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@ARTICLE{VomStein:274226,
      author       = {A. F. Vom Stein and R. Rebollido-Rios and A. Lukas and M.
                      Koch and A. von Lom and S. Reinartz and D. Bachurski and F.
                      Rose and K. Bozek and A. T. Abdallah and V. Kohlhas and J.
                      Saggau and R. Zölzer and Y. Zhao and C. Bruns and P. J.
                      Bröckelmann and P. Lohneis and R. Büttner and B.
                      Häupl$^*$ and T. Oellerich$^*$ and P.-H. Nguyen and M.
                      Hallek},
      title        = {{LYN} kinase programs stromal fibroblasts to facilitate
                      leukemic survival via regulation of c-{JUN} and {THBS}1.},
      journal      = {Nature Communications},
      volume       = {14},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Nature Publishing Group UK},
      reportid     = {DKFZ-2023-00512},
      pages        = {1330},
      year         = {2023},
      abstract     = {Microenvironmental bystander cells are essential for the
                      progression of chronic lymphocytic leukemia (CLL). We have
                      discovered previously that LYN kinase promotes the formation
                      of a microenvironmental niche for CLL. Here we provide
                      mechanistic evidence that LYN regulates the polarization of
                      stromal fibroblasts to support leukemic progression. LYN is
                      overexpressed in fibroblasts of lymph nodes of CLL patients.
                      LYN-deficient stromal cells reduce CLL growth in vivo.
                      LYN-deficient fibroblasts show markedly reduced leukemia
                      feeding capacity in vitro. Multi-omics profiling reveals
                      that LYN regulates the polarization of fibroblasts towards
                      an inflammatory cancer-associated phenotype through
                      modulation of cytokine secretion and extracellular matrix
                      composition. Mechanistically, LYN deletion reduces
                      inflammatory signaling including reduction of c-JUN
                      expression, which in turn augments the expression of
                      Thrombospondin-1, which binds to CD47 thereby impairing CLL
                      viability. Together, our findings suggest that LYN is
                      essential for rewiring fibroblasts towards a
                      leukemia-supportive phenotype.},
      cin          = {FM01},
      ddc          = {500},
      cid          = {I:(DE-He78)FM01-20160331},
      pnm          = {899 - ohne Topic (POF4-899)},
      pid          = {G:(DE-HGF)POF4-899},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:36899005},
      pmc          = {pmc:PMC10006233},
      doi          = {10.1038/s41467-023-36824-2},
      url          = {https://inrepo02.dkfz.de/record/274226},
}