This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Copyright Permission Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Li, X.-H. Articles by Ong, D. E. Search for Related Content PubMed PubMed Citation Articles by Li, X.-H. Articles by Ong, D. E.

Estrogen Directly Induces Expression of Retinoic Acid Biosynthetic Enzymes, Compartmentalized between the Epithelium and Underlying Stromal Cells in Rat Uterus

Department of Biochemistry, School of Medicine, Vanderbilt University, Nashville, Tennessee 37232

Address all correspondence and Requests for Reprints to: David E. Ong, Department of Biochemistry, Vanderbilt University, 23rd Avenue at Pierce, Nashville, Tennessee 37232. E-mail: david.e.ong{at}vanderbilt.edu.

Estrogen (E₂) has been shown to induce the biosynthesis of retinoic acid (RA) in rat uterus. Here we examined whether E₂ could directly induce the enzymes involved in this process by using the ovariectomized rat. A retinol dehydrogenase that we have previously described, eRolDH, and the retinal dehydrogenase, RalDH II, were found to have markedly increased uterine mRNA levels within 4 h of E₂ administration, independent of the prior administration of puromycin. eRolDH and RalDH II and their mRNAs were also increased in uteri of rats during estrus. This indicated that RA biosynthesis in rat uterus is directly controlled by E₂ and provides a direct link between the action of a steroid hormone and retinoid action. We also examined the cell-specific localization of RalDH II by immunohistochemistry. The enzyme was observed in the stromal compartment, particularly in cells close to the uterine lumenal epithelium. eRolDH was observed only in the lining epithelial cells. Taken together with the previous observations of cellular retinol-binding protein and cellular retinoic acid-binding protein, type two also being expressed in the lumenal epithelium, we propose that RA production is compartmentalized, with retinol oxidation occurring in the lumenal epithelium and subsequent oxidation of retinal to RA occurring in the underlying stromal cells.

This article has been cited by other articles:

				K. Mitko, S. E Ulbrich, H. Wenigerkind, F. Sinowatz, H. Blum, E. Wolf, and S. Bauersachs Dynamic changes in messenger RNA profiles of bovine endometrium during the oestrous cycle Reproduction, February 1, 2008; 135(2): 225 - 240. [Abstract] [Full Text] [PDF]

				B. K. Tan, J. Chen, H. Lehnert, R. Kennedy, and H. S. Randeva Raised Serum, Adipocyte, and Adipose Tissue Retinol-Binding Protein 4 in Overweight Women with Polycystic Ovary Syndrome: Effects of Gonadal and Adrenal Steroids J. Clin. Endocrinol. Metab., July 1, 2007; 92(7): 2764 - 2772. [Abstract] [Full Text] [PDF]

				S. E. Trasino, E. H. Harrison, and T. T. Y. Wang Androgen Regulation of Aldehyde Dehydrogenase 1A3 (ALDH1A3) in the Androgen-Responsive Human Prostate Cancer Cell Line LNCaP Experimental Biology and Medicine, June 1, 2007; 232(6): 762 - 771. [Abstract] [Full Text] [PDF]

				L. D. Nadauld, D. N. Shelton, S. Chidester, H. J. Yost, and D. A. Jones The Zebrafish Retinol Dehydrogenase, rdh1l, Is Essential for Intestinal Development and Is Regulated by the Tumor Suppressor Adenomatous Polyposis Coli J. Biol. Chem., August 26, 2005; 280(34): 30490 - 30495. [Abstract] [Full Text] [PDF]