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J Biol Chem, Vol. 275, Issue 17, 12530-12536, April 28, 2000

The Murine and Human Cholesterol 7alpha -Hydroxylase Gene Promoters Are Differentially Responsive to Regulation by Fatty Acids Mediated via Peroxisome Proliferator-activated Receptor alpha *

Sukhinder K. CheemaDagger and Luis B. Agellon§

From the Medical Research Council Group on Molecular and Cell Biology of Lipids and the Department of Biochemistry, University of Alberta, Edmonton, Alberta T6G 2S2, Canada

We determined if fatty acids can regulate the murine Cyp7a1 and human CYP7A1 gene promoters via peroxisome proliferator-activated receptor alpha  (PPARalpha )/9-cis-retinoic acid receptor alpha  (RXRalpha ). In transfected cells, the murine Cyp7a1 gene promoter displayed markedly lower basal activity, but greater sensitivity to fatty acid- or WY 14,643-activated PPARalpha /RXRalpha when compared with the human CYP7A1 gene promoter. PPARalpha /RXRalpha can bind to a site (Site II) located within the region at nucleotides -158 to -132 of both promoters. Mutagenesis of the human CYP7A1 Site II element abolished the response to activated PPARalpha /RXRalpha . The murine Cyp7a1 gene promoter contains an additional PPARalpha /RXRalpha -binding site (Site I) located within nucleotides -72 to -57. Replacement of a single residue in human CYP7A1 Site I with that found in the murine Cyp7a1 Site I sequence enabled PPARalpha /RXRalpha binding, and this mutation resulted in reduced basal activity, but substantially improved the response to activated PPARalpha /RXRalpha in transfected cells. We conclude that fatty acids can regulate the cyp7a gene promoter via PPARalpha /RXRalpha . The differential response of the murine Cyp7a1 and human CYP7A1 gene promoters to PPARalpha activators is attributable to the additional PPARalpha /RXRalpha -binding site in the murine Cyp7a1 gene promoter.

* This work was supported by Grant MT-14812 (to L. B. A.) from the Medical Research Council of Canada.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Present address: Dept. of Biochemistry, BT 3012, Memorial University of Newfoundland, St. John's, NF A1B 3X9, Canada.

§ Senior Medical Scholar of the Alberta Heritage Foundation for Medical Research. To whom correspondence should be addressed: 303 Heritage Medical Research Centre, Dept. of Biochemistry, University of Alberta, Edmonton, AB T6G 2S2, Canada. Tel.: 780-492-5251; Fax: 780-492-3383; E-mail: luis.agellon@ualberta.ca.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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