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http://purl.uniprot.org/citations/14517301http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14517301http://www.w3.org/2000/01/rdf-schema#comment"Phospholipase C (PLC) plays important roles in phosphoinositide turnover by regulating the calcium-protein kinase C signaling pathway. PLC-L2 is a novel PLC-like protein which lacks PLC activity, although it is very homologous with PLC delta. PLC-L2 is expressed in hematopoietic cells, but its physiological roles and intracellular functions in the immune system have not yet been clarified. To elucidate the physiological function of PLC-L2, we generated mice which had a genetic PLC-L2 deficiency. PLC-L2-deficient mice grew with no apparent abnormalities. However, mature B cells from PLC-L2-deficient mice were hyperproliferative in response to B-cell receptor (BCR) cross-linking, although B2 cell development appeared to be normal. Molecular biological analysis revealed that calcium influx and NFATc accumulation in nuclei were increased in PLC-L2-deficient B cells. Extracellular signal-regulated kinase activity was also enhanced in PLC-L2-deficient B cells. These mice had a stronger T-cell-independent antigen response. These results indicate that PLC-L2 is a novel negative regulator of BCR signaling and immune responses."xsd:string
http://purl.uniprot.org/citations/14517301http://purl.org/dc/terms/identifier"doi:10.1128/mcb.23.20.7329-7338.2003"xsd:string
http://purl.uniprot.org/citations/14517301http://purl.uniprot.org/core/author"Nakamura Y."xsd:string
http://purl.uniprot.org/citations/14517301http://purl.uniprot.org/core/author"Nishikawa S."xsd:string
http://purl.uniprot.org/citations/14517301http://purl.uniprot.org/core/author"Tsuji K."xsd:string
http://purl.uniprot.org/citations/14517301http://purl.uniprot.org/core/author"Wada M."xsd:string
http://purl.uniprot.org/citations/14517301http://purl.uniprot.org/core/author"Yoshida N."xsd:string
http://purl.uniprot.org/citations/14517301http://purl.uniprot.org/core/author"Takenawa T."xsd:string
http://purl.uniprot.org/citations/14517301http://purl.uniprot.org/core/author"Kataoka Y."xsd:string
http://purl.uniprot.org/citations/14517301http://purl.uniprot.org/core/author"Fukami K."xsd:string
http://purl.uniprot.org/citations/14517301http://purl.uniprot.org/core/author"Takenaka K."xsd:string
http://purl.uniprot.org/citations/14517301http://purl.uniprot.org/core/author"Otsuki M."xsd:string
http://purl.uniprot.org/citations/14517301http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/14517301http://purl.uniprot.org/core/name"Mol Cell Biol"xsd:string
http://purl.uniprot.org/citations/14517301http://purl.uniprot.org/core/pages"7329-7338"xsd:string
http://purl.uniprot.org/citations/14517301http://purl.uniprot.org/core/title"Role of phospholipase C-L2, a novel phospholipase C-like protein that lacks lipase activity, in B-cell receptor signaling."xsd:string
http://purl.uniprot.org/citations/14517301http://purl.uniprot.org/core/volume"23"xsd:string
http://purl.uniprot.org/citations/14517301http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/14517301
http://purl.uniprot.org/citations/14517301http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/14517301
http://purl.uniprot.org/uniprot/Q8K394#attribution-E962840B47CB183FE516743347E73CEBhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/14517301
http://purl.uniprot.org/uniprot/#_Q8K394-mappedCitation-14517301http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/14517301
http://purl.uniprot.org/uniprot/Q8K394http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/14517301