Identification of the novel substrates for caspase-6 in apoptosis using proteomic approaches

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dc.contributor.authorJin Hwa Cho-
dc.contributor.authorPhil Young Lee-
dc.contributor.authorW C Son-
dc.contributor.authorSeung-Wook Chi-
dc.contributor.authorByoung Chul Park-
dc.contributor.authorJeong Hoon Kim-
dc.contributor.authorSung Goo Park-
dc.date.accessioned2017-04-19T09:50:25Z-
dc.date.available2017-04-19T09:50:25Z-
dc.date.issued2013-
dc.identifier.issn1225-8687-
dc.identifier.uri10.5483/BMBRep.2013.46.12.081ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/11804-
dc.description.abstractApoptosis, programmed cell death, is a process involved in the development and maintenance of cell homeostasis in multicellular organisms. It is typically accompanied by the activation of a class of cysteine proteases called caspases. Apoptotic caspases are classified into the initiator caspases and the executioner caspases, according to the stage of their action in apoptotic processes. Although caspase-3, a typical executioner caspase, has been studied for its mechanism and substrates, little is known of caspase-6, one of the executioner caspases. To understand the biological functions of caspase-6, we performed proteomics analyses, to seek for novel caspase-6 substrates, using recombinant caspase-6 and HepG2 extract. Consequently, 34 different candidate proteins were identified, through 2-dimensional electrophoresis/MALDI-TOF analyses. Of these identified proteins, 8 proteins were validated with in vitro and in vivo cleavage assay. Herein, we report that HAUSP, Kinesin5B, GEP100, SDCCAG3 and PARD3 are novel substrates for caspase-6 during apoptosis.-
dc.publisherKorea Soc-Assoc-Inst-
dc.titleIdentification of the novel substrates for caspase-6 in apoptosis using proteomic approaches-
dc.title.alternativeIdentification of the novel substrates for caspase-6 in apoptosis using proteomic approaches-
dc.typeArticle-
dc.citation.titleBMB Reports-
dc.citation.number12-
dc.citation.endPage593-
dc.citation.startPage588-
dc.citation.volume46-
dc.contributor.affiliatedAuthorJin Hwa Cho-
dc.contributor.affiliatedAuthorPhil Young Lee-
dc.contributor.affiliatedAuthorSeung-Wook Chi-
dc.contributor.affiliatedAuthorByoung Chul Park-
dc.contributor.affiliatedAuthorJeong Hoon Kim-
dc.contributor.affiliatedAuthorSung Goo Park-
dc.contributor.alternativeName조진화-
dc.contributor.alternativeName이필영-
dc.contributor.alternativeName손우찬-
dc.contributor.alternativeName지승욱-
dc.contributor.alternativeName박병철-
dc.contributor.alternativeName김정훈-
dc.contributor.alternativeName박성구-
dc.identifier.bibliographicCitationBMB Reports, vol. 46, no. 12, pp. 588-593-
dc.identifier.doi10.5483/BMBRep.2013.46.12.081-
dc.subject.keywordApoptosis-
dc.subject.keywordCaspase-6-
dc.subject.keywordDegradomics-
dc.subject.keywordProteomic screening-
dc.subject.keywordSubstrate-
dc.subject.localApoptosis-
dc.subject.localapoptosis-
dc.subject.localCaspase-6-
dc.subject.localDegradomics-
dc.subject.localProteomic screening-
dc.subject.localSubstrate-
dc.subject.localSubstrates-
dc.description.journalClassY-
Appears in Collections:
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
Division of Biomedical Research > 1. Journal Articles
Critical Diseases Diagnostics Convergence Research Center > 1. Journal Articles
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