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@ARTICLE{Waldow:277869,
      author       = {A. Waldow and L.-S. Beier and J. Arndt and S. Schallenberg
                      and C. Vollbrecht and P. Bischoff$^*$ and M. Farrera-Sal and
                      F. N. Loch and C. Bojarski and M. Schumann and L. Winkler
                      and C. Kamphues and L. Ehlen and J. Piontek},
      title        = {c{CPE} {F}usion {P}roteins as {M}olecular {P}robes to
                      {D}etect {C}laudins and {T}ight {J}unction {D}ysregulation
                      in {G}astrointestinal {C}ell {L}ines, {T}issue {E}xplants
                      and {P}atient-{D}erived {O}rganoids.},
      journal      = {Pharmaceutics},
      volume       = {15},
      number       = {7},
      issn         = {1999-4923},
      address      = {Basel},
      publisher    = {MDPI},
      reportid     = {DKFZ-2023-01537},
      pages        = {1980},
      year         = {2023},
      abstract     = {Claudins regulate paracellular permeability, contribute to
                      epithelial polarization and are dysregulated during
                      inflammation and carcinogenesis. Variants of the
                      claudin-binding domain of Clostridium perfringens
                      enterotoxin (cCPE) are highly sensitive protein ligands for
                      generic detection of a broad spectrum of claudins. Here, we
                      investigated the preferential binding of YFP- or GST-cCPE
                      fusion proteins to non-junctional claudin molecules. Plate
                      reader assays, flow cytometry and microscopy were used to
                      assess the binding of YFP- or GST-cCPE to non-junctional
                      claudins in multiple in vitro and ex vivo models of human
                      and rat gastrointestinal epithelia and to monitor formation
                      of a tight junction barrier. Furthermore, YFP-cCPE was used
                      to probe expression, polar localization and dysregulation of
                      claudins in patient-derived organoids generated from gastric
                      dysplasia and gastric cancer. Live-cell imaging and
                      immunocytochemistry revealed cell polarity and presence of
                      tight junctions in glandular organoids (originating from
                      intestinal-type gastric cancer and gastric dysplasia) and,
                      in contrast, a disrupted diffusion barrier for granular
                      organoids (originating from discohesive tumor areas). In
                      sum, we report the use of cCPE fusion proteins as molecular
                      probes to specifically and efficiently detect claudin
                      expression, localization and tight junction dysregulation in
                      cell lines, tissue explants and patient-derived organoids of
                      the gastrointestinal tract.},
      keywords     = {adenoma (Other) / claudin (Other) / clostridium perfringens
                      enterotoxin (Other) / colon (Other) / gastric cancer (Other)
                      / gastric dysplasia (Other) / organoids (Other) / tight
                      junction (Other) / tumor (Other)},
      cin          = {BE01},
      ddc          = {610},
      cid          = {I:(DE-He78)BE01-20160331},
      pnm          = {899 - ohne Topic (POF4-899)},
      pid          = {G:(DE-HGF)POF4-899},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:37514167},
      pmc          = {pmc:PMC10385049},
      doi          = {10.3390/pharmaceutics15071980},
      url          = {https://inrepo02.dkfz.de/record/277869},
}