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http://purl.uniprot.org/citations/10570282http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10570282http://www.w3.org/2000/01/rdf-schema#comment"The cellular effects of stromal cell-derived factor-1 (SDF-1) are mediated primarily by binding to the CXC chemokine receptor-4. We report in this study that SDF-1 and its peptide analogues induce a concentration- and time-dependent accumulation of phosphatidylinositol-(3,4,5)-trisphosphate (PtdIns(3,4,5)P3) in Jurkat cells. This SDF-1-stimulated generation of D-3 phosphoinositide lipids was inhibited by pretreatment of the cells with an SDF-1 peptide antagonist or an anti-CXCR4 Ab. In addition, the phosphoinositide 3 (PI 3)-kinase inhibitors wortmannin and LY294002, as well as the Gi protein inhibitor pertussis toxin, also inhibited the SDF-1-stimulated accumulation of PtdIns(3,4,5)P3. The effects of SDF-1 on D-3 phosphoinositide lipid accumulation correlated well with activation of the known PI 3-kinase effector protein kinase B, which was also inhibited by wortmannin and pertussis toxin. Concentrations of PI 3-kinase inhibitors, sufficient to inhibit PtdIns(3,4,5)P3 accumulation, also inhibited chemotaxis of Jurkat and peripheral blood-derived T lymphocytes in response to SDF-1. In contrast, SDF-1-stimulated actin polymerization was only partially inhibited by PI 3-kinase inhibitors, suggesting that while chemotaxis is fully dependent on PI 3-kinase activation, actin polymerization requires additional biochemical inputs. Finally, SDF-1-stimulated extracellular signal-related kinase (ERK)-1/2 mitogen-activated protein kinase activation was inhibited by PI 3-kinase inhibitors. In addition, the mitogen-activated protein/ERK kinase inhibitor PD098059 partially attenuated chemotaxis in response to SDF-1. Hence, it appears that ERK1/2 activation is dependent on PI 3-kinase activation, and both biochemical events are involved in the regulation of SDF-1-stimulated chemotaxis."xsd:string
http://purl.uniprot.org/citations/10570282http://purl.uniprot.org/core/author"Westwick J."xsd:string
http://purl.uniprot.org/citations/10570282http://purl.uniprot.org/core/author"Ward S.G."xsd:string
http://purl.uniprot.org/citations/10570282http://purl.uniprot.org/core/author"Sotsios Y."xsd:string
http://purl.uniprot.org/citations/10570282http://purl.uniprot.org/core/author"Whittaker G.C."xsd:string
http://purl.uniprot.org/citations/10570282http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10570282http://purl.uniprot.org/core/name"J Immunol"xsd:string
http://purl.uniprot.org/citations/10570282http://purl.uniprot.org/core/pages"5954-5963"xsd:string
http://purl.uniprot.org/citations/10570282http://purl.uniprot.org/core/title"The CXC chemokine stromal cell-derived factor activates a Gi-coupled phosphoinositide 3-kinase in T lymphocytes."xsd:string
http://purl.uniprot.org/citations/10570282http://purl.uniprot.org/core/volume"163"xsd:string
http://purl.uniprot.org/citations/10570282http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10570282
http://purl.uniprot.org/citations/10570282http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10570282
http://purl.uniprot.org/uniprot/P31749#attribution-327F44B6F324CD35722074F2B209F597http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/10570282
http://purl.uniprot.org/uniprot/Q02750#attribution-327F44B6F324CD35722074F2B209F597http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/10570282
http://purl.uniprot.org/uniprot/P42338#attribution-327F44B6F324CD35722074F2B209F597http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/10570282
http://purl.uniprot.org/uniprot/P42338#attribution-F2E0FB4B67681677747F29D95947AB3Ehttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/10570282
http://purl.uniprot.org/uniprot/P48061#attribution-327F44B6F324CD35722074F2B209F597http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/10570282