Mining of caspase-7 substrates using a degradomic approach = 단백질체를 이용한 신규 캐스페이즈7의 기질 발굴

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dc.contributor.authorMi Jang-
dc.contributor.authorByoung Chul Park-
dc.contributor.authorSunghyun Kang-
dc.contributor.authorD H Lee-
dc.contributor.authorS Cho-
dc.contributor.authorSang Chul Lee-
dc.contributor.authorKwang-Hee Bae-
dc.contributor.authorSung Goo Park-
dc.date.accessioned2017-04-19T09:11:32Z-
dc.date.available2017-04-19T09:11:32Z-
dc.date.issued2008-
dc.identifier.issn1016-8478-
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/8565-
dc.description.abstractCaspases play critical roles in the execution of apoptosis. Caspase-3 and caspase-7 are closely related in sequence as well as in substrate specificity. The two caspases have overlapping substrate specificities with special preference for the DEVD motif. However, they are targeted to different subcellular locations during apoptosis, implying the existence of substrates specific for one or other caspase. To identify new caspase-7 substrates, we digested cell lysates obtained from the caspase-3-deficient MCF-7 cell line with purified recombinant caspase-7, and analyzed spots that disappeared or decreased by 2-DE (we refer to this as the caspase-7 degradome). Several proteins with various cellular functions underwent caspase-7-dependent proteolysis. The substrates of capase-7 identified by the degradomic approach were rather different from those of caspase-3 (Proteomics, 4, 3429-3435, 2004). Among the candidate substrates, we confirmed that Valosin-containing protein (VCP) was cleaved by both capspase-7 and caspase-3 in vito and during apoptosis. Cleavage occurred at both DELD307 and DELD580. The degradomic study yielded several candidate caspase-7 substrates and their further analysis should provide valuables clues to the functions of caspase-7 during apoptosis.-
dc.publisherKorea Soc-Assoc-Inst-
dc.titleMining of caspase-7 substrates using a degradomic approach = 단백질체를 이용한 신규 캐스페이즈7의 기질 발굴-
dc.title.alternativeMining of caspase-7 substrates using a degradomic approach-
dc.typeArticle-
dc.citation.titleMolecules and Cells-
dc.citation.number2-
dc.citation.endPage157-
dc.citation.startPage152-
dc.citation.volume26-
dc.contributor.affiliatedAuthorMi Jang-
dc.contributor.affiliatedAuthorByoung Chul Park-
dc.contributor.affiliatedAuthorSunghyun Kang-
dc.contributor.affiliatedAuthorSang Chul Lee-
dc.contributor.affiliatedAuthorKwang-Hee Bae-
dc.contributor.affiliatedAuthorSung Goo Park-
dc.contributor.alternativeName장미-
dc.contributor.alternativeName박병철-
dc.contributor.alternativeName강성현-
dc.contributor.alternativeName이도희-
dc.contributor.alternativeName조사연-
dc.contributor.alternativeName이상철-
dc.contributor.alternativeName배광희-
dc.contributor.alternativeName박성구-
dc.identifier.bibliographicCitationMolecules and Cells, vol. 26, no. 2, pp. 152-157-
dc.subject.keyword2-DE-
dc.subject.keywordApoptosis-
dc.subject.keywordCaspase-7-
dc.subject.keywordDegradome-
dc.subject.keywordVCP-
dc.subject.local2-DE-
dc.subject.localapoptosis-
dc.subject.localApoptosis-
dc.subject.localCaspase-7-
dc.subject.localcaspase-7-
dc.subject.localDegradome-
dc.subject.localVCP-
dc.description.journalClassY-
Appears in Collections:
Critical Diseases Diagnostics Convergence Research Center > 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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