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http://purl.uniprot.org/citations/11520793http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11520793http://www.w3.org/2000/01/rdf-schema#comment"In the inflammatory response, leukocyte rolling before adhesion and transmigration through the blood vessel wall is mediated by specific cell surface adhesion receptors. Neutrophil rolling involves the interaction of P-selectin expressed on activated endothelium and its counter-receptor on neutrophils, P-selectin glycoprotein ligand-1 (PSGL-1). Here, it is reported that P-selectin binding to neutrophils is lost under conditions that cause the release of proteinases from neutrophil primary granules. Treatment of neutrophils with the purified neutrophil granule proteinases, cathepsin G and elastase, rapidly abolished their capacity to bind P-selectin. This inactivation corresponded to loss of the N-terminal domain of PSGL-1, as assessed by Western blot analysis. A loss of intact PSGL-1 protein from the surfaces of neutrophils after the induction of degranulation was also detected by Western blot analysis. Cathepsin G initially cleaved near the PSGL-1 N-terminus, whereas neutrophil elastase predominantly cleaved at a more C-terminal site within the protein mucin core. Consistent with this, cathepsin G cleaved a synthetic peptide based on the PSGL-1 N-terminus between Tyr-7/Leu-8. Under conditions producing neutrophil degranulation in incubations containing mixtures of platelets and neutrophils, the loss of PSGL-1, but not P-selectin, from platelet-neutrophil lysates was detected. Cathepsin G- or neutrophil elastase-mediated PSGL-1 proteolysis may constitute a potential autocrine mechanism for down-regulation of neutrophil adhesion to P-selectin."xsd:string
http://purl.uniprot.org/citations/11520793http://purl.org/dc/terms/identifier"doi:10.1182/blood.v98.5.1440"xsd:string
http://purl.uniprot.org/citations/11520793http://purl.uniprot.org/core/author"Berndt M.C."xsd:string
http://purl.uniprot.org/citations/11520793http://purl.uniprot.org/core/author"Andrews R.K."xsd:string
http://purl.uniprot.org/citations/11520793http://purl.uniprot.org/core/author"Gardiner E.E."xsd:string
http://purl.uniprot.org/citations/11520793http://purl.uniprot.org/core/author"McNally T."xsd:string
http://purl.uniprot.org/citations/11520793http://purl.uniprot.org/core/author"Michelson A.D."xsd:string
http://purl.uniprot.org/citations/11520793http://purl.uniprot.org/core/author"De Luca M."xsd:string
http://purl.uniprot.org/citations/11520793http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11520793http://purl.uniprot.org/core/name"Blood"xsd:string
http://purl.uniprot.org/citations/11520793http://purl.uniprot.org/core/pages"1440-1447"xsd:string
http://purl.uniprot.org/citations/11520793http://purl.uniprot.org/core/title"Regulation of P-selectin binding to the neutrophil P-selectin counter-receptor P-selectin glycoprotein ligand-1 by neutrophil elastase and cathepsin G."xsd:string
http://purl.uniprot.org/citations/11520793http://purl.uniprot.org/core/volume"98"xsd:string
http://purl.uniprot.org/citations/11520793http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11520793
http://purl.uniprot.org/citations/11520793http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11520793
http://purl.uniprot.org/uniprot/#_P08311-mappedCitation-11520793http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/11520793
http://purl.uniprot.org/uniprot/P08311http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/11520793