Home > Publications Database > The NG2 Proteoglycan Protects Oligodendrocyte Precursor Cells against Oxidative Stress via Interaction with OMI/HtrA2. > print

001     138091
005     20240321220353.0
024 7 _ |a 10.1371/journal.pone.0137311
|2 doi
024 7 _ |a pmid:26340347
|2 pmid
024 7 _ |a pmc:PMC4560422
|2 pmc
024 7 _ |a altmetric:4476192
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037 _ _ |a DZNE-2020-04413
041 _ _ |a English
082 _ _ |a 610
100 1 _ |a Maus, Frank
|0 P:(DE-HGF)0
|b 0
245 _ _ |a The NG2 Proteoglycan Protects Oligodendrocyte Precursor Cells against Oxidative Stress via Interaction with OMI/HtrA2.
260 _ _ |a San Francisco, California, US
|c 2015
|b PLOS
264 _ 1 |3 online
|2 Crossref
|b Public Library of Science (PLoS)
|c 2015-09-04
336 7 _ |a article
|2 DRIVER
336 7 _ |a Output Types/Journal article
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336 7 _ |a Journal Article
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|m journal
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336 7 _ |a ARTICLE
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336 7 _ |a JOURNAL_ARTICLE
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336 7 _ |a Journal Article
|0 0
|2 EndNote
520 _ _ |a 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.
536 _ _ |a 345 - Population Studies and Genetics (POF3-345)
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542 _ _ |i 2015-09-04
|2 Crossref
|u http://creativecommons.org/licenses/by/4.0/
588 _ _ |a Dataset connected to CrossRef, PubMed,
650 _ 7 |a Antibodies, Neutralizing
|2 NLM Chemicals
650 _ 7 |a Antigens
|2 NLM Chemicals
650 _ 7 |a Mitochondrial Proteins
|2 NLM Chemicals
650 _ 7 |a Proteoglycans
|2 NLM Chemicals
650 _ 7 |a RNA, Small Interfering
|2 NLM Chemicals
650 _ 7 |a chondroitin sulfate proteoglycan 4
|2 NLM Chemicals
650 _ 7 |a Hydrogen Peroxide
|0 BBX060AN9V
|2 NLM Chemicals
650 _ 7 |a Serine Endopeptidases
|0 EC 3.4.21.-
|2 NLM Chemicals
650 _ 7 |a HTRA2 protein, human
|0 EC 3.4.21.108
|2 NLM Chemicals
650 _ 7 |a High-Temperature Requirement A Serine Peptidase 2
|0 EC 3.4.21.108
|2 NLM Chemicals
650 _ 7 |a Htra2 protein, mouse
|0 EC 3.4.21.108
|2 NLM Chemicals
650 _ 2 |a Animals
|2 MeSH
650 _ 2 |a Antibodies, Neutralizing: pharmacology
|2 MeSH
650 _ 2 |a Antigens: genetics
|2 MeSH
650 _ 2 |a Antigens: metabolism
|2 MeSH
650 _ 2 |a Apoptosis: drug effects
|2 MeSH
650 _ 2 |a Brain Neoplasms: genetics
|2 MeSH
650 _ 2 |a Brain Neoplasms: metabolism
|2 MeSH
650 _ 2 |a Brain Neoplasms: pathology
|2 MeSH
650 _ 2 |a Cell Line, Tumor
|2 MeSH
650 _ 2 |a Cerebellum: drug effects
|2 MeSH
650 _ 2 |a Cerebellum: metabolism
|2 MeSH
650 _ 2 |a Cerebellum: pathology
|2 MeSH
650 _ 2 |a Cytosol: drug effects
|2 MeSH
650 _ 2 |a Cytosol: metabolism
|2 MeSH
650 _ 2 |a Gene Expression Regulation, Neoplastic
|2 MeSH
650 _ 2 |a Glioblastoma: genetics
|2 MeSH
650 _ 2 |a Glioblastoma: metabolism
|2 MeSH
650 _ 2 |a Glioblastoma: pathology
|2 MeSH
650 _ 2 |a High-Temperature Requirement A Serine Peptidase 2
|2 MeSH
650 _ 2 |a Humans
|2 MeSH
650 _ 2 |a Hydrogen Peroxide: pharmacology
|2 MeSH
650 _ 2 |a Mice
|2 MeSH
650 _ 2 |a Mice, Inbred C57BL
|2 MeSH
650 _ 2 |a Mice, Knockout
|2 MeSH
650 _ 2 |a Mitochondria: drug effects
|2 MeSH
650 _ 2 |a Mitochondria: metabolism
|2 MeSH
650 _ 2 |a Mitochondrial Proteins: genetics
|2 MeSH
650 _ 2 |a Mitochondrial Proteins: metabolism
|2 MeSH
650 _ 2 |a Oxidative Stress
|2 MeSH
650 _ 2 |a Primary Cell Culture
|2 MeSH
650 _ 2 |a Protein Binding
|2 MeSH
650 _ 2 |a Proteoglycans: antagonists & inhibitors
|2 MeSH
650 _ 2 |a Proteoglycans: genetics
|2 MeSH
650 _ 2 |a Proteoglycans: metabolism
|2 MeSH
650 _ 2 |a RNA, Small Interfering: genetics
|2 MeSH
650 _ 2 |a RNA, Small Interfering: metabolism
|2 MeSH
650 _ 2 |a Serine Endopeptidases: genetics
|2 MeSH
650 _ 2 |a Serine Endopeptidases: metabolism
|2 MeSH
650 _ 2 |a Signal Transduction
|2 MeSH
700 1 _ |a Sakry, Dominik
|0 P:(DE-HGF)0
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700 1 _ |a Binamé, Fabien
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700 1 _ |a Karram, Khalad
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700 1 _ |a Rajalingam, Krishnaraj
|0 P:(DE-HGF)0
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700 1 _ |a Watts, Colin
|0 P:(DE-HGF)0
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700 1 _ |a Heywood, Richard
|0 P:(DE-HGF)0
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700 1 _ |a Krüger, Rejko
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700 1 _ |a Stegmüller, Judith
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700 1 _ |a Werner, Hauke B
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700 1 _ |a Nave, Klaus-Armin
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700 1 _ |a Krämer-Albers, Eva-Maria
|0 P:(DE-HGF)0
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700 1 _ |a Trotter, Jacqueline
|0 P:(DE-HGF)0
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773 1 8 |a 10.1371/journal.pone.0137311
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|v 10
|y 2015
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773 _ _ |a 10.1371/journal.pone.0137311
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856 7 _ |2 Pubmed Central
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910 1 _ |a Deutsches Zentrum für Neurodegenerative Erkrankungen
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914 1 _ |y 2015
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