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(Received for publication, July 25, 1996, and in revised form, August 30, 1996)
From the Retinoic acid (RA) metabolites of vitamin A are
key regulators of gene expression involved in embryonic development and
maintenance of epithelial tissues. The cellular effects of RA are
dependent upon the complement of nuclear receptors expressed (RARs and
RXRs), which transduce retinoid signals into transcriptional
regulation, the presence of cellular retinoid-binding proteins (CRABP
and CRBP), which may be involved in RA metabolism, and the activity of
RA metabolizing enzymes. We have been using the zebrafish as a model to
study these processes. To identify genes regulated by RA during
exogenous RA exposure, we utilized mRNA differential display. We
describe the isolation and characterization of a cDNA, P450RAI,
encoding a novel member of the cytochrome P450 family. mRNA
transcripts for P450RAI are expressed normally during gastrulation, and
in a defined pattern in epithelial cells of the regenerating caudal fin
in response to exogenous RA. In COS-1 cells transfected with the
P450RAI cDNA, all-trans-RA is rapidly metabolized to more polar metabolites. We have identified 4-oxo-RA and 4-OH-RA as
major metabolic products of this enzyme. P450RAI represents the first
enzymatic component of RA metabolism to be isolated and characterized
at the molecular level and provides key insight into regulation of
retinoid homeostasis.
Volume 271, Number 47,
Issue of November 22, 1996
pp. 29922-29927
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
§
,
,
,
,
,
and§¶
Cancer Research Laboratories, Departments of
§ Pathology, ¶ Biochemistry, and 
Medicine,
Queen's University, Kingston, Ontario, K7L 3N6 Canada
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S. S. Abu-Abed, B. R. Beckett, H. Chiba, J. V. Chithalen, G. Jones, D. Metzger, P. Chambon, and M. Petkovich Mouse P450RAI (CYP26) Expression and Retinoic Acid-inducible Retinoic Acid Metabolism in F9 Cells Are Regulated by Retinoic Acid Receptor gamma and Retinoid X Receptor alpha J. Biol. Chem., January 23, 1998; 273(4): 2409 - 2415. [Abstract] [Full Text] [PDF]
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J. A. White, B. Beckett-Jones, Y.-D. Guo, F. J. Dilworth, J. Bonasoro, G. Jones, and M. Petkovich cDNA Cloning of Human Retinoic Acid-metabolizing Enzyme (hP450RAI) Identifies a Novel Family of Cytochromes P450 (CYP26) J. Biol. Chem., July 25, 1997; 272(30): 18538 - 18541. [Abstract] [Full Text] [PDF]
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W. J. Ray, G. Bain, M. Yao, and D. I. Gottlieb CYP26, a Novel Mammalian Cytochrome P450, Is Induced by Retinoic Acid and Defines a New Family J. Biol. Chem., July 25, 1997; 272(30): 18702 - 18708. [Abstract] [Full Text] [PDF]
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J. A. White, H. Ramshaw, M. Taimi, W. Stangle, A. Zhang, S. Everingham, S. Creighton, S.-P. Tam, G. Jones, and M. Petkovich Identification of the human cytochrome P450, P450RAI-2, which is predominantly expressed in the adult cerebellum and is responsible for all-trans-retinoic acid metabolism PNAS, June 6, 2000; 97(12): 6403 - 6408. [Abstract] [Full Text] [PDF]
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