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http://purl.uniprot.org/citations/12891708http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12891708http://www.w3.org/2000/01/rdf-schema#comment"C1qRP/CD93 is a cell surface receptor predominantly expressed on monocytes, neutrophils, endothelial cells, and early stem cell precursors. In phagocytic cells, it has been characterized as contributing to the enhancement of FcR- and CR1-induced phagocytosis triggered by innate immune system defense collagens such as C1q and mannose binding lectin (MBL). Previously, we demonstrated a high level of glycosylation on C1qRP/CD93 that was predominantly O-linked. In this study, we investigate the role of glycosylation in C1qRP/CD93 stability first by inhibiting O-glycosylation by addition of benzyl 2-acetamido-2-deoxy-alpha-D-galactopyranoside (BAG) to the human histiocytic cell line U937, and secondly, by expression of C1qRP/CD93 in the CHO-derived cell line ldlD which has a reversible defect in protein glycosylation. In both U937 cells and in ldlD cells transfected to express C1qRP/CD93, glycosylation deficiency caused cell surface expression levels of C1qRP/CD93 to decrease, concomitant with the detection of C1qRP/CD93 reactivity in the culture media. Metabolic labeling studies show that when glycosylation is absent, C1qRP/CD93 is synthesized and rapidly released into the culture supernatant or degraded. These studies demonstrate that O-glycosylation is important in the stable cell surface expression of C1qRP/CD93 ."xsd:string
http://purl.uniprot.org/citations/12891708http://purl.org/dc/terms/identifier"doi:10.1002/jcp.10332"xsd:string
http://purl.uniprot.org/citations/12891708http://purl.uniprot.org/core/author"Park M."xsd:string
http://purl.uniprot.org/citations/12891708http://purl.uniprot.org/core/author"Tenner A.J."xsd:string
http://purl.uniprot.org/citations/12891708http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12891708http://purl.uniprot.org/core/name"J Cell Physiol"xsd:string
http://purl.uniprot.org/citations/12891708http://purl.uniprot.org/core/pages"512-522"xsd:string
http://purl.uniprot.org/citations/12891708http://purl.uniprot.org/core/title"Cell surface expression of C1qRP/CD93 is stabilized by O-glycosylation."xsd:string
http://purl.uniprot.org/citations/12891708http://purl.uniprot.org/core/volume"196"xsd:string
http://purl.uniprot.org/citations/12891708http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12891708
http://purl.uniprot.org/citations/12891708http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12891708
http://purl.uniprot.org/uniprot/#_B4DSX2-mappedCitation-12891708http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/12891708
http://purl.uniprot.org/uniprot/#_Q9NPY3-mappedCitation-12891708http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/12891708
http://purl.uniprot.org/uniprot/#_Q59EB6-mappedCitation-12891708http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/12891708
http://purl.uniprot.org/uniprot/#_Q8IXK1-mappedCitation-12891708http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/12891708
http://purl.uniprot.org/uniprot/Q9NPY3http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/12891708
http://purl.uniprot.org/uniprot/Q59EB6http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/12891708
http://purl.uniprot.org/uniprot/Q8IXK1http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/12891708
http://purl.uniprot.org/uniprot/B4DSX2http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/12891708