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@ARTICLE{Maus:138091,
      author       = {Maus, Frank and Sakry, Dominik and Binamé, Fabien and
                      Karram, Khalad and Rajalingam, Krishnaraj and Watts, Colin
                      and Heywood, Richard and Krüger, Rejko and Stegmüller,
                      Judith and Werner, Hauke B and Nave, Klaus-Armin and
                      Krämer-Albers, Eva-Maria and Trotter, Jacqueline},
      title        = {{T}he {NG}2 {P}roteoglycan {P}rotects {O}ligodendrocyte
                      {P}recursor {C}ells against {O}xidative {S}tress via
                      {I}nteraction with {OMI}/{H}tr{A}2.},
      journal      = {PLOS ONE},
      volume       = {10},
      number       = {9},
      issn         = {1932-6203},
      address      = {San Francisco, California, US},
      publisher    = {PLOS},
      reportid     = {DZNE-2020-04413},
      pages        = {e0137311},
      year         = {2015},
      abstract     = {The NG2 proteoglycan is characteristically expressed by
                      oligodendrocyte progenitor cells (OPC) and also by
                      aggressive brain tumours highly resistant to chemo- and
                      radiation therapy. Oligodendrocyte-lineage cells are
                      particularly sensitive to stress resulting in cell death in
                      white matter after hypoxic or ischemic insults of premature
                      infants and destruction of OPC in some types of Multiple
                      Sclerosis lesions. Here we show that the NG2 proteoglycan
                      binds OMI/HtrA2, a mitochondrial serine protease which is
                      released from damaged mitochondria into the cytosol in
                      response to stress. In the cytosol, OMI/HtrA2 initiates
                      apoptosis by proteolytic degradation of anti-apoptotic
                      factors. OPC in which NG2 has been downregulated by siRNA,
                      or OPC from the NG2-knockout mouse show an increased
                      sensitivity to oxidative stress evidenced by increased cell
                      death. The proapoptotic protease activity of OMI/HtrA2 in
                      the cytosol can be reduced by the interaction with NG2.
                      Human glioma expressing high levels of NG2 are less
                      sensitive to oxidative stress than those with lower NG2
                      expression and reducing NG2 expression by siRNA increases
                      cell death in response to oxidative stress. Binding of NG2
                      to OMI/HtrA2 may thus help protect cells against oxidative
                      stress-induced cell death. This interaction is likely to
                      contribute to the high chemo- and radioresistance of
                      glioma.},
      keywords     = {Animals / Antibodies, Neutralizing: pharmacology /
                      Antigens: genetics / Antigens: metabolism / Apoptosis: drug
                      effects / Brain Neoplasms: genetics / Brain Neoplasms:
                      metabolism / Brain Neoplasms: pathology / Cell Line, Tumor /
                      Cerebellum: drug effects / Cerebellum: metabolism /
                      Cerebellum: pathology / Cytosol: drug effects / Cytosol:
                      metabolism / Gene Expression Regulation, Neoplastic /
                      Glioblastoma: genetics / Glioblastoma: metabolism /
                      Glioblastoma: pathology / High-Temperature Requirement A
                      Serine Peptidase 2 / Humans / Hydrogen Peroxide:
                      pharmacology / Mice / Mice, Inbred C57BL / Mice, Knockout /
                      Mitochondria: drug effects / Mitochondria: metabolism /
                      Mitochondrial Proteins: genetics / Mitochondrial Proteins:
                      metabolism / Oxidative Stress / Primary Cell Culture /
                      Protein Binding / Proteoglycans: antagonists $\&$ inhibitors
                      / Proteoglycans: genetics / Proteoglycans: metabolism / RNA,
                      Small Interfering: genetics / RNA, Small Interfering:
                      metabolism / Serine Endopeptidases: genetics / Serine
                      Endopeptidases: metabolism / Signal Transduction /
                      Antibodies, Neutralizing (NLM Chemicals) / Antigens (NLM
                      Chemicals) / Mitochondrial Proteins (NLM Chemicals) /
                      Proteoglycans (NLM Chemicals) / RNA, Small Interfering (NLM
                      Chemicals) / chondroitin sulfate proteoglycan 4 (NLM
                      Chemicals) / Hydrogen Peroxide (NLM Chemicals) / Serine
                      Endopeptidases (NLM Chemicals) / HTRA2 protein, human (NLM
                      Chemicals) / High-Temperature Requirement A Serine Peptidase
                      2 (NLM Chemicals) / Htra2 protein, mouse (NLM Chemicals)},
      cin          = {AG Gasser 1},
      ddc          = {610},
      cid          = {I:(DE-2719)1210000},
      pnm          = {345 - Population Studies and Genetics (POF3-345)},
      pid          = {G:(DE-HGF)POF3-345},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:26340347},
      pmc          = {pmc:PMC4560422},
      doi          = {10.1371/journal.pone.0137311},
      url          = {https://pub.dzne.de/record/138091},
}