메뉴 건너뛰기




Volumn 60, Issue 4, 1999, Pages 855-860

Opposing changes in 3α-hydroxysteroid dehydrogenase oxidative and reductive activities in rat Leydig cells during pubertal development

Author keywords

[No Author keywords available]

Indexed keywords

3ALPHA HYDROXYSTEROID DEHYDROGENASE; ANDROGEN; ANDROSTANOLONE; 3 ALPHA HYDROXYSTEROID DEHYDROGENASE (B SPECIFIC); 3(OR 17)BETA HYDROXYSTEROID DEHYDROGENASE; ANDROSTANEDIOL; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

EID: 0032588278     PISSN: 00063363     EISSN: None     Source Type: Journal    
DOI: 10.1095/biolreprod60.4.855     Document Type: Article
Times cited : (39)

References (41)
  • 1
    • 0026786336 scopus 로고
    • Developmental changes in the levels of luteinizing hormone receptor and androgen receptor in rat leydig cells
    • Shan LX, Hardy MP. Developmental changes in the levels of luteinizing hormone receptor and androgen receptor in rat Leydig cells. Endocrinology 1992; 131:1107-1114.
    • (1992) Endocrinology , vol.131 , pp. 1107-1114
    • Shan, L.X.1    Hardy, M.P.2
  • 2
    • 0028103854 scopus 로고
    • Immunohistochemical localization of androgen receptors in the rat testis: Evidence for stage-dependent expression and regulation by androgens
    • Bremner WJ, Millar MR, Sharpe RM, Saunders PTK. Immunohistochemical localization of androgen receptors in the rat testis: evidence for stage-dependent expression and regulation by androgens. Endocrinology 1994; 135:1227-1234.
    • (1994) Endocrinology , vol.135 , pp. 1227-1234
    • Bremner, W.J.1    Millar, M.R.2    Sharpe, R.M.3    Saunders, P.T.K.4
  • 3
    • 0029150932 scopus 로고
    • Quantitative analysis of androgen receptor messenger ribonucleic acid in developing leydig cells and sertoli cells by in situ hybridization
    • Shan LX, Zhu LJ, Bardin CW, Hardy MP. Quantitative analysis of androgen receptor messenger ribonucleic acid in developing Leydig cells and Sertoli cells by in situ hybridization. Endocrinology 1995; 136:3856-3862.
    • (1995) Endocrinology , vol.136 , pp. 3856-3862
    • Shan, L.X.1    Zhu, L.J.2    Bardin, C.W.3    Hardy, M.P.4
  • 4
    • 0025333015 scopus 로고
    • Differentiation of leydig cell precursors in vitro: A role for androgen
    • Hardy MP, Kelce WR, Klinefelter GR, Ewing LL. Differentiation of Leydig cell precursors in vitro: a role for androgen. Endocrinology 1990; 127:488-490.
    • (1990) Endocrinology , vol.127 , pp. 488-490
    • Hardy, M.P.1    Kelce, W.R.2    Klinefelter, G.R.3    Ewing, L.L.4
  • 5
    • 0023655719 scopus 로고
    • Testosterone inhibits camp-induced de novo synthesis of leydig cell cytochrome P-450 by an androgen receptor-mediated mechanism
    • Hales DB, Sha L, Payne AH. Testosterone inhibits cAMP-induced de novo synthesis of Leydig cell cytochrome P-450 by an androgen receptor-mediated mechanism. J Biol Chem 1987; 262:11200-11206.
    • (1987) J Biol Chem , vol.262 , pp. 11200-11206
    • Hales, D.B.1    Sha, L.2    Payne, A.H.3
  • 6
    • 0015809090 scopus 로고
    • Steroid structure and androgenic activity: Specificities involved in the receptor binding and nuclear retention of various androgens
    • Liao S, Liang T, Fang S, Castaneda E, Shao TC. Steroid structure and androgenic activity: specificities involved in the receptor binding and nuclear retention of various androgens. J Biol Chem 1973; 248:6154-6162.
    • (1973) J Biol Chem , vol.248 , pp. 6154-6162
    • Liao, S.1    Liang, T.2    Fang, S.3    Castaneda, E.4    Shao, T.C.5
  • 7
    • 0014847075 scopus 로고
    • Dihydrotestosterone in prostatic hypertrophy, I: The formation and content of dihydrotestosterone in the hypertrophic prostate of man
    • Siiteri PK, Wilson JD. Dihydrotestosterone in prostatic hypertrophy, I: the formation and content of dihydrotestosterone in the hypertrophic prostate of man. J Clin Invest 1970; 49:1737-1745.
    • (1970) J Clin Invest , vol.49 , pp. 1737-1745
    • Siiteri, P.K.1    Wilson, J.D.2
  • 8
    • 0027365643 scopus 로고
    • Differential regulation of steroidogenic enzymes during differentiation optimizes testosterone production by adult rat leydig cells
    • Shan L-X, Phillips DM, Bardin CW, Hardy MP. Differential regulation of steroidogenic enzymes during differentiation optimizes testosterone production by adult rat Leydig cells. Endocrinology 1993; 133:2277-2283.
    • (1993) Endocrinology , vol.133 , pp. 2277-2283
    • Shan, L.-X.1    Phillips, D.M.2    Bardin, C.W.3    Hardy, M.P.4
  • 9
    • 0025773967 scopus 로고
    • Molecular structure of rat hepatic 3α-hydroxysteroid dehydrogenase: A member of the oxidoreductase gene family
    • Stolz A, Rahimi-Kiani M, Ameis D, Chan E, Ronk M, Shively JE. Molecular structure of rat hepatic 3α-hydroxysteroid dehydrogenase: a member of the oxidoreductase gene family. J Biol Chem 1991; 266: 15253-15257.
    • (1991) J Biol Chem , vol.266 , pp. 15253-15257
    • Stolz, A.1    Rahimi-Kiani, M.2    Ameis, D.3    Chan, E.4    Ronk, M.5    Shively, J.E.6
  • 10
    • 0025835877 scopus 로고
    • Cloning and sequencing of the cDNA for rat liver 3α-hydroxysteroid, dihydrodiol dehydrogenase
    • Pawlowski JE, Huizinga M, Penning TM. Cloning and sequencing of the cDNA for rat liver 3α-hydroxysteroid, dihydrodiol dehydrogenase. J Biol Chem 1991; 266:8820-8825.
    • (1991) J Biol Chem , vol.266 , pp. 8820-8825
    • Pawlowski, J.E.1    Huizinga, M.2    Penning, T.M.3
  • 11
    • 0025998395 scopus 로고
    • Molecular cloning and expression of rat liver 3α-hydroxysteroid dehydrogenase
    • Cheng KC, White PC, Qin KN. Molecular cloning and expression of rat liver 3α-hydroxysteroid dehydrogenase. Mol Endocrinol 1991; 5: 823-828.
    • (1991) Mol Endocrinol , vol.5 , pp. 823-828
    • Cheng, K.C.1    White, P.C.2    Qin, K.N.3
  • 12
    • 0028007003 scopus 로고
    • Purification of NADPH-dependent dehydroascorbate reductase from rat liver and its identification with 3α-hydroxysteroid dehydrogenase
    • Del Bello B, Maellaro E, Sugherini L, Santucci A, Comporti M, Casini AF. Purification of NADPH-dependent dehydroascorbate reductase from rat liver and its identification with 3α-hydroxysteroid dehydrogenase. Biochem J 1994; 304:385-390.
    • (1994) Biochem J , vol.304 , pp. 385-390
    • Del Bello, B.1    Maellaro, E.2    Sugherini, L.3    Santucci, A.4    Comporti, M.5    Casini, A.F.6
  • 13
    • 0026608243 scopus 로고
    • Characterization of bovine liver cytosolic 3α-hydroxysteroid dehydrogenase and its aldo-keto reductase activity
    • Nanjo H, Terada T, Umemura T, Nishinaka T, Mizoguchi T, Nishihara T. Characterization of bovine liver cytosolic 3α-hydroxysteroid dehydrogenase and its aldo-keto reductase activity. Int J Biochem 1992; 24:815-820.
    • (1992) Int J Biochem , vol.24 , pp. 815-820
    • Nanjo, H.1    Terada, T.2    Umemura, T.3    Nishinaka, T.4    Mizoguchi, T.5    Nishihara, T.6
  • 14
    • 0023944392 scopus 로고
    • Purification and characterization of NADP+-dependent 3α-hydroxysteroid dehydrogenase from mouse liver cytosol
    • Hara A, Inoue Y, Nakagawa M, Naganeo F, Sawada H. Purification and characterization of NADP+-dependent 3α-hydroxysteroid dehydrogenase from mouse liver cytosol. J Biochem (Tokyo) 1988; 103: 1027-1034.
    • (1988) J Biochem (Tokyo) , vol.103 , pp. 1027-1034
    • Hara, A.1    Inoue, Y.2    Nakagawa, M.3    Naganeo, F.4    Sawada, H.5
  • 16
    • 0031046241 scopus 로고    scopus 로고
    • 11β-hydroxysteroid dehydrogenase and the syndrome of apparent mineralocorticoid excess
    • White PC, Mune T, Agarwal AK. 11β-Hydroxysteroid dehydrogenase and the syndrome of apparent mineralocorticoid excess. Endocr Rev 1997; 18:135-156.
    • (1997) Endocr Rev , vol.18 , pp. 135-156
    • White, P.C.1    Mune, T.2    Agarwal, A.K.3
  • 17
    • 0029122448 scopus 로고
    • Cloning, expression, and tissue distribution of the rat nicotinamide adenine dinucleotide-dependent 11β-hydroxysteroid dehydrogenase
    • Zhou MY, Gomez-Sanchez EP, Cox DL, Cosby D, Gomez-Sanchez CE. Cloning, expression, and tissue distribution of the rat nicotinamide adenine dinucleotide-dependent 11β-hydroxysteroid dehydrogenase. Endocrinology 1995; 136:3729-373.
    • (1995) Endocrinology , vol.136 , pp. 3729-4373
    • Zhou, M.Y.1    Gomez-Sanchez, E.P.2    Cox, D.L.3    Cosby, D.4    Gomez-Sanchez, C.E.5
  • 18
    • 0027459238 scopus 로고
    • Rat liver 11β-hydroxysteroid dehydrogenase complementary deoxyribonucleic acid encodes oxoreductase activity in a mineralocorticoid-responsive toad bladder cell line
    • Duperrex H, Kenouch S, Gaeggeler HP, Seckl JR, Edwards CR, Farman N, Rossier BC. Rat liver 11β-hydroxysteroid dehydrogenase complementary deoxyribonucleic acid encodes oxoreductase activity in a mineralocorticoid-responsive toad bladder cell line. Endocrinology 1993; 132:612-619.
    • (1993) Endocrinology , vol.132 , pp. 612-619
    • Duperrex, H.1    Kenouch, S.2    Gaeggeler, H.P.3    Seckl, J.R.4    Edwards, C.R.5    Farman, N.6    Rossier, B.C.7
  • 19
    • 0029593494 scopus 로고
    • Characteristics of human types 1, 2 and 3 17β-hydroxysteroid dehydrogenase activities: Oxidation/reduction and inhibition
    • Luu-The V, Zhang Y, Poirier D, Labrie F. Characteristics of human types 1, 2 and 3 17β-hydroxysteroid dehydrogenase activities: oxidation/reduction and inhibition. J Steroid Biochem Mol Biol 1995; 55:581-587.
    • (1995) J Steroid Biochem Mol Biol , vol.55 , pp. 581-587
    • Luu-The, V.1    Zhang, Y.2    Poirier, D.3    Labrie, F.4
  • 20
    • 0030992888 scopus 로고    scopus 로고
    • Regional distribution of cytosolic and particulate 5α-dihydroprogesterone 3α-hydroxysteroid oxidoreductases in female rat brain
    • Li XD, Bertics PJ, Karavolas HJ. Regional distribution of cytosolic and particulate 5α-dihydroprogesterone 3α-hydroxysteroid oxidoreductases in female rat brain. J Steroid Biochem Mol Biol 1997; 60: 311-318.
    • (1997) J Steroid Biochem Mol Biol , vol.60 , pp. 311-318
    • Li, X.D.1    Bertics, P.J.2    Karavolas, H.J.3
  • 21
    • 0020035077 scopus 로고
    • Subcellular distribution of 3α-hydroxysteroid dehydrogenase and antiestrogen action on androgen-metabolizing enzymes in rat pituitary gland
    • Ghraf R, Schneider K, Kirchhoff J, Hiemke C. Subcellular distribution of 3α-hydroxysteroid dehydrogenase and antiestrogen action on androgen-metabolizing enzymes in rat pituitary gland. J Neurochem 1982; 38:876-883.
    • (1982) J Neurochem , vol.38 , pp. 876-883
    • Ghraf, R.1    Schneider, K.2    Kirchhoff, J.3    Hiemke, C.4
  • 22
    • 0000281516 scopus 로고
    • Isolation and culture of leydig cells from adult rats
    • Klinefelter GR, Kelce WR, Hardy MP. Isolation and culture of Leydig cells from adult rats. Methods Toxicol 1993; 3A:166-181.
    • (1993) Methods Toxicol , vol.3 A , pp. 166-181
    • Klinefelter, G.R.1    Kelce, W.R.2    Hardy, M.P.3
  • 23
    • 0018870772 scopus 로고
    • Luteinizing hormone receptors and testosterone synthesis in two distinct population of leydig cells
    • Payne AH, Downing JR, Wong KL. Luteinizing hormone receptors and testosterone synthesis in two distinct population of Leydig cells. Endocrinology 1980; 106:1424-1429.
    • (1980) Endocrinology , vol.106 , pp. 1424-1429
    • Payne, A.H.1    Downing, J.R.2    Wong, K.L.3
  • 25
    • 0023759441 scopus 로고
    • Electrophoretic and immunochemical characterization of 3α-hydroxysteroid/dihydrodiol dehydrogenases of rat tissues
    • Smithgall TE, Penning TM. Electrophoretic and immunochemical characterization of 3α-hydroxysteroid/dihydrodiol dehydrogenases of rat tissues. Biochem J 1988; 254:715-721.
    • (1988) Biochem J , vol.254 , pp. 715-721
    • Smithgall, T.E.1    Penning, T.M.2
  • 26
    • 0344759251 scopus 로고    scopus 로고
    • New York: WH Freeman and Co.
    • Sokal RR, Rohlf FJ. Biometry. New York: WH Freeman and Co.; 1981: 372-399.
    • Biometry , vol.1981 , pp. 372-399
    • Sokal, R.R.1    Rohlf, F.J.2
  • 27
    • 0031790274 scopus 로고    scopus 로고
    • Variation in the end products of androgen biosynthesis and metabolism during postnatal differentiation of rat leydig cells
    • Ge R-S, Hardy MP. Variation in the end products of androgen biosynthesis and metabolism during postnatal differentiation of rat Leydig cells. Endocrinology 1998; 139:3787-3795.
    • (1998) Endocrinology , vol.139 , pp. 3787-3795
    • Ge, R.-S.1    Hardy, M.P.2
  • 28
    • 0015278655 scopus 로고
    • Control of the redox state of the nicotinamide-adenine dinucleotide couple in the cytoplasm
    • Stubbs M, Veech RL, Krebs HA. Control of the redox state of the nicotinamide-adenine dinucleotide couple in the cytoplasm. Biochem J 1972; 126:59-65.
    • (1972) Biochem J , vol.126 , pp. 59-65
    • Stubbs, M.1    Veech, R.L.2    Krebs, H.A.3
  • 29
    • 0025822817 scopus 로고
    • Postnatal changes in pyridine nucleotides in rat hepatocytes: Composition and O2 dependence
    • Aw TY. Postnatal changes in pyridine nucleotides in rat hepatocytes: composition and O2 dependence. Pediatr Res 1991; 30:112-117.
    • (1991) Pediatr Res , vol.30 , pp. 112-117
    • Aw, T.Y.1
  • 30
    • 0028269192 scopus 로고
    • Molecular cloning of two human liver 3α-hydroxysteroid/dihydrodiol dehydrogenase isoenzymes that are identical with chlordecone reductase and bile-acid binder
    • Deyashiki Y, Ogasawara A, Nakayama T, Nakanishi M, Miyabe Y, Sato K, Hara A. Molecular cloning of two human liver 3α-hydroxysteroid/dihydrodiol dehydrogenase isoenzymes that are identical with chlordecone reductase and bile-acid binder. Biochem J 1994; 299: 545-552.
    • (1994) Biochem J , vol.299 , pp. 545-552
    • Deyashiki, Y.1    Ogasawara, A.2    Nakayama, T.3    Nakanishi, M.4    Miyabe, Y.5    Sato, K.6    Hara, A.7
  • 31
    • 0030784509 scopus 로고    scopus 로고
    • Expression and characterization of recombinant type 2 3α-hydroxy-steroid dehydrogenase (HSD) from human prostate: Demonstration of bifunctional 3α/17β-HSD activity and cellular distribution
    • Lin HK, Jez JM, Schlegel BP, Peehl DM, Pachter JA, Penning TM. Expression and characterization of recombinant type 2 3α-hydroxy-steroid dehydrogenase (HSD) from human prostate: demonstration of bifunctional 3α/17β-HSD activity and cellular distribution. Mol Endocrinol 1997; 11:1971-1984.
    • (1997) Mol Endocrinol , vol.11 , pp. 1971-1984
    • Lin, H.K.1    Jez, J.M.2    Schlegel, B.P.3    Peehl, D.M.4    Pachter, J.A.5    Penning, T.M.6
  • 32
    • 0030581692 scopus 로고    scopus 로고
    • Molecular cloning of human type 3 3α-hydroxysteroid dehydrogenase that differs from 20α-hydroxysteroid dehydrogenase by seven amino acids
    • Dufort I, Soucy P, Labrie F, Luu-The V. Molecular cloning of human type 3 3α-hydroxysteroid dehydrogenase that differs from 20α-hydroxysteroid dehydrogenase by seven amino acids. Biochem Biophys Res Commun 1996; 228:474-479.
    • (1996) Biochem Biophys Res Commun , vol.228 , pp. 474-479
    • Dufort, I.1    Soucy, P.2    Labrie, F.3    Luu-The, V.4
  • 33
    • 0032504149 scopus 로고    scopus 로고
    • cDNA cloning, tissue distribution, and substrate characteristics of a cis-retinol/3α-hydroxysteroid dehydroxysterol short-chain dehydrogenase isozyme
    • Su J, Chai XY, Kahn B, Napoli JL. cDNA cloning, tissue distribution, and substrate characteristics of a cis-retinol/3α-hydroxysteroid dehydroxysterol short-chain dehydrogenase isozyme. J Biol Chem 1998; 273:17910-17916.
    • (1998) J Biol Chem , vol.273 , pp. 17910-17916
    • Su, J.1    Chai, X.Y.2    Kahn, B.3    Napoli, J.L.4
  • 34
    • 0031435106 scopus 로고    scopus 로고
    • cDNA cloning and characterization of a cis-retinol/3α-hydroxysterol short-chain dehydrogenase
    • Chai XY, Zhai Y, Napoli JL. cDNA cloning and characterization of a cis-retinol/3α-hydroxysterol short-chain dehydrogenase. J Biol Chem 1997; 272:33125-33131.
    • (1997) J Biol Chem , vol.272 , pp. 33125-33131
    • Chai, X.Y.1    Zhai, Y.2    Napoli, J.L.3
  • 35
    • 0030991226 scopus 로고    scopus 로고
    • Expression cloning and characterization of oxidative 17β-and 3α-hydroxysteroid dehydrogenases from rat and human prostate
    • Biswas MG, Russell DW. Expression cloning and characterization of oxidative 17β-and 3α-hydroxysteroid dehydrogenases from rat and human prostate. J Biol Chem 1997; 272:15959-15966.
    • (1997) J Biol Chem , vol.272 , pp. 15959-15966
    • Biswas, M.G.1    Russell, D.W.2
  • 36
    • 0032584601 scopus 로고    scopus 로고
    • cDNA cloning and characterization of a new human microsomal NAD+-dependent dehydrogenase that oxidizes all-trans-retinol and 3α-hydroxysteroids
    • Gough WH, VanOoteghem S, Sint T, Kedishvili NY. cDNA cloning and characterization of a new human microsomal NAD+-dependent dehydrogenase that oxidizes all-trans-retinol and 3α-hydroxysteroids. J Biol Chem 1998; 273:19778-19785.
    • (1998) J Biol Chem , vol.273 , pp. 19778-19785
    • Gough, W.H.1    Vanooteghem, S.2    Sint, T.3    Kedishvili, N.Y.4
  • 37
    • 0019756014 scopus 로고
    • Steroid secretion by sexually immature rat and rabbit testis perfused in vitro
    • Chubb C, Ewing LL. Steroid secretion by sexually immature rat and rabbit testis perfused in vitro. Endocrinology 1981; 109:1999-2003.
    • (1981) Endocrinology , vol.109 , pp. 1999-2003
    • Chubb, C.1    Ewing, L.L.2
  • 38
    • 0019491126 scopus 로고
    • Testosterone, dihydrotestosterone and androstanediols in plasma, testes and prostates of rats during development
    • Corpechot C, Baulieu EE, Robel P. Testosterone, dihydrotestosterone and androstanediols in plasma, testes and prostates of rats during development. Acta Endocrinol (Copehn) 1981; 96:127-135.
    • (1981) Acta Endocrinol (Copehn) , vol.96 , pp. 127-135
    • Corpechot, C.1    Baulieu, E.E.2    Robel, P.3
  • 39
    • 0013953803 scopus 로고
    • Bioconversion of steroids in immature rat testes in vitro
    • Inano H, Tamaoki B-I. Bioconversion of steroids in immature rat testes in vitro. Endocrinology 1966; 79:579-590.
    • (1966) Endocrinology , vol.79 , pp. 579-590
    • Inano, H.1    Tamaoki, B.-I.2
  • 40
    • 0028804062 scopus 로고
    • Steady state steroid 5α-reductase messenger ribonucleic acid levels and immunocytochemical localization of the type I protein in the rat testis during postnatal development
    • Viger RS, Robaire B. Steady state steroid 5α-reductase messenger ribonucleic acid levels and immunocytochemical localization of the type I protein in the rat testis during postnatal development. Endocrinology 1995; 136:5409-5415.
    • (1995) Endocrinology , vol.136 , pp. 5409-5415
    • Viger, R.S.1    Robaire, B.2
  • 41
    • 0030013464 scopus 로고    scopus 로고
    • Inhibition of 5α-reductase activity impairs the testosterone-dependent restoration of spermiogenesis in adult rats
    • O'Donnell L, Stanton PG, Wreford NG, Robertson DM, McLachlan RI. Inhibition of 5α-reductase activity impairs the testosterone-dependent restoration of spermiogenesis in adult rats. Endocrinology 1996; 137:2703-2710.
    • (1996) Endocrinology , vol.137 , pp. 2703-2710
    • O'Donnell, L.1    Stanton, P.G.2    Wreford, N.G.3    Robertson, D.M.4    McLachlan, R.I.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.