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@ARTICLE{Donner:849980,
      author       = {Donner, Lili and Gremer, Lothar and Ziehm, Tamar and
                      Gertzen, Christoph G. W. and Gohlke, Holger and Willbold,
                      Dieter and Elvers, Margitta},
      title        = {{R}elevance of {N}-terminal residues for amyloid-β binding
                      to platelet integrin α {II}b β 3 , integrin outside-in
                      signaling and amyloid-β fibril formation},
      journal      = {Cellular signalling},
      volume       = {50},
      issn         = {0898-6568},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier Science},
      reportid     = {FZJ-2018-04075},
      pages        = {121 - 130},
      year         = {2018},
      abstract     = {A pathological hallmark of Alzheimer's disease (AD) is the
                      aggregation of amyloid-β peptides (Aβ) into fibrils,
                      leading to deposits in cerebral parenchyma and vessels known
                      as cerebral amyloid angiopathy (CAA). Platelets are major
                      players of hemostasis but are also implicated in AD.
                      Recently we provided strong evidence for a direct
                      contribution of platelets to AD pathology. We found that
                      monomeric Aβ40 binds through its RHDS sequence to integrin
                      αIIbβ3, and promotes the formation of fibrillar Aβ
                      aggregates by the secretion of adenosine diphosphate (ADP)
                      and the chaperone protein clusterin (CLU) from platelets.
                      Here we investigated the molecular mechanisms of Aβ binding
                      to integrin αIIbβ3 by using Aβ11 and Aβ16 peptides.
                      These peptides include the RHDS binding motif important for
                      integrin binding but lack the central hydrophobic core and
                      the C-terminal sequence of Aβ. We observed platelet
                      adhesion to truncated N-terminal Aβ11 and Aβ16 peptides
                      that was not mediated by integrin αIIbβ3. Thus, no
                      integrin outside-in signaling and reduced CLU release was
                      detected. Accordingly, platelet mediated Aβ fibril
                      formation was not observed. Taken together, the RHDS motif
                      of Aβ is not sufficient for Aβ binding to platelet
                      integrin αIIbβ3 and platelet mediated Aβ fibril formation
                      but requires other recognition or binding motifs important
                      for platelet mediated processes in CAA. Thus, increased
                      understanding of the molecular mechanisms of Aβ binding to
                      platelet integrin αIIbβ3 is important to understand the
                      role of platelets in amyloid pathology.},
      cin          = {NIC / JSC / ICS-6},
      ddc          = {540},
      cid          = {I:(DE-Juel1)NIC-20090406 / I:(DE-Juel1)JSC-20090406 /
                      I:(DE-Juel1)ICS-6-20110106},
      pnm          = {511 - Computational Science and Mathematical Methods
                      (POF3-511) / 553 - Physical Basis of Diseases (POF3-553) /
                      341 - Molecular Signaling (POF3-341) / Forschergruppe Gohlke
                      $(hkf7_20170501)$},
      pid          = {G:(DE-HGF)POF3-511 / G:(DE-HGF)POF3-553 /
                      G:(DE-HGF)POF3-341 / $G:(DE-Juel1)hkf7_20170501$},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:29964150},
      UT           = {WOS:000441493100012},
      doi          = {10.1016/j.cellsig.2018.06.015},
      url          = {https://juser.fz-juelich.de/record/849980},
}