Identification, characterization, and ontogeny of a second cytochrome P450 3A gene from the fresh water teleost medaka (Oryzias latipes)

Kullman, Seth W.; Hinton, David E.

doi:10.1002/1098-2795(200102)58:2<149::aid-mrd3>3.0.co;2-x

Cited by 28 publications

(16 citation statements)

References 33 publications

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“…Previous studies have demonstrated the developmental expression of multiple CYP3As (Stevens et al, 2003;Aleksa et al, 2005). Thus, CYP3A4 and CYP3A7 are expressed specifically in adult and fetal human livers, respectively (Komori et al, 1990), and distinct CYP3As are differentially expressed in embryonic and adult fish (Kullman and Hinton, 2001). …”

Section: Discussionmentioning

confidence: 99%

Isolation and phylogeny of novel cytochrome P450 genes from tunicates (Ciona spp.): A CYP3 line in early deuterostomes?

Verslycke

Goldstone

Stegeman

2006

Molecular Phylogenetics and Evolution

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Cytochromes P450 (CYPs) form a gene superfamily involved in the biotransformation of numerous endogenous and exogenous natural and synthetic compounds. In humans, CYP3A4 is regarded as one of the most important CYPs due to its abundance in liver and its capacity to metabolize more than 50% of all clinically used drugs. It has been suggested that all CYP3s arose from a common ancestral gene lineage that diverged between 800 and 1100 million years ago, before the deuterostome-protostome split. While CYP3s are well known in mammals and have been described in lower vertebrates, they have not been reported in non-vertebrate deuterostomes. Members of the genus Ciona belong to the tunicates, whose lineage is thought to be the most basal among the chordates, and from which the vertebrate line diverged. Here we describe the cloning, exon-intron structure, phylogeny, and estimated expression of four novel genes from Ciona intestinalis. We also describe the gene structure and phylogeny of homologous genes in Ciona savignyi. Comparing these genes with other members of the CYP clan 3, show that the Ciona sequences bear remarkable similarity to vertebrate CYP3A genes, and may be an early deuterostome CYP3 line.

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Section: Discussionmentioning

confidence: 99%

Isolation and phylogeny of novel cytochrome P450 genes from tunicates (Ciona spp.): A CYP3 line in early deuterostomes?

Verslycke

Goldstone

Stegeman

2006

Molecular Phylogenetics and Evolution

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“…However, the intestine has been shown to be the major extrahepatic site of expression of various CYP3A isoforms in rainbow trout (Lee et al, 1998(Lee et al, , 2001, killifish (Hegelund and Celander, 2003) and zebrafish (Tseng et al, 2005). The expression of CYP3A40 mRNA has been identified in liver of the fish species medaka (Kullman and Hinton, 2001), but information regarding distribution and induction of this isoform is scarce. Soy contains several phytochemicals such as isoflavons and phytosterols that could potentially induce the expression of CYP3A40 mRNA in the SBM group of the present study.…”

Section: Discussionmentioning

confidence: 99%

Comparison of intestinal gene expression in Atlantic cod (Gadus morhua) fed standard fish meal or soybean meal by means of suppression subtractive hybridization and real-time PCR

et al. 2007

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Gene expression was studied in Atlantic cod fed two different diets, fish meal (FM) and dehulled and extracted soybean meal (SBM). RNA was isolated from the distal part of the mid-intestine of Atlantic cod and suppression subtractive hybridization (SSH) was employed to screen for genes that showed changes in expression in response to the two dietary treatments. We made a cDNA subtracted library, isolated and sequenced 192 clones. Identification of 157 clones was predicted by BLAST. Most of the clones were previously unidentified in cod. Expression of 12 selected clones was further studied by quantitative PCR. Expression of four clones showing similarity to aminopeptidase N, transcobalamin I precursor, cytochrome P450 3A40, and ras-related nuclear protein was significantly up regulated in intestine of cod fed SBM compared to cod fed FM. A trend towards up regulation of a clone with similarity to fatty acid binding protein in SBM-fed cod was also observed. No significant differences in expression were observed for: transmembrane 4 superfamily protein member, polypeptide N-acetylgalactosaminyltransferase, glutathione peroxidase, peroxiredoxin 4, SEC61, F-BOX, and 14-3-3.

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“…As another control experiment to control the functionality of the CYP3A assay, we incubated ZFL and FHM cells with different concentrations of BFC (10,20,30,40, and 50 mM). There was a clear correlation between measured fluorescence and concentration of BFC.…”

Section: Dependency Of Cyp3a Activity On Bfc Concentrationmentioning

confidence: 99%

“…Induction of CYP3A expression by rifampicin and dexamethasone has been shown to occur in fish [7]. Cytochrome P450 3A was identified in several teleost species (e.g., CYP3A27 and CYP3A45 in rainbow trout [5,8], CYP3A38 and CYP3A40 in medaka [9,10], CYP3A30 and CYP3A56 in killifish [11], and CYP3A65 in Danio rerio [7]). …”

Section: Introductionmentioning

confidence: 99%

A microtiter‐plate‐based cytochrome P450 3A activity assay in fish cell lines

Christen

Oggier

Fent

2009

Enviro Toxic and Chemistry

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Abstract-Enzymes belonging to the cytochrome P450 3A (CYP3A) subfamily play an important role in the metabolism of endogenous substances and xenobiotics, including pharmaceuticals. Xenobiotics can alter CYP3A expression and activity, and therefore, changes in CYP3A activity may serve as a biomarker of xenobiotic exposure. To determine changes in CYP3A enzyme activity for environmental risk assessment of xenobiotics including pharmaceuticals, high-throughput assays are needed, but these are missing for fish cells to date. Here, we report on the development of a fluorescent-based CYP3A high-throughput assay for four fish cell lines cultivated in 96-well plates based on 7-benzyloxy-4-trifluoromethylcoumarin as a CYP3A substrate. We show that human CYP3A substrate BFC is catalyzed by fish CYP3A enzymes to a fluorescent product. Its formation is dependent on cell numbers and incubation time. Furthermore, we demonstrate that with this new CYP3A assay induction and inhibition of enzyme activity by pharmaceuticals can be determined. This new cell-based assay is suitable for detection of alteration in CYP3A enzyme activity in largescale experiments for screening of pharmaceuticals occurring in the environment.

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Identification, characterization, and ontogeny of a second cytochrome P450 3A gene from the fresh water teleost medaka (Oryzias latipes)

Cited by 28 publications

References 33 publications

Isolation and phylogeny of novel cytochrome P450 genes from tunicates (Ciona spp.): A CYP3 line in early deuterostomes?

Isolation and phylogeny of novel cytochrome P450 genes from tunicates (Ciona spp.): A CYP3 line in early deuterostomes?

Comparison of intestinal gene expression in Atlantic cod (Gadus morhua) fed standard fish meal or soybean meal by means of suppression subtractive hybridization and real-time PCR

A microtiter‐plate‐based cytochrome P450 3A activity assay in fish cell lines

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