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Cytochrome P450, family 4, subfamily F, polypeptide 12

CYP4F12, Cytochrome P450 4F12
This gene 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 likely localizes to the endoplasmic reticulum. When expressed in yeast the enzyme is capable of oxdizing arachidonic acid; however, its physiological function has not been determined. This gene is part of a cluster of cytochrome P450 genes on chromosome 19. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: ACID, CYP3A4, CYP4F11, POLYMERASE, CYP2J2
Papers on CYP4F12
Immunochemical quantification of cynomolgus CYP2J2, CYP4A and CYP4F enzymes in liver and small intestine.
Uno et al., Kainan, Japan. In Xenobiotica, Feb 2015
2. In this study, cynomolgus CYP4A11, CYP4F2/3, CYP4F11 and CYP4F12, along with CYP2J2, were immunoquantified using selective antibodies in 28 livers and 35 small intestines, and their content was compared with CYP1A, CYP2A, CYP2B6, CYP2C9/19, CYP2D, CYP2E1, CYP3A4 and CYP3A5, previously quantified.
Characterization of the active site properties of CYP4F12.
Foti et al., Chengde, China. In Drug Metab Dispos, 2014
Cytochrome P450 4F12 is a drug-metabolizing enzyme that is primarily expressed in the liver, kidney, colon, small intestine, and heart.
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.
Chemotherapeutic agents induce the expression and activity of their clearing enzyme CYP3A4 by activating p53.
Rotter et al., Israel. In Carcinogenesis, 2013
In a microarray screen performed in human liver cells, we found a group of eleven P450 genes whose expression was induced by p53 (CYP3A4, CYP3A43, CYP3A5, CYP3A7, CYP4F2, CYP4F3, CYP4F11, CYP4F12, CYP19A1, CYP21A2 and CYP24A1).
Effect of estradiol on gene expression profile in cynomolgus macaque liver: implications for drug-metabolizing enzymes.
Kito et al., Sapporo, Japan. In Drug Metab Dispos, 2011
Expression of drug-metabolizing enzyme genes was also influenced by estradiol treatment; estradiol enhanced expression of GSTM5 (3.8-fold, P < 0.05) and CYP3A8(4) (2.7-fold, P < 0.01), but lowered expression of CYP4F12 (2.2-fold, P < 0.01), as verified by quantitative polymerase chain reaction.
CYP4F3B expression is associated with differentiation of HepaRG human hepatocytes and unaffected by fatty acid overload.
Corlu et al., France. In Drug Metab Dispos, 2011
When treated with saturated, monounsaturated, or polyunsaturated fatty acids, CYP4F3B and CYP4A11 expression remained unchanged whereas CYP4F2 and CYP4F12 expression was transiently up-regulated.
Genistein, resveratrol, and 5-aminoimidazole-4-carboxamide-1-β-D-ribofuranoside induce cytochrome P450 4F2 expression through an AMP-activated protein kinase-dependent pathway.
Johnson et al., Los Angeles, United States. In J Pharmacol Exp Ther, 2011
A 24-h treatment of either primary human hepatocytes or the human hepatoma cell line HepG2 with 5-aminoimidazole-4-carboxamide-1-β-D-ribofuranoside (AICAR), which is converted to 5-aminoimidazole-4-carboxamide-1-β-D-ribofuranosyl 5'-monophosphate, an activator of AMPK, caused an average 2.5- or 7-fold increase, respectively, of CYP4F2 mRNA expression but not of CYP4A11 or CYP4F3, CYP4F11, and CYP4F12 mRNA.
Identification of pregnane-X receptor target genes and coactivator and corepressor binding to promoter elements in human hepatocytes.
Evers et al., Rahway, United States. In Nucleic Acids Res, 2009
Of these, only CYP4F12 demonstrated increased binding in the presence of rifampicin.
Distinction between human cytochrome P450 (CYP) isoforms and identification of new phosphorylation sites by mass spectrometry.
Marcus et al., Bochum, Germany. In J Proteome Res, 2008
In the present work, we demonstrate the performance of a mass spectrometry-based strategy to simultaneously detect and differentiate distinct human Cytochrome P450 (CYP) isoforms including the highly similar CYP3A4, CYP3A5, CYP3A7, as well as CYP2C8, CYP2C9, CYP2C18, CYP2C19, and CYP4F2, CYP4F3, CYP4F11, CYP4F12.
Expression of CYP4F2 in human liver and kidney: assessment using targeted peptide antibodies.
Lasker et al., Hackensack, United States. In Arch Biochem Biophys, 2008
Peptide antibodies elicited in rabbits to CYP4F2 amino acid residues 61-74 (WGHQGMVNPTEEG) and 65-77 (GMVNPTEEGMRVL) recognized on immunoblots only CYP4F2 and not CYP4F3b, CYP4F11 or CYP4F12.
Omega oxidation of 3-hydroxy fatty acids by the human CYP4F gene subfamily enzyme CYP4F11.
Lasker et al., Hackensack, United States. In J Lipid Res, 2008
3-hydroxystearate and 3-hydroxypalmitate are converted to omega-hydroxylated 3-OHDCA precursors in liver; CYP4F11 and, to a lesser extent, CYP4F2 catalyzed omega-hydroxylation of 3-hydroxystearate; CYP4F3b, CYP4F12, and CYP4A11 had negligible activity.
Expression and physiological function of CYP4F subfamily in human eosinophils.
Ohkawa et al., Fukuyama, Japan. In Biochim Biophys Acta, 2007
CYP4F12 mRNA was detected in eosinophils and neutrophils.
Characterization of cynomolgus monkey cytochrome P450 (CYP) cDNAs: is CYP2C76 the only monkey-specific CYP gene responsible for species differences in drug metabolism?
Nagata et al., Sapporo, Japan. In Arch Biochem Biophys, 2007
To determine if CYP2C76 is the only monkey-specific CYP gene, we identified cynomolgus monkey cDNAs for CYP2A23, CYP2A24, CYP2E1, CYP2J2, CYP3A5, CYP3A8, CYP4A11, CYP4F3, CYP4F11, CYP4F12, and CYP4F45.
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.
Human CYP4F12 genetic polymorphism: identification and functional characterization of seven variant allozymes.
Broly et al., Lille, France. In Biochem Pharmacol, 2005
The human cytochrome CYP4F12 has been shown to be metabolically active toward inflammatory mediators and exogenous compounds such as antihistaminic drugs.
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