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http://purl.uniprot.org/citations/17889653http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17889653http://www.w3.org/2000/01/rdf-schema#comment"Extracellular serpins such as antithrombin and alpha1-antitrypsin are the quintessential regulators of proteolytic pathways. In contrast, the biological functions of the intracellular serpins remain obscure. We now report that the C. elegans intracellular serpin, SRP-6, exhibits a prosurvival function by blocking necrosis. Minutes after hypotonic shock, srp-6 null animals underwent a catastrophic series of events culminating in lysosomal disruption, cytoplasmic proteolysis, and death. This newly defined hypo-osmotic stress lethal (Osl) phenotype was dependent upon calpains and lysosomal cysteine peptidases, two in vitro targets of SRP-6. By protecting against both the induction of and the lethal effects from lysosomal injury, SRP-6 also blocked death induced by heat shock, oxidative stress, hypoxia, and cation channel hyperactivity. These findings suggest that multiple noxious stimuli converge upon a peptidase-driven, core stress response pathway that, in the absence of serpin regulation, triggers a lysosomal-dependent necrotic cell death routine."xsd:string
http://purl.uniprot.org/citations/17889653http://purl.org/dc/terms/identifier"doi:10.1016/j.cell.2007.07.013"xsd:string
http://purl.uniprot.org/citations/17889653http://purl.uniprot.org/core/author"Bromme D."xsd:string
http://purl.uniprot.org/citations/17889653http://purl.uniprot.org/core/author"Watkins S.C."xsd:string
http://purl.uniprot.org/citations/17889653http://purl.uniprot.org/core/author"Stolz D.B."xsd:string
http://purl.uniprot.org/citations/17889653http://purl.uniprot.org/core/author"Long O.S."xsd:string
http://purl.uniprot.org/citations/17889653http://purl.uniprot.org/core/author"Luke C.J."xsd:string
http://purl.uniprot.org/citations/17889653http://purl.uniprot.org/core/author"Pak S.C."xsd:string
http://purl.uniprot.org/citations/17889653http://purl.uniprot.org/core/author"Silverman G.A."xsd:string
http://purl.uniprot.org/citations/17889653http://purl.uniprot.org/core/author"Barstead R.J."xsd:string
http://purl.uniprot.org/citations/17889653http://purl.uniprot.org/core/author"Askew D.J."xsd:string
http://purl.uniprot.org/citations/17889653http://purl.uniprot.org/core/author"Askew Y.S."xsd:string
http://purl.uniprot.org/citations/17889653http://purl.uniprot.org/core/author"Moulder G.L."xsd:string
http://purl.uniprot.org/citations/17889653http://purl.uniprot.org/core/author"Nobar S.M."xsd:string
http://purl.uniprot.org/citations/17889653http://purl.uniprot.org/core/author"Naviglia T.L."xsd:string
http://purl.uniprot.org/citations/17889653http://purl.uniprot.org/core/author"Vetica A.C."xsd:string
http://purl.uniprot.org/citations/17889653http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17889653http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/17889653http://purl.uniprot.org/core/pages"1108-1119"xsd:string
http://purl.uniprot.org/citations/17889653http://purl.uniprot.org/core/title"An intracellular serpin regulates necrosis by inhibiting the induction and sequelae of lysosomal injury."xsd:string
http://purl.uniprot.org/citations/17889653http://purl.uniprot.org/core/volume"130"xsd:string
http://purl.uniprot.org/citations/17889653http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17889653
http://purl.uniprot.org/citations/17889653http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/17889653
http://purl.uniprot.org/uniprot/#_A0A8I6A3B4-mappedCitation-17889653http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17889653