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@ARTICLE{Guilbaud:275969,
      author       = {Guilbaud, Lucie and Roger, Kévin and Schmidt, Andree and
                      Chhuon, Cerina and Breimann, Stephan and Lipecka, Joanna and
                      Dreux, Sophie and Müller, Stephan A and Zérah, Michel and
                      Larghero, Jérôme and Jouannic, Jean-Marie and
                      Lichtenthaler, Stefan F and Guerrera, Ida C},
      title        = {{M}olecular insights into myelomeningocele via proteomic
                      analysis of amniotic fluid.},
      journal      = {Journal of proteomics},
      volume       = {313},
      issn         = {1874-3919},
      address      = {New York, NY [u.a.]},
      publisher    = {Elsevier},
      reportid     = {DZNE-2025-00165},
      pages        = {105372},
      year         = {2025},
      abstract     = {Despite numerous studies on fetal therapy for
                      myelomeningoceles (MMC), the pathophysiology of this
                      malformation remains poorly understood. This study aimed to
                      analyze the biochemical profile and proteome of amniotic
                      fluid (AF) supernatants from MMC fetuses to explore the
                      prenatal pathophysiology. Biochemical analysis of 61 AF
                      samples from MMC fetuses was compared with 45 healthy
                      fetuses' samples. Proteome analysis was conducted in 18 MMC
                      and 18 healthy singleton fetuses, and in 5 dichorionic
                      pregnancies with MMC fetuses and their healthy co-twins.
                      ELISA tests were used to validate proteome results.
                      Biochemical analysis revealed anal incontinence in 37 $\%$
                      of MMC cases, absent in controls (p < 0.0001). Proteomics
                      identified 2453 quantified proteins with 39 significantly
                      up-regulated and 10 down-regulated in the MMC group.
                      Up-regulated proteins included ectodomains of CHL1, APLP1,
                      SEZ6, SEZ6L, known targets of the protease BACE1. We
                      explored the overlap of neonatal cerebrospinal fluid (CSF)
                      and AF proteome and highlighted 411 proteins in common,
                      mostly upregulated in MMC AF compared to controls. Our study
                      thoroughly characterizes the AF proteome and reveals
                      numerous proteins to be changed as a consequence of MMC.
                      Many of these proteins are typical constituents of CSF. No
                      difference in AF inflammation markers were observed between
                      MMC and healthy fetuses. SIGNIFICANCE: This study provides
                      good evidence that neuroepithelial destruction in MMC is
                      independent of inflammation or presumed meconium toxicity.},
      keywords     = {Amniotic fluid (Other) / BACE1 (Other) / Myelomeningocele
                      (Other) / Pathophysiology (Other) / Proteomics (Other) /
                      Spina bifida (Other)},
      cin          = {AG Lichtenthaler / AG Steiner},
      ddc          = {540},
      cid          = {I:(DE-2719)1110006 / I:(DE-2719)1110000-1},
      pnm          = {352 - Disease Mechanisms (POF4-352)},
      pid          = {G:(DE-HGF)POF4-352},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:39778765},
      doi          = {10.1016/j.jprot.2024.105372},
      url          = {https://pub.dzne.de/record/275969},
}