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@ARTICLE{Hartwig:59197,
      author       = {Hartwig, B. and Borm, B. and Schneider, H. and Arin, M. J.
                      and Kirfel, G. and Herzog, V.},
      title        = {{L}aminin-5-deficient human keratinocytes: {D}efective
                      adhesion results in a saltatory and inefficient mode of
                      migration},
      journal      = {Experimental cell research},
      volume       = {313},
      issn         = {0014-4827},
      address      = {Orlando, Fla.},
      publisher    = {Academic Press},
      reportid     = {PreJuSER-59197},
      pages        = {1575 - 1587},
      year         = {2007},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Laminin-5 is a major adhesion protein of the skin basement
                      membrane and crucially involved in integrin-mediated cell
                      substrate attachment of keratinocytes, which is important
                      for hemidesmosomal anchorage as well as for keratinocyte
                      migration during epidermal wound healing. To investigate its
                      role in keratinocyte migration, we analyzed
                      laminin-5-deficient cells of patients with a lethal variant
                      of junctional epidermolysis bullosa. Normal migrating
                      keratinocytes adopted monopolar morphology with a distinct
                      front lamella and employed a continuous mode of
                      translocation. In contrast, laminin-5-deficient cells
                      assumed a stretched bipolar shape with two lamella regions
                      and migrated in a discontinuous, saltatory manner
                      characterized by significantly decreased directional
                      persistence and reduced migration velocity. The distinct
                      morphology as well as the migratory phenotype apparently
                      resulted from a defect in the formation of cell substrate
                      adhesions that were completely missing in the cell body and
                      less stable in the lamella regions. Accordingly in normal
                      keratinocytes, a bipolar shape and a saltatory migration
                      mode were inducible by blocking laminin-5-mediated substrate
                      adhesion. Our findings clearly point to an essential role of
                      laminin-5 in forming dynamic cell substrate adhesion during
                      migration of epidermal keratinocytes and provide an
                      explanation for the cellular mechanisms that underlie the
                      lethal form of junctional epidermolysis bullosa.},
      keywords     = {Cell Adhesion / Cell Adhesion Molecules: genetics / Cell
                      Adhesion Molecules: metabolism / Cell Adhesion Molecules:
                      physiology / Cell Movement / Cell Polarity / Cell Shape /
                      Cells, Cultured / Epidermolysis Bullosa, Junctional:
                      metabolism / Epidermolysis Bullosa, Junctional: pathology /
                      Extracellular Matrix Proteins: metabolism / Humans /
                      Keratinocytes: physiology / Pseudopodia: physiology / Cell
                      Adhesion Molecules (NLM Chemicals) / Extracellular Matrix
                      Proteins (NLM Chemicals) / kalinin (NLM Chemicals) / J
                      (WoSType)},
      cin          = {IBN-4},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB802},
      pnm          = {Kondensierte Materie},
      pid          = {G:(DE-Juel1)FUEK414},
      shelfmark    = {Oncology / Cell Biology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:17335805},
      UT           = {WOS:000246128300006},
      doi          = {10.1016/j.yexcr.2007.02.003},
      url          = {https://juser.fz-juelich.de/record/59197},
}