Expression and characterization of cytochrome P450 2X1 in channel catfish (Ictalurus punctatus)

Mosadeghi, Sasan; Furnes, Bjarte; Matsuo, Aline Y.O.; Schlenk, Daniel

doi:10.1016/j.bbagen.2007.03.008

Cited by 16 publications

(8 citation statements)

References 21 publications

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“…The CYP2X genes do not appear to share synteny with any mammalian CYP. Catalytic activities of CYP2Xs in zebrafish are unknown, although CYP2X1 from channel catfish has been cloned [76] and heterologously expressed [77]. Aminopyrine and benzphetamine demethylase activities were observed, but no biological function has as yet been ascribed.…”

Section: Resultsmentioning

confidence: 99%

Identification and developmental expression of the full complement of Cytochrome P450 genes in Zebrafish

McArthur²,

et al. 2010

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BackgroundIncreasing use of zebrafish in drug discovery and mechanistic toxicology demands knowledge of cytochrome P450 (CYP) gene regulation and function. CYP enzymes catalyze oxidative transformation leading to activation or inactivation of many endogenous and exogenous chemicals, with consequences for normal physiology and disease processes. Many CYPs potentially have roles in developmental specification, and many chemicals that cause developmental abnormalities are substrates for CYPs. Here we identify and annotate the full suite of CYP genes in zebrafish, compare these to the human CYP gene complement, and determine the expression of CYP genes during normal development.ResultsZebrafish have a total of 94 CYP genes, distributed among 18 gene families found also in mammals. There are 32 genes in CYP families 5 to 51, most of which are direct orthologs of human CYPs that are involved in endogenous functions including synthesis or inactivation of regulatory molecules. The high degree of sequence similarity suggests conservation of enzyme activities for these CYPs, confirmed in reports for some steroidogenic enzymes (e.g. CYP19, aromatase; CYP11A, P450scc; CYP17, steroid 17a-hydroxylase), and the CYP26 retinoic acid hydroxylases. Complexity is much greater in gene families 1, 2, and 3, which include CYPs prominent in metabolism of drugs and pollutants, as well as of endogenous substrates. There are orthologous relationships for some CYP1 s and some CYP3 s between zebrafish and human. In contrast, zebrafish have 47 CYP2 genes, compared to 16 in human, with only two (CYP2R1 and CYP2U1) recognized as orthologous based on sequence. Analysis of shared synteny identified CYP2 gene clusters evolutionarily related to mammalian CYP2 s, as well as unique clusters.ConclusionsTranscript profiling by microarray and quantitative PCR revealed that the majority of zebrafish CYP genes are expressed in embryos, with waves of expression of different sets of genes over the course of development. Transcripts of some CYP occur also in oocytes. The results provide a foundation for the use of zebrafish as a model in toxicological, pharmacological and chemical disease research.

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Section: Resultsmentioning

confidence: 99%

Identification and developmental expression of the full complement of Cytochrome P450 genes in Zebrafish

McArthur²,

et al. 2010

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“…In catfish, however, their function could be replaced by other CYP genes during evolution. For example, CYP2X1 in channel catfish have been proved to possess benzphetamine demethylase activity (110). In addition, only subfamilies CYP 1A, CYP 1B, CYP 2U and CYP 2R appear to be evolutionarily conserved across species.…”

Section: Discussionmentioning

confidence: 99%

The cytochrome P450 genes of channel catfish: Their involvement in disease defense responses as revealed by meta-analysis of RNA-Seq data sets

Zhang

Yao

Wang

et al. 2014

Biochimica et Biophysica Acta (BBA) - General Subjects

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Background Cytochrome P450s (CYPs) encode one of the most diverse enzyme superfamily in nature. They catalyze oxidative reactions of endogenous molecules and exogenous chemicals. Methods We identified CYPs genes through in silico analysis using EST, RNA-Seq and genome databases of channel catfish. Phylogenetic analyses and conserved syntenic analyses were conducted to determine their identities and orthologies. Meta-analysis of RNA-Seq databases was conducted to analyze expression profile of CYP genes following bacterial infection. Results A full set of 61 CYP genes were identified and characterized in channel catfish. Phylogenetic tree and conserved synteny provided strong evidence of their identities and orthorlogy. Lineage-specific gene duplication was evident in a number of clans in channel catfish. CYP46A1 is missing in the catfish genome as observed with syntenic analysis and RT-PCR analysis. Thirty CYPs were found up- or down-regulated in liver, while seven and eight CYPs were observed regulated in intestine and gill following bacterial infection. Conclusion We systematically identified and characterized a full set of 61 CYP genes in channel catfish and studied their expression profiles after bacterial infection. Strikingly large numbers of CYP genes appear to be involved in the bacterial defense processes. General significance This work provides an example to systematically study CYP genes in non-model species. Moreover, it provides a basis for further toxicological and physiological studies in channel catfish.

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“…More than 11,290 distinct sequences were named in 2009 according to Dr. Nelson's Home Page records . CYP1A, CYP3A, CYP2K, CYP2M, CYP2N, CYP2P, CYP2V, CYP2X, CYP3C, CYP4T, and CYP2B‐like protein are cytochrome P450 subfamilies that have been purified or cloned from different fish species .…”

Section: Introductionmentioning

confidence: 99%

Aldrin Epoxidation in Flathead Mullet (Mugil cephalus): Possible Involvement of CYP1A and CYP3A

Bozcaarmutlu

Turna

Sapmaz

et al. 2014

J Biochem Mol Toxicol

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The primary objective of this study was to determine specific cytochrome P450 isozyme(s) involved in the metabolism of aldrin to its toxic metabolite dieldrin in flathead mullet (Mugil cephalus) liver microsomes. To identify the cytochrome P450 isozyme responsible for the aldrin metabolism in mullet liver, the effects of mammalian-specific cytochrome P450 inhibitors and substrates were determined in the epoxidation reaction of aldrin. CYP3A-related inhibitors, ketoconazole, SKF-525A, and cimetidine, inhibited the metabolism of aldrin. The contribution of CYP1A to the aldrin metabolism was shown by the inhibition of 7-ethoxyresorufin-O-deethylase activity in the presence of aldrin. The results indicate that CY1A and CYP3A are the cytochrome P450s involved in aldrin epoxidase activity in mullet. In addition, the suitability of aldrin epoxidase activity for monitoring of environmental pollution was also assessed in the fish samples caught from four different locations of the West Black Sea coast of Turkey.

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Expression and characterization of cytochrome P450 2X1 in channel catfish (Ictalurus punctatus)

Cited by 16 publications

References 21 publications

Identification and developmental expression of the full complement of Cytochrome P450 genes in Zebrafish

Identification and developmental expression of the full complement of Cytochrome P450 genes in Zebrafish

The cytochrome P450 genes of channel catfish: Their involvement in disease defense responses as revealed by meta-analysis of RNA-Seq data sets

Aldrin Epoxidation in Flathead Mullet (Mugil cephalus): Possible Involvement of CYP1A and CYP3A

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