Publication | Open Access
Cloning and expression of a novel form of leukotriene B<sub>4</sub> ω‐hydroxylase from human liver
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Citations
27
References
1994
Year
Lipid PeroxidationMolecular BiologyOxidative StressProtein ExpressionBiochemical GeneticsHepatotoxicityHuman MetabolismBiochemistryLiver PhysiologyGene ExpressionPharmacologyLiverHuman LiverProtein BiosynthesisLtb4 Omega-hydroxylaseHuman PmnCellular EnzymologyNatural SciencesCellular BiochemistryMetabolismMedicineLipid SynthesisNovel Form
We have isolated and sequenced a cDNA for human liver LTB4 omega-hydroxylase. The cDNA encoded a protein of 520 amino acids with a molecular weight of 59,853 Da. The cDNA-deduced amino acid sequence showed 87.3% homology to that of human polymorphonuclear leukocytes (PMN) LTB4 omega-hydroxylase (CYP4F3). Northern blot analysis revealed that the mRNA hybridized to the specific cDNA fragment is expressed in human liver, but not in human PMN. The microsomes from yeast cells transfected with the cDNA catalyzed the omega-hydroxylation of LTB4 with a Km of 44.8 microM. These results clearly show that a new form of the CYP4F LTB4 omega-hydroxylase exists in human liver.
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