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Nucleic Acids Research, 2003, Vol. 31, No. 12 3194-3207
© 2003 Oxford University Press

Alternatively spliced isoforms of the human constitutive androstane receptor

Scott S. Auerbach, Richard Ramsden1, Matthew A. Stoner3, Christophe Verlinde2, Christopher Hassett3 and Curtis J. Omiecinski3

Department of Pharmacology, 1 Department of Environmental Health, 2 Department of Biological Structure, University of Washington, Seattle, WA, USA and 3 Department of Veterinary Science, 115 Henning Building, The Pennsylvania State University, University Park, PA 16802, USA

*To whom correspondence should be addressed. Tel: +1 814 863 1625; Fax: +1 814 863 6140; Email: cjo10{at}psu.edu

The nuclear receptor CAR (NR1I3) regulates transcription of genes encoding xenobiotic- and steroid-metabolizing enzymes. Regulatory processes that are mediated by CAR are modulated by a structurally diverse array of chemicals including common pharmaceutical and environmental agents. Here we describe four in-frame splice variants of the human CAR receptor gene. The variant mRNA splice transcripts were expressed in all human livers evaluated. Molecular modeling of the splice variant proteins predicts that the structural effects are localized within the receptor’s ligand-binding domain. Assays to assess function indicate that the variant proteins, when compared with the reference protein isoform, exhibit compromised activities with respect to DNA binding, transcriptional activation and coactivator recruitment.


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