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@ARTICLE{Kramer:15797,
      author       = {Kramer, B. and Schulte, D. and Korner, C. and Zwank, C. and
                      Hartmann, A. and Michalk, M. and Sohne, J. and Langhans, B.
                      and Nischalke, H.D. and Coenen, M. and Möhl, C. and Vogt,
                      A. and Hennenberg, M. and Sauerbruch, T. and Spengler, U.
                      and Nattermann, J.},
      title        = {{R}egulation of {NK} {C}ell {T}rafficking by {CD}81},
      journal      = {European journal of immunology},
      volume       = {39},
      issn         = {0014-2980},
      address      = {Weinheim},
      publisher    = {Wiley-VCH},
      reportid     = {PreJuSER-15797},
      pages        = {3447 - 3458},
      year         = {2009},
      note         = {This work was supported by a grant from BMBF (German
                      Ministry for Science and Education) (01KI0791). We thank
                      Dirk Stabenow from the Institute of Molecular Medicine and
                      Experimental Immunology, University of Bonn, for his support
                      performing calcium influx.},
      abstract     = {NK cells, a heterogeneous sub-population of lymphocytes,
                      are critically involved in the regulation of both innate and
                      adaptive immune responses in humans. Besides their
                      participation in the control of tumors and viral infections,
                      they also regulate inflammatory processes, mediating both
                      beneficial and detrimental effects. To effectively fulfil
                      their role in immune surveillance, proper trafficking of NK
                      cells is essential. However, the mechanisms and factors
                      governing NK cell recruitment are only poorly dissected.
                      Here, we describe the functional role of tetraspanins, a
                      family of evolutionary conserved cell-surface proteins, in
                      modulating migration and transmigration of human NK cells.
                      We demonstrate expression of various tetraspanins on NK
                      cells. Furthermore, we show that stimulation of the NK
                      cell-expressed tetraspanin CD81 induces phosphorylation of
                      ezrin/radixin/moesin proteins and leads to NK cell
                      polarization thereby facilitating NK cell migration toward
                      various chemokines/cytokines. Finally, we provide evidence
                      for a role of CD81 in promoting adhesion of NK cells to
                      components of the extracellular matrix, a prerequisite for
                      extravasation of lymphocytes in inflamed tissues. Thus, our
                      data suggest that the tetraspanin CD81 is importantly
                      involved in the regulation of NK cell recruitment.},
      keywords     = {Antigens, CD: metabolism / Antigens, CD63 / Antigens, CD81
                      / Blotting, Western / Cell Adhesion / Cell Movement / Cell
                      Polarity / Chemokine CCL5: metabolism / Chemokine CCL5:
                      pharmacology / Chemotaxis: drug effects / Cytoskeletal
                      Proteins: metabolism / Flow Cytometry / Humans / Killer
                      Cells, Natural: cytology / Killer Cells, Natural: metabolism
                      / Membrane Proteins: metabolism / Microfilament Proteins:
                      metabolism / Phosphorylation / Platelet Membrane
                      Glycoproteins: metabolism / Protein Binding / Protein Kinase
                      C: metabolism / rho-Associated Kinases: metabolism /
                      Antigens, CD (NLM Chemicals) / Antigens, CD63 (NLM
                      Chemicals) / Antigens, CD81 (NLM Chemicals) / CD63 protein,
                      human (NLM Chemicals) / CD81 protein, human (NLM Chemicals)
                      / Chemokine CCL5 (NLM Chemicals) / Cytoskeletal Proteins
                      (NLM Chemicals) / Membrane Proteins (NLM Chemicals) /
                      Microfilament Proteins (NLM Chemicals) / Platelet Membrane
                      Glycoproteins (NLM Chemicals) / ezrin (NLM Chemicals) /
                      moesin (NLM Chemicals) / radixin (NLM Chemicals) /
                      rho-Associated Kinases (NLM Chemicals) / Protein Kinase C
                      (NLM Chemicals) / J (WoSType)},
      cin          = {ICS-7},
      ddc          = {610},
      cid          = {I:(DE-Juel1)ICS-7-20110106},
      pnm          = {BioSoft: Makromolekulare Systeme und biologische
                      Informationsverarbeitung},
      pid          = {G:(DE-Juel1)FUEK505},
      shelfmark    = {Immunology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:19830727},
      UT           = {WOS:000272928300021},
      doi          = {10.1002/eji.200939234},
      url          = {https://juser.fz-juelich.de/record/15797},
}