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Chromatin repair after oxidative stress: Role of PARP-mediated proteasome activation

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dc.contributor.authorYILMAZ, BETÜL
dc.contributor.authorsCatalgol, Betul; Wendt, Brigitte; Grimm, Stephanie; Breusing, Nicolle; Ozer, Nesrin Kartal; Grune, Tilman
dc.date.accessioned2022-03-12T17:48:08Z
dc.date.available2022-03-12T17:48:08Z
dc.date.issued2010
dc.description.abstractOxidative stress is an inevitable process in the nucleus, especially in antitumor chemotherapy, and adaptation by defense mechanisms seems to be one element in the development of long-term resistance to many chemotherapeutic drugs. In this study, a potential chromatin repair mechanism during oxidative stress was investigated in HT22 cells. The 20S proteasome has been shown to be largely responsible for the degradation of oxidatively modified histone proteins in the nucleus. Poly(ADP-ribosyl)ation reactions also play an important role in DNA repair as a consequence of oxidative damage and single-strand breaks. Such a reaction may occur also with the 20S proteasome-with a known increase in enzymatic activity-and also with histones-reducing their proteolytic susceptibility as shown for the first time here. After hydrogen peroxide treatment of HT22 cells, degradation of the model peptide substrate suc-LLVY-MCA and degradation of oxidized histones by nuclear proteasome increased. During the removal of protein carbonyls, single-strand breaks and 8-hydroxy-2'-deoxyguanosine, proteasome, and poly(ADP-ribose) polymerase-1 enzymes were shown to play tightly interacting roles. Our results following the repair of oxidative damage show the proteolytic activation of proteasome concerning poly(ADP-ribosyl)ation together with a decline in poly(ADP-ribosyl)ation of oxidized histones, leading to a selective recognition of oxidatively modified histones. (C) 2009 Elsevier Inc. All rights reserved.
dc.identifier.doi10.1016/j.freeradbiomed.2009.12.010
dc.identifier.eissn1873-4596
dc.identifier.issn0891-5849
dc.identifier.pubmed20025963
dc.identifier.urihttps://hdl.handle.net/11424/229903
dc.identifier.wosWOS:000274503100005
dc.language.isoeng
dc.publisherELSEVIER SCIENCE INC
dc.relation.ispartofFREE RADICAL BIOLOGY AND MEDICINE
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectProtein oxidation
dc.subjectOxidative stress
dc.subjectHistone degradation
dc.subjectProteasome activation
dc.subjectPARP-1
dc.subjectFree radicals
dc.subjectADP-RIBOSE-POLYMERASE
dc.subjectPOLY(ADP-RIBOSE) POLYMERASE
dc.subjectCANCER-CHEMOTHERAPY
dc.subjectNUCLEAR PROTEASOME
dc.subjectHYDROGEN-PEROXIDE
dc.subjectMAMMALIAN-CELLS
dc.subject20S PROTEASOME
dc.subjectDNA-DAMAGE
dc.subjectDEGRADATION
dc.subjectINHIBITION
dc.titleChromatin repair after oxidative stress: Role of PARP-mediated proteasome activation
dc.typearticle
dspace.entity.typePublication
local.avesis.id9cd2c7de-02a8-4133-881a-f77f5f1754b7
local.import.packageSS17
local.indexed.atWOS
local.indexed.atSCOPUS
local.journal.numberofpages8
oaire.citation.endPage680
oaire.citation.issue5
oaire.citation.startPage673
oaire.citation.titleFREE RADICAL BIOLOGY AND MEDICINE
oaire.citation.volume48
relation.isAuthorOfPublication81633a07-e5fb-4760-b3ef-bf0878d87827
relation.isAuthorOfPublication.latestForDiscovery81633a07-e5fb-4760-b3ef-bf0878d87827

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