| http://purl.uniprot.org/citations/14688365 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/14688365 | http://www.w3.org/2000/01/rdf-schema#comment | "The urokinase receptor (CD87) participates to the pericellular proteolytic potential of migrating cells and to the recruitment of leukocytes during inflammation. It consists of three structurally homologous domains, with the C-terminal domain D3 attached to cell membranes through a GPI anchor. CD87 is susceptible to an endoproteolytic processing removing the N-terminal domain D1 and generating truncated D2D3 membrane species, thus modulating CD87-associated functions. Full-length or truncated CD87 can be also released from cells via juxtamembrane cleavage by phospholipases and/or by yet unidentified proteinases. Using a recombinant CD87 and the CD87-positive monocytic U937 cell line and isolated blood monocytes, we show by protein immunoblotting and flow immunocytometry that the human neutrophil serine-proteinases elastase and cathepsin G cleave CD87 within the D1-D2 linker sequence, while in addition cathepsin G is highly efficient in cleaving the C terminus of D3. The combination of cathepsin G and elastase provided by degranulated neutrophils results in enzymatic cooperation leading to the release from monocytic cells of a truncated D2D3 species resembling that previously described in pathological body fluids. Using mass spectrometry analysis, the proteolytic fragmentation of synthetic peptides mapping the D1-D2 linker and D3 C-terminal domains identifies potential cleavage sites for each enzyme and suggests the existence of a mechanism regulating the CD87(D1-D2)-associated chemotactic activity. Finally, isolated or combined elastase and cathepsin G drastically reduce the capacity of cells to bind urokinase. Secretable leukocyte serine-proteinases are thus endowed with high potential for the regulation of CD87 expression and function on inflammatory cells."xsd:string |
| http://purl.uniprot.org/citations/14688365 | http://purl.org/dc/terms/identifier | "doi:10.4049/jimmunol.172.1.540"xsd:string |
| http://purl.uniprot.org/citations/14688365 | http://purl.uniprot.org/core/author | "Namane A."xsd:string |
| http://purl.uniprot.org/citations/14688365 | http://purl.uniprot.org/core/author | "Leduc D."xsd:string |
| http://purl.uniprot.org/citations/14688365 | http://purl.uniprot.org/core/author | "Magdolen V."xsd:string |
| http://purl.uniprot.org/citations/14688365 | http://purl.uniprot.org/core/author | "Chignard M."xsd:string |
| http://purl.uniprot.org/citations/14688365 | http://purl.uniprot.org/core/author | "Rousselle J.C."xsd:string |
| http://purl.uniprot.org/citations/14688365 | http://purl.uniprot.org/core/author | "Beaufort N."xsd:string |
| http://purl.uniprot.org/citations/14688365 | http://purl.uniprot.org/core/author | "Pidard D."xsd:string |
| http://purl.uniprot.org/citations/14688365 | http://purl.uniprot.org/core/author | "Luther T."xsd:string |
| http://purl.uniprot.org/citations/14688365 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/14688365 | http://purl.uniprot.org/core/name | "J Immunol"xsd:string |
| http://purl.uniprot.org/citations/14688365 | http://purl.uniprot.org/core/pages | "540-549"xsd:string |
| http://purl.uniprot.org/citations/14688365 | http://purl.uniprot.org/core/title | "Proteolytic regulation of the urokinase receptor/CD87 on monocytic cells by neutrophil elastase and cathepsin G."xsd:string |
| http://purl.uniprot.org/citations/14688365 | http://purl.uniprot.org/core/volume | "172"xsd:string |
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