Histone H4 is cleaved by granzyme A during staurosporine-induced cell death in B-lymphoid Raji cells

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dc.contributor.authorPhil Young Lee-
dc.contributor.authorByoung Chul Park-
dc.contributor.authorSeung-Wook Chi-
dc.contributor.authorKwang-Hee Bae-
dc.contributor.authorSunhong Kim-
dc.contributor.authorS Cho-
dc.contributor.authorS Kang-
dc.contributor.authorJeong Hoon Kim-
dc.contributor.authorSung Goo Park-
dc.date.accessioned2017-04-19T10:27:59Z-
dc.date.available2017-04-19T10:27:59Z-
dc.date.issued2016-
dc.identifier.issn1225-8687-
dc.identifier.uri10.5483/BMBRep.2016.49.10.105ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/13458-
dc.description.abstractGranzyme A (GzmA) was first identified as a cytotoxic T lymphocyte protease protein with limited tissue expression. A number of cellular proteins are known to be cleaved by GzmA, and its function is to induce apoptosis. Histones H1, H2B, and H3 were identified as GzmA substrates during apoptotic cell death. Here, we demonstrated that histone H4 was cleaved by GzmA during staurosporine-induced cell death; however, in the presence of caspase inhibitors, staurosporine-treated Raji cells underwent necroptosis instead of apoptosis. Furthermore, histone H4 cleavage was blocked by the GzmA inhibitor nafamostat mesylate and by GzmA knockdown using siRNA. These results suggest that histone H4 is a novel substrate for GzmA in staurosporine-induced cells.-
dc.publisherKorea Soc-Assoc-Inst-
dc.titleHistone H4 is cleaved by granzyme A during staurosporine-induced cell death in B-lymphoid Raji cells-
dc.title.alternativeHistone H4 is cleaved by granzyme A during staurosporine-induced cell death in B-lymphoid Raji cells-
dc.typeArticle-
dc.citation.titleBMB Reports-
dc.citation.number10-
dc.citation.endPage565-
dc.citation.startPage560-
dc.citation.volume49-
dc.contributor.affiliatedAuthorPhil Young Lee-
dc.contributor.affiliatedAuthorByoung Chul Park-
dc.contributor.affiliatedAuthorSeung-Wook Chi-
dc.contributor.affiliatedAuthorKwang-Hee Bae-
dc.contributor.affiliatedAuthorSunhong Kim-
dc.contributor.affiliatedAuthorJeong Hoon Kim-
dc.contributor.affiliatedAuthorSung Goo Park-
dc.contributor.alternativeName이필영-
dc.contributor.alternativeName박병철-
dc.contributor.alternativeName지승욱-
dc.contributor.alternativeName배광희-
dc.contributor.alternativeName김선홍-
dc.contributor.alternativeName조사연-
dc.contributor.alternativeName강성만-
dc.contributor.alternativeName김정훈-
dc.contributor.alternativeName박성구-
dc.identifier.bibliographicCitationBMB Reports, vol. 49, no. 10, pp. 560-565-
dc.identifier.doi10.5483/BMBRep.2016.49.10.105-
dc.subject.keywordCaspase-independent cell death-
dc.subject.keywordGranzyme A-
dc.subject.keywordHistone H4-
dc.subject.keywordRaji cell-
dc.subject.localCaspase-independent cell death-
dc.subject.localGranzyme A-
dc.subject.localHistone H4-
dc.subject.localRaji cell-
dc.description.journalClassY-
Appears in Collections:
Critical Diseases Diagnostics Convergence Research Center > 1. Journal Articles
Division of Biomedical Research > 1. Journal Articles
Division of Biomedical Research > Metabolic Regulation Research Center > 1. Journal Articles
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
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