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Molecular Pharmacology

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Research ArticleArticle

cDNA Cloning and Initial Characterization of CYP3A43, a Novel Human Cytochrome P450

Tammy L. Domanski, Csaba Finta, James R. Halpert and Peter G. Zaphiropoulos
Molecular Pharmacology February 2001, 59 (2) 386-392; DOI: https://doi.org/10.1124/mol.59.2.386
Tammy L. Domanski
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Csaba Finta
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James R. Halpert
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Peter G. Zaphiropoulos
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Abstract

The RACE amplification technology was used on a novel CYP3A-like exon 1 sequence detected during the reverse transcriptase/polymerase chain reaction analysis of human CYP3A gene expression. This resulted in the identification of cDNAs encompassing the complete coding sequence of a new member of the CYP3A gene subfamily, CYP3A43. Interestingly, the majority of the cDNAs identified were characterized by alternative splicing events such as exon skipping and complete or partial intron inclusion.CYP3A43 expression was detected in liver, kidney, pancreas, and prostate. The amino acid sequence is 75% identical to that of CYP3A4 and CYP3A5 and 71% identical to CYP3A7. CYP3A43 differs from CYP3A4 at six amino acid residues, found within the putative substrate recognition sites of CYP3A4, that are known to be determinants of substrate selectivity. The N terminus of CYP3A43 was modified for efficient expression of the protein in Escherichia coli, and a 6X histidine tag was added at the C terminus to facilitate purification. CYP3A43 gave a reduced carbon monoxide difference spectra with an absorbance maximum at 450 nm. The level of heterologous expression was significantly lower than that observed for CYP3A4 and CYP3A5. Immunoblot analyses revealed that CYP3A43 comigrates with CYP3A4 in polyacrylamide gel electrophoresis but does separate from CYP3A5. Monooxygenase assays were performed under a variety of conditions, several of which yielded reproducible, albeit low, testosterone hydroxylase activity. The findings from this study demonstrate that there is a novel CYP3A member expressed in human tissues, although its relative contribution to drug metabolism has yet to be ascertained.

Footnotes

    • Received August 7, 2000.
    • Accepted October 30, 2000.
  • Send reprint requests to: Tammy Domanski, Department of Pharmacology and Toxicology, University of Texas Medical Branch, 301 University Blvd., Galveston, TX 77555-1031. E-mail:tadomans{at}utmb.edu

  • ↵1 GenBank Accession Number .

  • This work was supported by National Institutes of Health Grants GM54995 and Center Grant ES06676, the Swedish Natural Science Research Council, the Åke Wibergs Foundation, and the Karolinska Institute.

  • T.L.D. and C.F. contributed equally to this work.

  • The American Society for Pharmacology and Experimental Therapeutics
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Molecular Pharmacology: 59 (2)
Molecular Pharmacology
Vol. 59, Issue 2
1 Feb 2001
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Research ArticleArticle

cDNA Cloning and Initial Characterization of CYP3A43, a Novel Human Cytochrome P450

Tammy L. Domanski, Csaba Finta, James R. Halpert and Peter G. Zaphiropoulos
Molecular Pharmacology February 1, 2001, 59 (2) 386-392; DOI: https://doi.org/10.1124/mol.59.2.386

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Research ArticleArticle

cDNA Cloning and Initial Characterization of CYP3A43, a Novel Human Cytochrome P450

Tammy L. Domanski, Csaba Finta, James R. Halpert and Peter G. Zaphiropoulos
Molecular Pharmacology February 1, 2001, 59 (2) 386-392; DOI: https://doi.org/10.1124/mol.59.2.386
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