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Endocrinology Vol. 139, No. 1 272-279
Copyright © 1998 by The Endocrine Society

ARTICLES

Luteinizing Hormone-Dependent Gene Regulation in Leydig Cells May Be Mediated by CCAAT/Enhancer-Binding Protein-ß1

Demet Nalbant, Simon C. Williams, Douglas M. Stocco and Shafiq A. Khan

Department of Cell Biology and Biochemistry (D.N., S.C.W., D.M.S., S.A.K.) and Southwest Cancer Center (S.C.W., S.A.K.), University Medical Center, Texas Tech University Health Sciences Center, Lubbock, Texas 79430

Address all correspondence and requests for reprints to: Shafiq A. Khan, Ph.D., Department of Cell Biology and Biochemistry, Texas Tech University Health Sciences Center, 3601 4th Street, Lubbock, Texas 79430. E-mail: cbbsak{at}wpoffice.net.ttuhsc.edu

Leydig cells are located in the interstitium of the testis and function as the primary site for testosterone biosynthesis. Leydig cell development and steroidogenic function are dependent upon pituitary-derived LH. Circulating LH levels in prepubertal mammals are low but rise sharply during puberty, inducing terminal differentiation of immature Leydig cells into adult Leydig cells. The molecular mechanisms involved in LH action on differentiation specific gene expression and initiation of steroidogenic function in immature Leydig cells are poorly understood. Members of the CCAAT/enhancer-binding protein (C/EBP) family of basic region/leucine zipper transcription factors have previously been implicated as regulators of terminal differentiation in several cell types. In the present study we have investigated the possible involvement of C/EBP proteins in regulating LH-dependent gene expression in Leydig cells. We have detected the expression of one family member, C/EBPß, in Leydig cells. C/EBPß messenger RNA and protein levels were significantly higher in mature adult Leydig cells than in immature cells, displaying an expression pattern similar to those of other developmentally regulated genes in Leydig cells such as steroidogenesis acute regulatory (StAR) protein and 3ß-hydroxysteroid dehydrogenase. C/EBPß messenger RNA and protein levels also increased when immature Leydig cells were treated with either hCG, a functional analog of LH (hCG/LH), or (Bu)2cAMP. To confirm that hCG/LH and (Bu)2cAMP were acting specifically on Leydig cells, we studied their effects on C/EBPß expression in an established Leydig cell line (MA-10). hCG and (Bu)2cAMP treatment also induced the expression of C/EBPß and StAR in MA-10 cells, coincident with stimulation of steroid production in these cells. (Bu)2cAMP treatment did not alter the subcellular localization of C/EBPß protein in MA-10 cells, suggesting that the increase is due to stimulation of C/EBPß expression. We conclude that expression of C/EBPß is regulated by hCG/LH in Leydig cells and that C/EBPß may play a significant role in LH-regulated Leydig cell differentiation and function.




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