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@ARTICLE{Zampar:154287,
      author       = {Zampar, S. and Klafki, H. W. and Sritharen, K. and Bayer,
                      T. A. and Wiltfang, J. and Rostagno, A. and Ghiso, J. and
                      Miles, L. A. and Wirths, O.},
      title        = {{N}-terminal heterogeneity of parenchymal and vascular
                      amyloid-β deposits in {A}lzheimer's disease.},
      journal      = {Neuropathology $\&$ applied neurobiology},
      volume       = {46},
      number       = {7},
      issn         = {1365-2990},
      address      = {Oxford [u.a.]},
      publisher    = {Wiley-Blackwell},
      reportid     = {DZNE-2021-00141},
      pages        = {673 - 685},
      year         = {2020},
      note         = {ISSN 1365-2990 not unique: **3 hits**.},
      abstract     = {The 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.},
      keywords     = {Aged / Aged, 80 and over / Alzheimer Disease: metabolism /
                      Amyloid beta-Peptides: metabolism / Animals / Antibodies,
                      Monoclonal, Humanized: pharmacology / Brain: metabolism /
                      Disease Models, Animal / Humans / Peptide Fragments:
                      metabolism / Plaque, Amyloid: metabolism / Abeta (Other) /
                      Alzheimer disease (Other) / N-terminal truncation (Other) /
                      amyloid (Other) / antibody (Other) / capillary isoelectric
                      focusing immunoassay (Other)},
      cin          = {AG Wiltfang},
      ddc          = {610},
      cid          = {I:(DE-2719)1410006},
      pnm          = {342 - Disease Mechanisms and Model Systems (POF3-342)},
      pid          = {G:(DE-HGF)POF3-342},
      typ          = {PUB:(DE-HGF)16},
      pmc          = {pmc:PMC8082844},
      pubmed       = {pmid:32497293},
      doi          = {10.1111/nan.12637},
      url          = {https://pub.dzne.de/record/154287},
}