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Division of Basic Sciences, National Cancer Institute, NIH, Bethesda, Maryland 20892-4255 [F. A., P. M. F-S., M. V. C., F. J. G., L. M. D. L.], and Cancer Research Laboratories, Queen's University, Kingston, Ontario, Canada K7L 3N6 [M. P. P.]
Livers from aryl hydrocarbon receptor-null mice showed a 3-fold increase in retinoids and a 65% decrease in retinoic acid metabolism. Levels of expression of the retinoic acid 4-hydroxylase, P450RAI, did not change, whereas cytochrome P4501A2 levels were lower in the null mouse, as shown earlier; however, this enzyme was found not to be active toward retinoic acid. These data suggest that aryl hydrocarbon receptor controls retinoic acid catabolism, through modulation of an unidentified target gene. Aldehyde dehydrogenases 1 and 2 were down-regulated markedly in the aryl hydrocarbon receptor-deficient mouse liver. 2,3,7,8-Tetrachlorodibenzo-p-dioxin induced cytochrome P4501A2 but not the aldehyde dehydrogenases in wild-type mice, suggesting that aryl hydrocarbon receptor is not involved directly in the down-regulation of this gene. Transglutaminase II, a retinoic acid-responsive gene product, was increased 2-fold, consistent with the liver fibrosis phenotype observed in the null mice. These findings suggest a molecular connection between xenobioticactivated receptor signaling and retinoid homeostasis.
1 These two authors contributed equally to this work.
2 To whom requests for reprints should be addressed, at Building 37, Room 3A-17, LCCTP, National Cancer Institute, NIH, 37 Convent Drive, Bethesda, MD 20892-4255. Phone: (301) 496-2698; Fax: (301) 496-8709.
Received 5/ 7/97. Accepted 5/29/97.
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