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@ARTICLE{Homberg:189847,
      author       = {Homberg, Melanie and Ramms, Lena and Schwarz, Nicole and
                      Dreissen, Georg and Leube, Rudolf and Merkel, Rudolf and
                      Hoffmann, Bernd and Magin, Thomas M.},
      title        = {{D}istinct impact of two keratin mutations causing
                      epidermolysis bullosa simplex on keratinocyte adhesion and
                      stiffness},
      journal      = {The journal of investigative dermatology},
      volume       = {135},
      number       = {000},
      issn         = {0022-202X},
      address      = {Basingstoke [u.a.]},
      publisher    = {Nature Publishing Group},
      reportid     = {FZJ-2015-02853},
      pages        = {2437–2445},
      year         = {2015},
      abstract     = {Keratin filaments constitute the major component of the
                      epidermal cytoskeleton from heterodimers of type I and type
                      II keratin subunits. Missense mutations in keratin 5 or
                      keratin 14, highly expressed in the basal epidermis, cause
                      the severe skin blistering disease epidermolysis bullosa
                      simplex (EBS) in humans by rendering the keratin
                      cytoskeleton sensitive to mechanical stress; yet, the
                      mechanisms by which individual mutations cause cell
                      fragility are incompletely understood. Here, we compared the
                      K14p.Arg125Pro with the K5p.Glu477Asp mutation, both giving
                      rise to severe generalized EBS, by stable expression in
                      keratin-free keratinocytes. This revealed distinctly
                      different effects on keratin cytoskeletal organization, in
                      agreement with in vivo observations, thus validating the
                      cell system. Although the K14p.Arg125Pro mutation led to
                      impaired desmosomes, downregulation of desmosomal proteins,
                      and weakened epithelial sheet integrity upon shear stress,
                      the K5p.Glu477Asp mutation did not impair these functions,
                      although causing EBS with squamous cell carcinoma in vivo.
                      Atomic force microscopy demonstrated that K14 mutant cells
                      were even less resistant against deformation compared with
                      keratin-free keratinocytes. Thus, a keratin mutation causing
                      EBS compromises cell stiffness to a greater extent than the
                      lack of keratins. Finally, re-expression of K14 in K14
                      mutant cells did not rescue the above defects. Collectively,
                      our findings have implications for EBS therapy approaches.},
      cin          = {ICS-7},
      ddc          = {610},
      cid          = {I:(DE-Juel1)ICS-7-20110106},
      pnm          = {552 - Engineering Cell Function (POF3-552)},
      pid          = {G:(DE-HGF)POF3-552},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000360995600016},
      pubmed       = {pmid:25961909},
      doi          = {10.1038/jid.2015.184},
      url          = {https://juser.fz-juelich.de/record/189847},
}