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http://purl.uniprot.org/citations/16380383http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16380383http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16380383http://www.w3.org/2000/01/rdf-schema#comment"Leukotriene B(4) (LTB(4)) is a potent chemoattractant for polymorphonuclear leukocytes (PMN) and other cells. Human PMN inactivate LTB(4) by omega-oxidation catalyzed by cytochrome P-450 (CYP) 4F3A. The contribution of the enzymatic inactivation of LTB(4) by CYP4Fs to down-regulating functional responses of cells to LTB(4) is unknown. To elucidate the role of CYP4F-mediated inactivation of LTB(4) in terminating the responses of PMN to LTB(4) and to identify a target for future genetic studies in mice, we have identified the enzyme that catalyzes the omega-1 and omega-2 oxidation of LTB(4) in mouse myeloid cells as CYP4F18. As determined by mass spectrometry, this enzyme catalyzes the conversion of LTB(4) to 19-OH LTB(4) and to a lesser extent 18-OH LTB(4). Inhibition of CYP4F18 resulted in a marked increase in calcium flux and a 220% increase in the chemotactic response of mouse PMN to LTB(4). CYP4F18 expression was induced in bone marrow-derived dendritic cells by bacterial lipopolysaccharide, a ligand for TLR4, and by poly(I.C), a ligand for TLR3. However, when bone marrow-derived myeloid dendritic cells trafficked to popliteal lymph nodes from paw pads, the expression of CYP4F18 was down-regulated. The results identify CYP4F18 as a critical protein in the regulation of LTB(4) metabolism and functional responses in mouse PMN and identify it as the functional orthologue of human PMN CYP4F3A."xsd:string
http://purl.uniprot.org/citations/16380383http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m513101200"xsd:string
http://purl.uniprot.org/citations/16380383http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m513101200"xsd:string
http://purl.uniprot.org/citations/16380383http://purl.uniprot.org/core/author"Chen M."xsd:string
http://purl.uniprot.org/citations/16380383http://purl.uniprot.org/core/author"Chen M."xsd:string
http://purl.uniprot.org/citations/16380383http://purl.uniprot.org/core/author"Christmas P."xsd:string
http://purl.uniprot.org/citations/16380383http://purl.uniprot.org/core/author"Christmas P."xsd:string
http://purl.uniprot.org/citations/16380383http://purl.uniprot.org/core/author"Lee D.M."xsd:string
http://purl.uniprot.org/citations/16380383http://purl.uniprot.org/core/author"Lee D.M."xsd:string
http://purl.uniprot.org/citations/16380383http://purl.uniprot.org/core/author"Soberman R.J."xsd:string
http://purl.uniprot.org/citations/16380383http://purl.uniprot.org/core/author"Soberman R.J."xsd:string
http://purl.uniprot.org/citations/16380383http://purl.uniprot.org/core/author"Murphy R.C."xsd:string
http://purl.uniprot.org/citations/16380383http://purl.uniprot.org/core/author"Murphy R.C."xsd:string
http://purl.uniprot.org/citations/16380383http://purl.uniprot.org/core/author"Berry K.Z."xsd:string
http://purl.uniprot.org/citations/16380383http://purl.uniprot.org/core/author"Berry K.Z."xsd:string
http://purl.uniprot.org/citations/16380383http://purl.uniprot.org/core/author"Primo V."xsd:string
http://purl.uniprot.org/citations/16380383http://purl.uniprot.org/core/author"Primo V."xsd:string
http://purl.uniprot.org/citations/16380383http://purl.uniprot.org/core/author"Tolentino K."xsd:string
http://purl.uniprot.org/citations/16380383http://purl.uniprot.org/core/author"Tolentino K."xsd:string
http://purl.uniprot.org/citations/16380383http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16380383http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16380383http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/16380383http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string