| http://purl.uniprot.org/citations/26599267 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/26599267 | http://www.w3.org/2000/01/rdf-schema#comment | "Mononuclear phagocytes utilize caspase-1 activation as a means to respond to danger signals. Although caspase-1 was discovered using highly concentrated cell extracts that spontaneously activate caspase-1, it is now clear that in live cell models caspase-1 activation occurs in the process of its cellular release and is not an intracellular event. Therefore, we compared the characteristics of caspase-1 activation in the cell lysate model to that of caspase-1 that is released in response to exogenous inflammasome activation. Whereas both models generated active caspase-1, the cell-lysate induced caspase-1 required highly concentrated cell lysates and had a short half-life (~15 min) whereas, the activation induced released caspase-1 required 2-3 log fold fewer cells and was stable for greater than 12 h. Both forms were able to cleave proIL-1beta but unexpectedly, the released activity was unable to be immunodepleted by caspase-1 antibodies. Size exclusion chromatography identified two antigenic forms of p20 caspase-1 in the activation induced released caspase-1: one at the predicted size of tetrameric, p20/p10 caspase-1 and the other at >200 kDa. However, only the high molecular weight form had stable functional activity. These results suggest that released caspase-1 exists in a unique complex that is functionally stable and protected from immunodepletion whereas cell-extract generated active caspase-1 is rapidly inhibited in the cytosolic milieu."xsd:string |
| http://purl.uniprot.org/citations/26599267 | http://purl.org/dc/terms/identifier | "doi:10.1371/journal.pone.0142203"xsd:string |
| http://purl.uniprot.org/citations/26599267 | http://purl.uniprot.org/core/author | "Mitra S."xsd:string |
| http://purl.uniprot.org/citations/26599267 | http://purl.uniprot.org/core/author | "Wewers M.D."xsd:string |
| http://purl.uniprot.org/citations/26599267 | http://purl.uniprot.org/core/author | "Gavrilin M.A."xsd:string |
| http://purl.uniprot.org/citations/26599267 | http://purl.uniprot.org/core/author | "Shamaa O.R."xsd:string |
| http://purl.uniprot.org/citations/26599267 | http://purl.uniprot.org/core/date | "2015"xsd:gYear |
| http://purl.uniprot.org/citations/26599267 | http://purl.uniprot.org/core/name | "PLoS One"xsd:string |
| http://purl.uniprot.org/citations/26599267 | http://purl.uniprot.org/core/pages | "e0142203"xsd:string |
| http://purl.uniprot.org/citations/26599267 | http://purl.uniprot.org/core/title | "Monocyte Caspase-1 Is Released in a Stable, Active High Molecular Weight Complex Distinct from the Unstable Cell Lysate-Activated Caspase-1."xsd:string |
| http://purl.uniprot.org/citations/26599267 | http://purl.uniprot.org/core/volume | "10"xsd:string |
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