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000138091 0247_ $$2doi$$a10.1371/journal.pone.0137311
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000138091 037__ $$aDZNE-2020-04413
000138091 041__ $$aEnglish
000138091 082__ $$a610
000138091 1001_ $$0P:(DE-HGF)0$$aMaus, Frank$$b0
000138091 245__ $$aThe NG2 Proteoglycan Protects Oligodendrocyte Precursor Cells against Oxidative Stress via Interaction with OMI/HtrA2.
000138091 260__ $$aSan Francisco, California, US$$bPLOS$$c2015
000138091 264_1 $$2Crossref$$3online$$bPublic Library of Science (PLoS)$$c2015-09-04
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000138091 520__ $$aThe NG2 proteoglycan is characteristically expressed by oligodendrocyte progenitor cells (OPC) and also by aggressive brain tumours highly resistant to chemo- and radiation therapy. Oligodendrocyte-lineage cells are particularly sensitive to stress resulting in cell death in white matter after hypoxic or ischemic insults of premature infants and destruction of OPC in some types of Multiple Sclerosis lesions. Here we show that the NG2 proteoglycan binds OMI/HtrA2, a mitochondrial serine protease which is released from damaged mitochondria into the cytosol in response to stress. In the cytosol, OMI/HtrA2 initiates apoptosis by proteolytic degradation of anti-apoptotic factors. OPC in which NG2 has been downregulated by siRNA, or OPC from the NG2-knockout mouse show an increased sensitivity to oxidative stress evidenced by increased cell death. The proapoptotic protease activity of OMI/HtrA2 in the cytosol can be reduced by the interaction with NG2. Human glioma expressing high levels of NG2 are less sensitive to oxidative stress than those with lower NG2 expression and reducing NG2 expression by siRNA increases cell death in response to oxidative stress. Binding of NG2 to OMI/HtrA2 may thus help protect cells against oxidative stress-induced cell death. This interaction is likely to contribute to the high chemo- and radioresistance of glioma.
000138091 536__ $$0G:(DE-HGF)POF3-345$$a345 - Population Studies and Genetics (POF3-345)$$cPOF3-345$$fPOF III$$x0
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000138091 650_7 $$2NLM Chemicals$$aAntibodies, Neutralizing
000138091 650_7 $$2NLM Chemicals$$aAntigens
000138091 650_7 $$2NLM Chemicals$$aMitochondrial Proteins
000138091 650_7 $$2NLM Chemicals$$aProteoglycans
000138091 650_7 $$2NLM Chemicals$$aRNA, Small Interfering
000138091 650_7 $$2NLM Chemicals$$achondroitin sulfate proteoglycan 4
000138091 650_7 $$0BBX060AN9V$$2NLM Chemicals$$aHydrogen Peroxide
000138091 650_7 $$0EC 3.4.21.-$$2NLM Chemicals$$aSerine Endopeptidases
000138091 650_7 $$0EC 3.4.21.108$$2NLM Chemicals$$aHTRA2 protein, human
000138091 650_7 $$0EC 3.4.21.108$$2NLM Chemicals$$aHigh-Temperature Requirement A Serine Peptidase 2
000138091 650_7 $$0EC 3.4.21.108$$2NLM Chemicals$$aHtra2 protein, mouse
000138091 650_2 $$2MeSH$$aAnimals
000138091 650_2 $$2MeSH$$aAntibodies, Neutralizing: pharmacology
000138091 650_2 $$2MeSH$$aAntigens: genetics
000138091 650_2 $$2MeSH$$aAntigens: metabolism
000138091 650_2 $$2MeSH$$aApoptosis: drug effects
000138091 650_2 $$2MeSH$$aBrain Neoplasms: genetics
000138091 650_2 $$2MeSH$$aBrain Neoplasms: metabolism
000138091 650_2 $$2MeSH$$aBrain Neoplasms: pathology
000138091 650_2 $$2MeSH$$aCell Line, Tumor
000138091 650_2 $$2MeSH$$aCerebellum: drug effects
000138091 650_2 $$2MeSH$$aCerebellum: metabolism
000138091 650_2 $$2MeSH$$aCerebellum: pathology
000138091 650_2 $$2MeSH$$aCytosol: drug effects
000138091 650_2 $$2MeSH$$aCytosol: metabolism
000138091 650_2 $$2MeSH$$aGene Expression Regulation, Neoplastic
000138091 650_2 $$2MeSH$$aGlioblastoma: genetics
000138091 650_2 $$2MeSH$$aGlioblastoma: metabolism
000138091 650_2 $$2MeSH$$aGlioblastoma: pathology
000138091 650_2 $$2MeSH$$aHigh-Temperature Requirement A Serine Peptidase 2
000138091 650_2 $$2MeSH$$aHumans
000138091 650_2 $$2MeSH$$aHydrogen Peroxide: pharmacology
000138091 650_2 $$2MeSH$$aMice
000138091 650_2 $$2MeSH$$aMice, Inbred C57BL
000138091 650_2 $$2MeSH$$aMice, Knockout
000138091 650_2 $$2MeSH$$aMitochondria: drug effects
000138091 650_2 $$2MeSH$$aMitochondria: metabolism
000138091 650_2 $$2MeSH$$aMitochondrial Proteins: genetics
000138091 650_2 $$2MeSH$$aMitochondrial Proteins: metabolism
000138091 650_2 $$2MeSH$$aOxidative Stress
000138091 650_2 $$2MeSH$$aPrimary Cell Culture
000138091 650_2 $$2MeSH$$aProtein Binding
000138091 650_2 $$2MeSH$$aProteoglycans: antagonists & inhibitors
000138091 650_2 $$2MeSH$$aProteoglycans: genetics
000138091 650_2 $$2MeSH$$aProteoglycans: metabolism
000138091 650_2 $$2MeSH$$aRNA, Small Interfering: genetics
000138091 650_2 $$2MeSH$$aRNA, Small Interfering: metabolism
000138091 650_2 $$2MeSH$$aSerine Endopeptidases: genetics
000138091 650_2 $$2MeSH$$aSerine Endopeptidases: metabolism
000138091 650_2 $$2MeSH$$aSignal Transduction
000138091 7001_ $$0P:(DE-HGF)0$$aSakry, Dominik$$b1
000138091 7001_ $$0P:(DE-HGF)0$$aBinamé, Fabien$$b2
000138091 7001_ $$0P:(DE-HGF)0$$aKarram, Khalad$$b3
000138091 7001_ $$0P:(DE-HGF)0$$aRajalingam, Krishnaraj$$b4
000138091 7001_ $$0P:(DE-HGF)0$$aWatts, Colin$$b5
000138091 7001_ $$0P:(DE-HGF)0$$aHeywood, Richard$$b6
000138091 7001_ $$0P:(DE-2719)2811170$$aKrüger, Rejko$$b7$$udzne
000138091 7001_ $$0P:(DE-HGF)0$$aStegmüller, Judith$$b8
000138091 7001_ $$0P:(DE-HGF)0$$aWerner, Hauke B$$b9
000138091 7001_ $$0P:(DE-HGF)0$$aNave, Klaus-Armin$$b10
000138091 7001_ $$0P:(DE-HGF)0$$aKrämer-Albers, Eva-Maria$$b11
000138091 7001_ $$0P:(DE-HGF)0$$aTrotter, Jacqueline$$b12
000138091 77318 $$2Crossref$$3journal-article$$a10.1371/journal.pone.0137311$$b : Public Library of Science (PLoS), 2015-09-04$$n9$$pe0137311$$tPLOS ONE$$v10$$x1932-6203$$y2015
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000138091 8567_ $$2Pubmed Central$$uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC4560422
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