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Cytochrome P450, family 4, subfamily F, polypeptide 8

This gene, CYP4F8, encodes a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. This protein localizes to the endoplasmic reticulum and functions as a 19-hydroxylase of prostaglandins in seminal vesicles. This gene is part of a cluster of cytochrome P450 genes on chromosome 19. Another member of this family, CYP4F3, is approximately 18 kb away. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: ACID, fibrillin-1, CYP4F12, POLYMERASE, CYP4F11
Papers on CYP4F8
Pharmacogenomic characterization of gemcitabine response--a framework for data integration to enable personalized medicine.
Deeken et al., Silver Spring, United States. In Pharmacogenet Genomics, 2014
RESULTS: Genetic variants in the ABC transporters (ABCC1, ABCC4) and the CYP4 family members CYP4F8 and CYP4F12, CHST3, and PPARD were found to be significant in both the NCI-60 and GWAS data sets.
Arachidonic acid pathway members PLA2G7, HPGD, EPHX2, and CYP4F8 identified as putative novel therapeutic targets in prostate cancer.
Iljin et al., Turku, Finland. In Am J Pathol, 2011
The PLA2G7, HPGD, EPHX2, and CYP4F8 genes are highly expressed in prostate cancer.
LC-MS/MS analysis of epoxyalcohols and epoxides of arachidonic acid and their oxygenation by recombinant CYP4F8 and CYP4F22.
Oliw et al., Uppsala, Sweden. In Arch Biochem Biophys, 2010
CYP4F22 and CYP4F8 are expressed in epidermis, and mutations of CYP4F22 are associated with lamellar ichthyosis.
Co-localization of COX-2, CYP4F8, and mPGES-1 in epidermis with prominent expression of CYP4F8 mRNA in psoriatic lesions.
Oliw et al., Uppsala, Sweden. In Prostaglandins Other Lipid Mediat, 2006
Cyclooxygenase-2 (COX-2), cytochrome P450 4F8 (CYP4F8), and microsomal PGE synthase-1 (mPGES-1) form PGE and 19-hydroxy-PGE in human seminal vesicles.
Oxygenation of polyunsaturated long chain fatty acids by recombinant CYP4F8 and CYP4F12 and catalytic importance of Tyr-125 and Gly-328 of CYP4F8.
Oliw et al., Uppsala, Sweden. In Arch Biochem Biophys, 2005
We conclude that CYP4F8 and CYP4F12 catalyze epoxidation of 22:6n-3 and 22:5n-3, and CYP4F8 omega3-hydroxylation of 22:5n-6.
On the mechanism of biosynthesis of 19-hydroxyprostaglandins of human seminal fluid and expression of cyclooxygenase-2, PGH 19-hydroxylase (CYP4F8) and microsomal PGE synthase-1 in seminal vesicles and vas deferens.
Oliw et al., Uppsala, Sweden. In Prostaglandins Other Lipid Mediat, 2005
PGH synthase-2, CYP4F8, and PGE synthase-1 likely forms 19-hydroxy-PGE compounds in seminal vesicles and vas deferens
Expression of CYP4F8 (prostaglandin H 19-hydroxylase) in human epithelia and prominent induction in epidermis of psoriatic lesions.
Oliw et al., Uppsala, Sweden. In Arch Biochem Biophys, 2003
expression analysis of CYP4F8 shows that high levels are found in epithelial linings and epidermis of psoriatic lesions
Prostaglandin and leukotriene omega-hydroxylases.
Kusunose et al., Fukuyama, Japan. In Prostaglandins Other Lipid Mediat, 2002
Human seminal vesicle CYP4F8 is the first elucidated hydroxylase with substrate specificity for PG endoperoxides, whereas ram seminal vesicle CYP4F21 is the only elucidated PGE omega-hydroxylase within the CYP4F subfamily [corrected].
Oxidation of prostaglandin H(2) and prostaglandin H(2) analogues by human cytochromes P450: analysis of omega-side chain hydroxy metabolites and four steroisomers of 5-hydroxyprostaglandin I(1) by mass spectrometry.
Bylund et al., Uppsala, Sweden. In Biochem Pharmacol, 2001
CYP2C19, CYP4A11, CYP4F8, and liver and renal cortical microsomes oxidized the omega-side chain of U44069, U46619, and U51605, whereas only CYP4F8 oxidized the omega-side chain of PGH(2).
A novel cytochrome P450 enzyme responsible for the metabolism of ebastine in monkey small intestine.
Miyazaki et al., Ōsaka, Japan. In Drug Metab Dispos, 2001
The internal amino acid sequence of P450 MI-2 had high similarity with those of human CYP4F2, CYP4F3, and CYP4F8.
Cloning and characterization of CYP4F21: a prostaglandin E2 20-hydroxylase of ram seminal vesicles.
Oliw et al., Uppsala, Sweden. In Arch Biochem Biophys, 2001
The deduced protein sequence of CYP4F21 contained 528 amino acids and showed 74% amino acid identity with CYP4F8 of human seminal vesicles.
cDNA cloning and expression of a novel cytochrome p450 (cyp4f12) from human small intestine.
Funae et al., Suita, Japan. In Biochem Biophys Res Commun, 2001
This cDNA contains an entire coding region of a 524-amino-acid protein that is 81.7, 78.3, and 78.2% identical to CYP4F2, CYP4F3, and CYP4F8, respectively.
cDna cloning and expression of CYP4F12, a novel human cytochrome P450.
Oliw et al., Uppsala, Sweden. In Biochem Biophys Res Commun, 2001
The open reading frame coded for 524 amino acids, and the sequence could be aligned with 78-83% amino acid identity to the four human CYP4F enzymes (CYP4F2, CYP4F3, CYP4F8 and CYP4F11).
A novel human cytochrome P450 4F isoform (CYP4F11): cDNA cloning, expression, and genomic structural characterization.
Strobel et al., Houston, United States. In Genomics, 2000
The CYP4F11 amino acid sequence has 80.0, 82.3, and 79.2% identity to CYP4F2, CYP4F3, and CYP4F8 amino acid sequences, respectively.
Identification of CYP4F8 in human seminal vesicles as a prominent 19-hydroxylase of prostaglandin endoperoxides.
Oliw et al., Uppsala, Sweden. In J Biol Chem, 2000
A novel cytochrome P450, CYP4F8, was recently cloned from human seminal vesicles.
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