.]$$bWiley-Blackwell$$c2020
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000154287 520__ $$aThe deposition of amyloid-β (Aβ) peptides in the form of extracellular plaques in the brain represents one of the classical hallmarks of Alzheimer's disease (AD). In addition to 'full-length' Aβ starting with aspartic acid (Asp-1), considerable amounts of various shorter, N-terminally truncated Aβ peptides have been identified by mass spectrometry in autopsy samples from individuals with AD.Selectivity of several antibodies detecting full-length, total or N-terminally truncated Aβ species has been characterized with capillary isoelectric focusing assays using a set of synthetic Aβ peptides comprising different N-termini. We further assessed the N-terminal heterogeneity of extracellular and vascular Aβ peptide deposits in the human brain by performing immunohistochemical analyses using sporadic AD cases with antibodies targeting different N-terminal residues, including the biosimilar antibodies Bapineuzumab and Crenezumab.While antibodies selectively recognizing Aβ1-x showed a much weaker staining of extracellular plaques and tended to accentuate cerebrovascular amyloid deposits, antibodies detecting Aβ starting with phenylalanine at position 4 of the Aβ sequence showed abundant amyloid plaque immunoreactivity in the brain parenchyma. The biosimilar antibody Bapineuzumab recognized Aβ starting at Asp-1 and demonstrated abundant immunoreactivity in AD brains.In contrast to other studied Aβ1-x -specific antibodies, Bapineuzumab displayed stronger immunoreactivity on fixed tissue samples than with sodium dodecyl sulfate-denatured samples on Western blots. This suggests conformational preferences of this antibody. The diverse composition of plaques and vascular deposits stresses the importance of understanding the roles of various Aβ variants during disease development and progression in order to generate appropriate target-developed therapies.
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000154287 650_7 $$2Other$$aAbeta
000154287 650_7 $$2Other$$aAlzheimer disease
000154287 650_7 $$2Other$$aN-terminal truncation
000154287 650_7 $$2Other$$aamyloid
000154287 650_7 $$2Other$$aantibody
000154287 650_7 $$2Other$$acapillary isoelectric focusing immunoassay
000154287 650_2 $$2MeSH$$aAged
000154287 650_2 $$2MeSH$$aAged, 80 and over
000154287 650_2 $$2MeSH$$aAlzheimer Disease: metabolism
000154287 650_2 $$2MeSH$$aAmyloid beta-Peptides: metabolism
000154287 650_2 $$2MeSH$$aAnimals
000154287 650_2 $$2MeSH$$aAntibodies, Monoclonal, Humanized: pharmacology
000154287 650_2 $$2MeSH$$aBrain: metabolism
000154287 650_2 $$2MeSH$$aDisease Models, Animal
000154287 650_2 $$2MeSH$$aHumans
000154287 650_2 $$2MeSH$$aPeptide Fragments: metabolism
000154287 650_2 $$2MeSH$$aPlaque, Amyloid: metabolism
000154287 7001_ $$aKlafki, H. W.$$b1
000154287 7001_ $$aSritharen, K.$$b2
000154287 7001_ $$aBayer, T. A.$$b3
000154287 7001_ $$0P:(DE-2719)2811317$$aWiltfang, J.$$b4$$udzne
000154287 7001_ $$aRostagno, A.$$b5
000154287 7001_ $$aGhiso, J.$$b6
000154287 7001_ $$aMiles, L. A.$$b7
000154287 7001_ $$0P:(DE-HGF)0$$aWirths, O.$$b8
000154287 773__ $$0PERI:(DE-600)2008293-9$$a10.1111/nan.12637$$gVol. 46, no. 7, p. 673 - 685$$n7$$p673 - 685$$tNeuropathology & applied neurobiology$$v46$$x1365-2990$$y2020
000154287 8564_ $$uhttps://pub.dzne.de/record/154287/files/nan.12637.pdf$$yOpenAccess
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