Cytochrome P450 super family proteins are monooxygenases which catalyze multiple biochemical reactions involved in drug metabolism and synthesis of cholesterol, steroids and lipids. CYP4F3, a 60 kDa protein, is a novel member of this family. It consists of a conserved heme-binding domain near the C-terminus and catalyzes the u-hydroxylation of LTB4. CYP4F3 is localized in the ER and plays a vital role in the inactivation of LTB4 and controlling inflammation. CYP4F3 exists in two functionally distinct isoforms: CYP4F3A, a neutrophil isoform, is particularly expressed in neutrophils and myeloid cells and catalyzes the microsomal u-hydroxylation of LTB4. It interacts with CD11b and myeloperoxidase on myeloid cells and regulates cellular development in bone marrow. CYP4F3B, a liver isoform, catalyzes the conversion of arachidonic acid to 20-HETE, a potent activator of PKC. Its role has been implicated in cell proliferation, vascular tone and natriuresis.
20-HETE synthase; 20-hydroxyeicosatetraenoic acid synthase; CYPIVF3; cytochrome P-450; Cytochrome P450 4F3; cytochrome P450, family 4, subfamily F, polypeptide 3; cytochrome P450, subfamily IVF, polypeptide 3 (leukotriene B4 omega hydroxylase); Cytochrome P450-LTB-omega; Docosahexaenoic acid omega-hydroxylase CYP4F3; leukotriene B4 omega hydroxylase; Leukotriene-B(4) 20-monooxygenase 2; Leukotriene-B(4) omega-hydroxylase 2; leukotriene-B4 20-monooxygenase