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@ARTICLE{Krueger:889872,
      author       = {Krueger, Irena and Gremer, Lothar and Mangels, Lena and
                      Klier, Meike and Jurk, Kerstin and Willbold, Dieter and
                      Bock, Hans H. and Elvers, Margitta},
      title        = {{R}eelin {A}mplifies {G}lycoprotein {VI} {A}ctivation and
                      {A}lpha{II}b {B}eta3 {I}ntegrin {O}utside-{I}n {S}ignaling
                      via {PLC} {G}amma 2 and {R}ho {GTP}ases},
      journal      = {Arteriosclerosis, thrombosis, and vascular biology},
      volume       = {40},
      number       = {10},
      issn         = {1524-4636},
      address      = {Stanford, Calif.},
      publisher    = {HighWire},
      reportid     = {FZJ-2021-00480},
      pages        = {2391 - 2403},
      year         = {2020},
      abstract     = {Objective:Reelin, a secreted glycoprotein, was originally
                      identified in the central nervous system, where it plays an
                      important role in brain development and maintenance. In the
                      cardiovascular system, reelin plays a role in
                      atherosclerosis by enhancing vascular inflammation and in
                      arterial thrombosis by promoting platelet adhesion,
                      activation, and thrombus formation via APP (amyloid
                      precursor protein) and GP (glycoprotein) Ib. However, the
                      role of reelin in hemostasis and arterial thrombosis is not
                      fully understood to date.Approach and Results:In the present
                      study, we analyzed the importance of reelin for cytoskeletal
                      reorganization of platelets and thrombus formation in more
                      detail. Platelets release reelin to amplify alphaIIb beta3
                      integrin outside-in signaling by promoting platelet
                      adhesion, cytoskeletal reorganization, and clot retraction
                      via activation of Rho GTPases RAC1 (Ras-related C3 botulinum
                      toxin substrate) and RhoA (Ras homolog family member A).
                      Reelin interacts with the collagen receptor GP
                      (glycoprotein) VI with subnanomolar affinity, induces
                      tyrosine phosphorylation in a GPVI-dependent manner, and
                      supports platelet binding to collagen and GPVI-dependent
                      RAC1 activation, PLC gamma 2
                      (1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase
                      gamma-2) phosphorylation, platelet activation, and
                      aggregation. When GPVI was deleted from the platelet surface
                      by antibody treatment in reelin-deficient mice, thrombus
                      formation was completely abolished after injury of the
                      carotid artery while being only reduced in either
                      GPVI-depleted or reelin-deficient mice.Conclusions:Our study
                      identified a novel signaling pathway that involves
                      reelin-induced GPVI activation and alphaIIb beta3 integrin
                      outside-in signaling in platelets. Loss of both, GPVI and
                      reelin, completely prevents stable arterial thrombus
                      formation in vivo suggesting that inhibiting
                      reelin-platelet-interaction might represent a novel strategy
                      to avoid arterial thrombosis in cardiovascular disease.},
      cin          = {IBI-7},
      ddc          = {610},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {551 - Functional Macromolecules and Complexes (POF3-551)},
      pid          = {G:(DE-HGF)POF3-551},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {32787521},
      UT           = {WOS:000576399500009},
      doi          = {10.1161/ATVBAHA.120.314902},
      url          = {https://juser.fz-juelich.de/record/889872},
}