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@ARTICLE{Kocsmr:275261,
      author       = {É. Kocsmár and M. Schmid and M. Cosenza-Contreras and I.
                      Kocsmár and M. Föll$^*$ and L. Krey and B. A. Barta and G.
                      Rácz and A. Kiss and M. Werner$^*$ and O. Schilling$^*$ and
                      G. Lotz and P. Bronsert},
      title        = {{P}roteome alterations in human autopsy tissues in relation
                      to time after death.},
      journal      = {Cellular and molecular life sciences},
      volume       = {80},
      number       = {5},
      issn         = {1420-682X},
      address      = {Cham (ZG)},
      publisher    = {Springer International Publishing AG},
      reportid     = {DKFZ-2023-00708},
      pages        = {117},
      year         = {2023},
      abstract     = {Protein expression is a primary area of interest for
                      routine histological diagnostics and tissue-based research
                      projects, but the limitations of its post-mortem
                      applicability remain largely unclear. On the other hand,
                      tissue specimens obtained during autopsies can provide
                      unique insight into advanced disease states, especially in
                      cancer research. Therefore, we aimed to identify the maximum
                      post-mortem interval (PMI) which is still suitable for
                      characterizing protein expression patterns, to explore
                      organ-specific differences in protein degradation, and to
                      investigate whether certain proteins follow specific
                      degradation kinetics. Therefore, the proteome of human
                      tissue samples obtained during routine autopsies of deceased
                      patients with accurate PMI (6, 12, 18, 24, 48, 72, 96 h) and
                      without specific diseases that significantly affect tissue
                      preservation, from lungs, kidneys and livers, was analyzed
                      by liquid chromatography-tandem mass spectrometry
                      (LC-MS/MS). For the kidney and liver, significant protein
                      degradation became apparent at 48 h. For the lung, the
                      proteome composition was rather static for up to 48 h and
                      substantial protein degradation was detected only at 72 h
                      suggesting that degradation kinetics appear to be organ
                      specific. More detailed analyses suggested that proteins
                      with similar post-mortem kinetics are not primarily shared
                      in their biological functions. The overrepresentation of
                      protein families with analogous structural motifs in the
                      kidney indicates that structural features may be a common
                      factor in determining similar postmortem stability. Our
                      study demonstrates that a longer post-mortem period may have
                      a significant impact on proteome composition, but sampling
                      within 24 h may be appropriate, as degradation is within
                      acceptable limits even in organs with faster autolysis.},
      keywords     = {Autopsy (Other) / Degradation (Other) / Proteomics (Other)},
      cin          = {FR01},
      ddc          = {610},
      cid          = {I:(DE-He78)FR01-20160331},
      pnm          = {899 - ohne Topic (POF4-899)},
      pid          = {G:(DE-HGF)POF4-899},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:37020120},
      doi          = {10.1007/s00018-023-04754-3},
      url          = {https://inrepo02.dkfz.de/record/275261},
}