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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},
}