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http://purl.uniprot.org/citations/9261102http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9261102http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/9261102http://www.w3.org/2000/01/rdf-schema#comment"Members of the CED-3/interleukin-1beta-converting enzyme (ICE) protease (caspase) family are synthesized as proforms, which are proteolytically cleaved and activated during apoptosis. We report here that caspase-2 (ICH-1/NEDD-2), a member of the ICE family, is activated during apoptosis by another ICE member, a caspase-3 (CPP32)-like protease(s). When cells are induced to undergo apoptosis, endogenous caspase-2 is first cleaved into three fragments of 32-33 kDa and 14 kDa, which are then further processed into 18- and 12-kDa active subunits. Up to 50 microM N-acetyl-Asp-Glu-Val-Asp-aldehyde (DEVD-CHO), a caspase-3-preferred peptide inhibitor, inhibits caspase-2 activation and DNA fragmentation in vivo, but does not prevent loss of mitochondrial function, while higher concentrations of DEVD-CHO (>50 microM) inhibit both. In comparison, although the activity of caspase-3 is very sensitive to the inhibition of DEVD-CHO (<50 nM), inhibition of caspase-3 activation as marked by processing of the proform requires more than 100 microM DEVD-CHO. Our results suggest that the first cleavage of caspase-2 is accomplished by a caspase-3-like activity, and other ICE-like proteases less sensitive to DEVD-CHO may be responsible for activation of caspase-3 and loss of mitochondrial function."xsd:string
http://purl.uniprot.org/citations/9261102http://purl.org/dc/terms/identifier"doi:10.1074/jbc.272.34.21010"xsd:string
http://purl.uniprot.org/citations/9261102http://purl.uniprot.org/core/author"Li H."xsd:string
http://purl.uniprot.org/citations/9261102http://purl.uniprot.org/core/author"Zhu H."xsd:string
http://purl.uniprot.org/citations/9261102http://purl.uniprot.org/core/author"Yuan J."xsd:string
http://purl.uniprot.org/citations/9261102http://purl.uniprot.org/core/author"Shi L."xsd:string
http://purl.uniprot.org/citations/9261102http://purl.uniprot.org/core/author"Greenberg A."xsd:string
http://purl.uniprot.org/citations/9261102http://purl.uniprot.org/core/author"Bergeron L."xsd:string
http://purl.uniprot.org/citations/9261102http://purl.uniprot.org/core/author"Pasternack M.S."xsd:string
http://purl.uniprot.org/citations/9261102http://purl.uniprot.org/core/author"Cryns V."xsd:string
http://purl.uniprot.org/citations/9261102http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9261102http://purl.uniprot.org/core/name"J Biol Chem"xsd:string
http://purl.uniprot.org/citations/9261102http://purl.uniprot.org/core/pages"21010-21017"xsd:string
http://purl.uniprot.org/citations/9261102http://purl.uniprot.org/core/title"Activation of caspase-2 in apoptosis."xsd:string
http://purl.uniprot.org/citations/9261102http://purl.uniprot.org/core/volume"272"xsd:string
http://purl.uniprot.org/citations/9261102http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9261102
http://purl.uniprot.org/citations/9261102http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9261102
http://purl.uniprot.org/citations/9261102http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9261102
http://purl.uniprot.org/citations/9261102http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9261102
http://purl.uniprot.org/enzyme/3.4.22.55http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/9261102
http://purl.uniprot.org/enzyme/3.4.22.56http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/9261102
http://purl.uniprot.org/uniprot/#_P42575-mappedCitation-9261102http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/9261102
http://purl.uniprot.org/uniprot/P42575http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/9261102