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 Google Scholar Google Scholar Articles by Guo, X. Articles by Gudas, L. J. Search for Related Content PubMed PubMed Citation Articles by Guo, X. Articles by Gudas, L. J.

Follicle-Stimulating Hormone and Leukemia Inhibitory Factor Regulate Sertoli Cell Retinol Metabolism¹

Department of Pharmacology, Weill Medical College of Cornell University (X.G., L.J.G.); The Center for Biomedical Research, The Population Council (P.L.M.); and Rockefeller University (P.L.M.), New York, New York 10021

Address all correspondence and requests for reprints to: Dr. Lorraine J. Gudas, Department of Pharmacology, Weill Medical College of Cornell University, 1300 York Avenue, New York, New York 10021. E-mail: ljgudas{at}mail.med.cornell.edu

Sertoli cells, the somatic epithelial cells of the seminiferous tubules, provide both structural and biochemical support for developing male germ cells. The Sertoli cells are targets of retinoid action in the testis. We have found that FSH, (Bu)₂cAMP, and leukemia inhibitory factor elicit substantial changes in the metabolism of [³H]retinol (vitamin A) in primary cultures of purified rat Sertoli cells. Addition of (Bu)₂cAMP for 2 h or FSH for 6 h results in a 3-fold increase in the metabolism of [³H]retinol to [³H]retinoic acid ([³H]RA); the esterification of [³H]retinol to [³H]retinyl esters, especially [³H]retinyl palmitate, is also increased by approximately 5-fold. The addition of 1 µM all-trans-RA also elicits changes in [³H]retinol metabolism, but in this case the metabolism of [³H]retinol to [³H]RA is inhibited, whereas the metabolism of [³H]retinol to [³H]retinyl esters is increased by over 50-fold. Leukemia inhibitory factor increases the esterification of [³H]retinol by 2- to 3-fold. FSH leads to a reduction in the level of cellular retinol binding protein I transcripts, whereas RA increases the cellular retinol binding protein I messenger RNA level by about 2-fold at approximately 24 h. Levels of AHD-2 (aldehyde dehydrogenase-2) and RALDH-2 (retinaldehyde dehydrogenase-2) messenger RNAs, which encode enzymes that convert [³H]retinaldehyde to [³H]RA, are increased by about 2-fold by FSH, whereas no change in CYP26 (RA hydroxylase) expression is seen. Our results suggest that one function of FSH (and/or (Bu)₂cAMP) in Sertoli cells is to increase the metabolism of retinol to the biologically active metabolite RA and to retinyl esters.