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@ARTICLE{Weiden:309977,
      author       = {E.-M. Weiden and Z. Serianz and Y. Klingl and S. Jörs and
                      D. Jaślan and M. Keller and S. P. Castro and M. Mkhitaryan
                      and A. Jeridi and D. Briukhovetska and B. Spix and A. Scotto
                      Rosato and A. Agami and H. B. Schiller and S. Rajan and J.
                      Schredelseker and G. Fois and M. Frick and S. Kobold$^*$ and
                      M. Klein and F. Geisler and J. Garcia-Fortanet and L. O.
                      Murphy and F. Bracher and C. Wahl-Schott and T. Gudermann
                      and A. Dietrich and M. Biel and A. Ö. Yildirim and C.
                      Grimm},
      title        = {{TRPML}1 suppresses pulmonary fibrosis by limiting collagen
                      and elastin deposition.},
      journal      = {The EMBO journal},
      volume       = {nn},
      issn         = {0261-4189},
      address      = {[London]},
      publisher    = {Nature Publishing Group UK},
      reportid     = {DKFZ-2026-00403},
      pages        = {nn},
      year         = {2026},
      note         = {epub},
      abstract     = {In pulmonary fibrosis lung tissue is thickened and scarred,
                      and the lungs become progressively stiffer and smaller,
                      leading to low levels of blood oxygen and shortness of
                      breath. Lung fibrosis is not curable and life expectancy is
                      reduced. Fibrosis is characterized by an increased
                      accumulation of extracellular matrix (ECM) proteins such as
                      collagen and elastin. ECM proteins are degraded
                      predominantly by matrix metalloproteinases (MMPs). Here, we
                      show that the lysosomal cation channel TRPML1, which causes
                      the lysosomal storage disorder mucolipidosis type IV (MLIV)
                      when mutated or lost, regulates the levels of MMPs in the
                      ECM of mouse airways, modulating exocytosis of MMP2, 8, 9,
                      12, and 19, which mediate collagen/elastin degradation.
                      While TRPML1 loss reduces MMP levels in lung macrophage and
                      fibroblast supernatants, small molecule activation of TRPML1
                      results in increased levels. MLIV mice display a
                      fibrosis-like lung phenotype similar to the phenotype evoked
                      by bleomycin. We thus identify TRPML1 as a regulator of MMP
                      release in the lung with loss of TRPML1 resulting in lung
                      fibrosis due to excessive extracellular collagen and elastin
                      accumulation.},
      keywords     = {Mcoln1 (Other) / Pulmonary Fibrosis (Other) / TRPML (Other)
                      / TRPML1 (Other) / TRPML3 (Other)},
      cin          = {MU01},
      ddc          = {570},
      cid          = {I:(DE-He78)MU01-20160331},
      pnm          = {899 - ohne Topic (POF4-899)},
      pid          = {G:(DE-HGF)POF4-899},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:41714729},
      doi          = {10.1038/s44318-026-00712-4},
      url          = {https://inrepo02.dkfz.de/record/309977},
}