title: Differentiation-dependent expression of 17beta-hydroxysteroid dehydrogenase, type 10, in the rodent testis: effect of aging in Leydig cells.
abstract: Expression of the new 17beta-hydroxysteroid dehydrogenase (HSD), type 10 (17beta-HSD-10), formerly known as endoplasmic reticulum-associated amyloid-binding protein, has been investigated in the testes of various mammals under normal and perturbed conditions. Results show that 17beta-HSD-10 is a major product of both fetal and adult-type Leydig cells. In the former, protein persists until late in postnatal development; and in the short-day hamster model, it does not disappear when Leydig cells involute. During puberty in the rat, immunohistochemical staining for 17beta-HSD-10 in adult-type Leydig cells first becomes evident on d 20, increasing to maximal staining intensity by d 35. In the rat, but not in the mouse or any other species examined, there is also staining in late spermatids. Examination of testes from rats subjected to perinatal treatment with either a GnRH antagonist or low and high doses of diethylstilbestrol revealed that expression of 17beta-HSD-10 follows closely Leydig cell differentiation status, correlating with 3beta-HSD expression in a previous study. In aging (23 months) rat testes, Leydig cell (but not germ cell) immunostaining for 17beta-HSD-10 is markedly reduced. 17beta-HSD-10 seems to preferentially convert 3alpha-androstanediol into dihydrotestosterone, and estradiol to estrone. Thus, perinatal expression of this enzyme in fetal Leydig cells may contribute to protecting these cells from estrogens and encourage androgen formation.
authors.affiliation: Institute for Hormone and Fertility Research, University of Hamburg, Falkenreid 88, 20251 Hamburg, Germany. ivell@ihf.de
authors.forename: Richard
authors.initials: R
authors.lastname: Ivell
authors.forename: Marga
authors.initials: M
authors.lastname: Balvers
authors.forename: Ravinder J K
authors.initials: RJ
authors.lastname: Anand
authors.forename: Hans-Joachim
authors.initials: HJ
authors.lastname: Paust
authors.forename: Chris
authors.initials: C
authors.lastname: McKinnell
authors.forename: Richard
authors.initials: R
authors.lastname: Sharpe
mesh_terms: D015067:17-Hydroxysteroid Dehydrogenases / Q000235:genetics*; D015094:3-Hydroxyacyl CoA Dehydrogenases; D000818:Animals; D002144:Callithrix; D002454:Cell Differentiation / Q000502:physiology; D016922:Cellular Senescence / Q000502:physiology*; D006224:Cricetinae; D018507:Gene Expression Regulation, Developmental; D015971:Gene Expression Regulation, Enzymologic; D006801:Humans; D007985:Leydig Cells / Q000166:cytology* / Q000201:enzymology*; D008297:Male; D051379:Mice; D008817:Mice, Mutant Strains; D012333:RNA, Messenger / Q000032:analysis; D051381:Rats; D017208:Rats, Wistar; D013737:Testis / Q000166:cytology / Q000201:enzymology / Q000254:growth & development
chemical_list: D012333:RNA, Messenger; D015067:17-Hydroxysteroid Dehydrogenases; D015094:3-Hydroxyacyl CoA Dehydrogenases; C458480:Hsd17b10 protein, mouse