| Title | Intracrinology and hormone-dependent cancers | |
| Authors | Van Luu-The, Jacques Simard, Claude Labrie, Alain Bélanger and Fernand Labrie
MRC Group in Molecular Endocrinology, CHUL Research Center and Laval University, Quebec, Canada G1V 4G2 |
|
| Citation | Luu-The, V., Simard, J., Labrie, C., Bélanger, A., Labrie, F.: Intracrinology and hormone-dependent cancers, Epitheorese Klin. Farmakol. Farmakokinet. 11(1): 18-26 (1997) | |
| Publication Date | Accepted for publication: 15 April 1997 | |
| Full Text Language | English | |
| Order – Buy | Ηλεκτρονική Μορφή: pdf (10 €) – Digital Type: pdf (10 €)
pharmakonpress[at]pharmakonpress[.]gr |
|
| Keywords | Cancer, hormone-dependent, intracrinology. | |
| Other Terms | review article | |
| Summary | Sex steroid hormones are produced by two main sources, the gonads and the peripheral tissues. Although the ovaries and testis are the exclusive sources of androgens and estrogens in small mammals, in higher primates and humans they are also produced in large amounts locally in the peripheral tissues via the adrenal precursors DHEA, its sulfate (DHEAS) and 4-androstenedione (4-dione), and could thus exert their action in the same cells that they are produced. A decade ago, our group has used the term intracrinology to describe this new mode of steroid hormone formation and action, which is specific to nuclear receptor-mediated action and represents an economical system that requires minimal amounts of hormone to exert maximal function. Such system also provides autonomous control to target tissues. The production of sex steroids in peripheral tissues via adrenal precursors is particularly important in postmenauposal women or elderly men in whom the ability of the ovaries and testis to produce estrogen and androgen, respectively, are dramatically decreased. Intracrinology is, thus, crucial for the breast and prostate cancers, the sex steroid-dependent diseases that appear more frequently in the advancing age. To better understand the role of intracrinology, in the last few years, our laboratory has focused in elucidating the pathway leading to the formation and degradation of sex steroid hormones in peripheral target tissues. We and others have demonstrated the existence of multiple genes encoding various steroidogenic enzymes, namely 3β-hydroxysteroid dehydrogenases (3β-HSD), 17β-hydroxysteroid dehydrogenases (17β-HSD), and 5α-reductases. These genes are expressed in a tissue-specific manner, and they are also differentially regulated. It is noteworthy that the mutation of only one form is responsible for the congenital disease. Since the hormones provided by the other isoenzymes are not sufficient to cover the need of a specific organ, the general concept that most of the sex hormones are provided by gonads and distributed to different tissues by systemic circulation need thus to be revised. Recently, we find that cytokines regulate markedly the 3β– and 17β-HSD gene expression. We have also shown that over production of steroidogenic enzymes modulate potently the receptor activity. The results thus strengthen the crucial role of intracrine hormones, especially in androgen- and estrogen-dependent diseases, such as the prostate and breast cancers, respectively. | |
| References | 1. Labrie C, Bélanger A, Labrie F: Androgenic activity of dehydroepiandrosterone and androstenedione in the rat ventral prostate. Endocrinology 123: 1412-1417 (1988)
2. Labrie F: Intracrinology. Mol. Cell. Endocrinol. 78: C113-C118 (1991) 3. Labrie F.: Intracrinology: its impact on prostate cancer. Curr. Opin. Urol. 3: 381-387 (1993) 4. Luu-The V, Lachance Y, Labrie C, Leblanc G, Thomas JL, Strickler RC, Labrie F: Full length cPNA structure and deduced amino acid sequence of human 3β-hydroxy-5-ene steroid dehydrogenase. Mol. Endocrinol. 3: 1310-1312 (1989) 5. Lachance Y, Luu-The V, Labrie C, Simard J, Dumont M, de Launoit Y, Guérin S, LeBlanc G, Labrie F Characterization of human 3β-hydroxysteroid dehydrogenase/Δ5-Δ⁴ isomerase gene and its expression in mammalian cells. J. Biol. Chem. 265: 20469-20475 (1990) 6. Lachance Y, Luu-The V, Verreault H, Dumont M, Rhéaume E, Leblanc G, Labrie F: Structure of the human type II 3β-hydroxysteroid dehydrogenase /A5-A4 isomerase (3f3-HSD) gene: adrenal and gonadal specificity. DNA Cell. Biol. 10: 701-711 (1991) 7. Lorence MC, Murry, BA, Trant JM. Mason JI: Human 3β-hydroxysteroid dehydrogenase/A5-A4 isomerase from placenta: expression in nonsteroidogenic cells of a protein that catalyzes the dehydrogenation/ isomeration of C21 and C19 steroids. Endocrinology 126: 2493-2498 (1990) 8. Lorence MC, Corbin C, Kaninura N, Mahendro MS, Mason JI: (1990) Structural analysis of the gene encoding human 3β-hydroxysteroid dehydrogenase/A5-A⁴ isomerase. Mol. Endocrinol. 4: 1850-1855 (1990) 9. Rhéaume E, Lachance Y, Zhao HF, Breton N, Dumont M, de Launoit Y, Trudel C, Luu-The V, Simard J, Labrie F: Structure and expression of a new cDNA encoding the almost exclusive 3β-hydroxysteroid dehydrogenase/A5-A⁴ isomerase in human adrenals and gonads. Mol. Endocrinol. 5: 1147-1157 (1991) 10. Luu-The V, Labrie C, Zhao HF, Couët J, Lachance Y, Simard J, LeBlanc G, Côté J, Bérubé G, Gagné R, Labrie F: Characterization of cDNAs for human estradiol 17p-dehydro- genase and assignment of the gene to chromosome 17: evidence of two mRNA species with distinct 5′-termini in human placenta. Mol. Endocrinol. 3: 1301-1309 (1989) 11. Peltoketo H, Isomaa V, Maentausta O, Vihko R: Complete amino acid sequence of human placental 7β-hydroxysteroid dehydrogenase deduced from cDNA. FEBS Lett. 239: 73-77 (1988) 12. Luu-The V, Labrie C, Simard J, Lachance Y, Zhao HF, Couët J, Leblanc G, Labrie F: Structure of two in tandem human 17b-hydroxysteroid dehydrogenase genes. Mol. Endocrinol. 4: 268-275 (1990) 13. Wu L, Einstein M, Geissler WM, Chan HK, Elliston KO, Andersson S: Expression cloning and characterization of human 17β-hydroxysteroid dehydrogenase type 2, a micro-somal enzyme possessing 20a-hydroxysteroid dehydrogenase activity. J. Biol. Chem. 268: 12964-12969 (1993) 14. Labrie Y, Durocher F, Lachance Y, Turgeon C, Simard J, Labrie C, Labrie F: The human type II 17β-hydroxysteroid dehydrogenase gene encodes two alternative-spliced messenger RNA Species. DNA Celt. Biol, in press (1995) 15. Geissler WM, Davis DL, Wu L, Bradshaw KD, Patel S, Mendonca BB, Elliston KO, Wilson JD, Russell DW, Anders-son S: Male pseudohermaphroditism caused by mutations of testicular 17β-hydroxysteroid dehydrogenase 3. Nature Genetics 7: 34-39 (1994) 16. Leenders F, Adamski J, Husen B, Thole HH, Jungblut PW: Molecular cloning and amino acid sequence of the porcine 17beta-estradiol dehydrogenase. Eur. J. Biochem. 222: 221-227 (1994) 17. Adamski J, Normand T, Leenders F, Monté D, Begue A, Stehelin D, Jungblut PW, de Launoit Y: Molecular cloning of a novel widely expressed human 80 kDa 17b-hydroxysteroid dehydrogenase 4. Biochem. J. 311: 437-443 (1995) 18. 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. 55: 581-587 (1995) 19. Andersson S, Russell DW: Structural and biochemical properties of cloned and expressed human and rat steroid 5α-reductases. Proc. Natl. Acad. Set. USA 87: 3640-3644 (1990) 20. Jenkins EP, Hsien C, Milatovich A, Normington K, Berman DM, Francke U, Russell DW: Characterization and chromosomal mapping of human steroid 5a-reductase gene and pseudogene and mapping of the mouse homologue. Genomics 11: 1102-1112 (1991) 21. Andersson S, Berman DM, Jenkins EP, Russell DW: Deletion of steroid 5a-reductase 2 gene in male pseudohermaphroditism. Nature 354: 159-161 (1991) 22. Labrie F, Sugimoto Y, Luu-The V, Simard J, Lachance Y, Bachvarov D, LeBlanc G, Durucher F, Paquet N: Structure of human type II 5a-reductase gene. Endocrinology 131: 1571-1573 (1992) 23. Rhéaume E, Simard J, Morel Y, Mebarki F, Zachmann M, Forest MG, New Ml, Labrie F: Congenital adrenal hyperplasia due to point mutations in the type II 3β-hydroxysteroid dehydrogenase gene. Nature Genet 1: 239-245 (1992) 24. Simard J, Rhéaume E, Sanchez R, Laflamme N, de Launoit Y, Luu-The V, van Seters AP, Gordon RD, Bettendorf M, Heinrich U, Moshang T, New MI, Labrie F: Molecular basis of congenital adrenal hyperplasia due to 3β-hydroxysteroid dehydrogenase deficiency. Mol. Endocrinol. 7: 716- 728 (1993) 25. Thigpen AE, Davis DL, Milatovich A, Mendonca BB, Imperato-McGinley J, Griffin JE, Francke U, Wilson JD, Russell DW: Molecular genetics of steroid 5α-reductase 2 deficiency. J. Clin. Ιnvest. 90: 799-809 (1992) 26. Luu-The V, Côté J, Labrie F: Purification and characterization of human placental 3β-hydroxysteroid dehydrogenase/A5-A⁴ isomerase. Clin. Invest. Med. 11: C200 (1988) 27. Luu-The V, Takahashi M, Labrie F: Purification of microsomal and mitochondrial 3ß-hydroxysteroid dehydrogenase/A5-A⁴ isomerase from human placenta. Ann. N.Y. Acad. Sci. 595: 386-388 (1990) 28. Bérubé D, Luu-The V, Lachance Y, Gagné R, Labrie F: Assignment of the human 3β-hydroxysteroid dehydrogenase gene to the p13 band of chromosome 1. Cytogenet. Cell. Genet 52: 199-200 (1989) 29. Dumont M, Luu-The V, Dupont E, Pelletier G, Labrie F: Characterization, expression and immunohistochemical localization of 3β-hydroxysteroid dehydrogenase/A5-A4 isomerase in human skin. J. Invest Dermatol 99: 415-421 (1992) 30. Dupont E, Luu-The V, Labrie F, Pelletier G: Ontogeny of 3β-hydroxy steroid dehydrogenase/A5-A⁴ isomerase (3β-HSD) in human adrenal gland performed by immunocytochemistry. Mol. Cell. Endocrinol. 74: R7-R10 (1990) 31. Dupont E, Luu-The V, Labrie F, Pelletier G: Ontogeny of 3β-hydroxysteroid dehydrogenase/A5-A⁴ isomerase (3β-HSD) in human testis as studied by immunocytochemistry. J. Androl. 12: 161-164 (1991) 32. Dupont E, Labrie F, Luu-The V, Pelletier G: Immunocytochemical localization of 3β-hydroxysteroid dehydrogenase/A5-A⁴ isomerase (3β-HSD) in human ovary. J. Clin. Endocrinol. Metab. 74: 994-998 (1992) 33. Riley SC, Dupont E, Walton JC, Luu-The V, Labrie F, Pelletier G, Challis JRG: Immunohistochemical localization of 3β-hydroxy-5-ene-steroid dehydrogenase/Δ5-Δ⁴ isomerase in human placenta and fetal membranes throughout gestation. J. Clin. Endocrinol. Metab. 75: 956-961 (1992) 34. Dupont E, Rhéaume E, Simard J, Luu-The V, Labrie F, Pelletier G: Ontogeny of 3β-hydroxysteroid dehydrogenase/Δ5-Δ⁴ isomerase in the rat adrenal as revealed by immunocytochemistry and in situ hybridization. Endocrinology 129: 2687-2692 (1991) 35. Juneau C, Dupont E, Luu-The V, Labrie F, Pelletier G: Ontogenesis of 3β-hydroxysteroid dehydrogenase/Δ5-Δ⁴ isomerase (3β-HSD) in the rat ovary as studied by immunocytochemistry and insitu hybridization. Biol. Reprod. 48: 226- 234 (1993) 36. Dupont E, Zhao HF, Rhéaume E, Simard J, Luu-The V, Labrie F, Pelletier G: Localization of 3β-hydroxysteroid dehydrogenase/Δ5-Δ⁴ isomerase in the rat gonads and adrenal glands by immunocytochemistry and in situ hybridization. Endocrinology 127: 1394-1403 (1990) 37. Zhao HF, Rhéaume E, Trudel C Zhao HF, Couët J, Labrie F, Simard J: Structure and sexual dimorphic expression of a liver-specific rat 3β-hydroxysteroid dehydrogenase/isomerase. Endocrinology 127: 3237-3239 (1990) 38. Zhao HF, Labrie C, Simard J, de Launoit Y, Trudel C, Martel C, Rhéaume E, Dupont E, Luu-The V, Pelletier G, Labrie F: Characterization of rat 3β-hydroxysteroid dehydrogenase/Δ5-Δ⁴ isomerase cDNAs and differential tissue-specific expression of the corresponding mRNAs in steroidogenic and peripheral tissues. J. Biol. Chem. 266: 583- 593 (1991) 39. Lorence MC, Naville D, Graham-Lorence SE, Mack SO, Murry BA. Trant JM, Mason Jl: 3ß-hydroxysteroid dehydrogenase/Δ5-Δ⁴ isomerase expression in rat and characterization of the testis isoform. Mol. Cell. Endocrinol. 80: 21-31 (1991) 40. Naville D, Keeney DS, Jenkin G, Murry BA, Head JR, Mason JΙ: Regulation of expression of male-specific rat liver microsomal 3β-hydroxy-steroid dehydrogenase. Mol. Endocrinol. 5: 1090-1100 (1991) 41. Simard J, Couët J, Durocher F, Labrie Y, .Sanchez R, Breton N, Turgeon C, Labrie F: Structure and tissue-specific expression of a novel member of the rat 3β-hydroxysteroid dehydrogenase/Δ5-Δ⁴ isomerase (3β-HSD) family: the exclusive 3ß-HSD gene expressed in the skin. J. Biol. Chem. 268: 19659-1966 (1993) 42. Bain PA, Yoo M, Clarke T, Hammond SH, Payne AH: Multiple forms of mouse 3β-hydroxysteroid dehydrogenase/Δ5-Δ⁴ isomerase and differential expression in gonads, adrenal glands, liver, and kidneys of both sexes. Proc. Natl. Acad. Sci. USA 88: 8870-8874 (1991) 43. Clarke TR, Bain PA, Greco TL, Payne AH: A novel mouse kidney 3β-hydroxysteroid dehydrogenase complementary DNA encodes a 3-ketosteroid reductase instead of a 3p-hydroxysteroid dehydrogenase/ Δ5-Δ⁴ isomerase. Mot. Endocrinol 7: 1569-1578 (1993) 44. Keeney DS, Navüle D, Milewich L, Bartke A, and Mason, J. I.: Multiple isoforms of 3β-hydroxysteroid dehydrogenase/ Δ5-Δ⁴ isomerase in mouse tissues: male-specific isoforms are expressed in the gonads and liver Endocrinology 133: 39-45 (1993) 45. Chedrese PJ, Luu-The V, Labrie F, Juorio AV, Murphy BD: Evidence for the regulation of 3p-hydroxysteroid dehydrogenase/messenger RNA by human chorionic gonadotropin in luteinized porcine granulosa cells Endocrinology 126: 2228-2230 (1990) 46. Chedrese PJ, Zhang D, Luu-The V, Labrie F, Juorio AV, Murphy BD: Regulation of the mRNA expression of 3β-hydroxy-5-ene steroid dehydrogenase in porcine granulosa cells in culture: a role for the protein kinase C pathway. Mol. Endocrinol. 4: 1532-1538 (1991) 47. Trudel C, Couët J, Martel C, Labrie C, Labrie F: Regu-lation of adrenal 3β-hydroxysteroid dehydrogenase/ Δ5-Δ⁴ isomerase expression and activity by adrenocorticotropin and corticosterone in the rat. Endocrinology 129: 2077-2084 (1991) 48. Srivastava RK, Luu-The V, Marronr BL, Sridaran R: Suppression of luteal steroidogenesis by an LHRH antagonist (Nal-Lys antagonist: antide) in vitro during early pregnancy in the rat. J. Mol. Endocrinol. 13: 87-94 (1994) 49. Potts J, Creange JE, Harding HR, Schane HP: Trilostane, an orally active inhibitor of steroid biosynthesis. Steroids 32: 257-260 (1978) 50. Takahashi M, Luu-The V, Labrie F: Inhibitory effect of synthetic progestins, 4-MA and cyanoketone on human placental 3P-hydroxysterold dehydrogenase/5-4-ene-isomerase activity. J. Steroid Biochem. Mol. Biol 37: 231-236 (1990) 51. Luu-The V, Takahashi M, de Launoit Y, Dumont M, Lachance Y, Labrie F: Evidence for distinct dehydrogenase and isomerase sites within a single 3p-hydroxysteroid dehydrogenase 5-ene-4-ene isomerase protein. Biochemistry 30: 8861-8865 (1991) 53. Zerah M, Rhéaume E, Mani P, Schram P, Simard J, Labrie F, New MI: No evidence of mutations in the genes for type I and type II 3β-hydroxysterold dehydrogenase (3β-HSD) in nonclassical 3βHSD deficiency. J. Clin. Endocrinol. Metab. 79: 1811-1817 (1994) 54. Verreault H: (1994) In: Régulation transcriptionnelle des gènes de types I et II encodant la 3β-hydroxystéroide déshydrogénase/ Δ5-Δ⁴ isomérase humaine. Thesis (with Dr Van Luu-The) Laval University, 1994 55. Guerin SL, Leclerc S, Verreault H, Labrie F, Luu-The V: Overlapping c/s-acting elements located in the first intron of the gene for type I 3p-hydroxysteroid dehydrogenase modulate its transcriptional activity. Moi. Endocrinol. 9: 1583- 1597 (1995) 56. Pittaway DE, Andersen RN, Coleman SA.Jr, Givens JR, Wiser WL: Human ovarian 17β-hydroxysteroid oxidoreductase activity. A comparison of normal and polycystic ovarian tissues. J. Clin. Endocrinol. Metab. 56: 715-719 (1983) 57. Inano H, Tamaoki B: Testicular 17β-hydroxysteroid de-hydrogenase: molecular properties and reaction mechanism. Steroids 48: 3-26 (1986) 58. Martel C, Rhéaume E, Takahashi M, Trudel C, Couët J, Luu-The V, Simard J, Labrie F: Distribution of 17β-hydroxysteroid dehydrogenase gene expression and activity in rat and in human tissues. J. Steroid Biochem. Mol. Biol. 41: 597- 603 (1992) 59. Bleau G, Roberts KD, Chapdelaine A: The in vitro and in vivo uptake and metabolism of steroid in human adipose tissue. J. Clin. Endocrinol. Metab. 39: 236-246 (1974) 60. Casey ML, MacDonald PC, Andersson S: 17β-Hydroxysteroid dehydrogenase type 2: Chromosomal Assignment and progestin regulation of gene expression in human endometrium. J. Clin. Invest. 94: 2135-2141 (1994) 61. Dumont M, Luu-The V, de Launoit Y, Labrie F: Expression of human 17β-hydroxysteroid dehydrogenase in mammalian cells. J. Steroid. Biochem. Mol. Biol 41: 605-608 (1992) 62. Lin S-X, Yang F, Jin J-Z, Breton R, Zhu D-W, Luu-The V, Labrie F: Subunit identity of the dimeric 17β-hydroxysteroid dehydrogenase from human placenta. J. Biol. Chem. 267: 16182-16187 (1992) 63. Ghosh D, Pletnev VZ, Zhu D-W, Wawrzak Z, Duax WL, Pangborn W, Labrie F, Lin S-X (1995) Structure of human estrogenic 17β-hydroxysteroid dehydrogenase at 2.2 A resolution. Structure 3: 503-513 (1995) 64. Sansone G, Reisner RM: Differential rates of conversion of testosterone to dihydrotestosterone in acne and in normal human skin: a possible pathologic factor in acne. J. Invest. Dermatol. 56: 366-372 (1971) 65. Kuttenn F, Mowszowicz I, Schaison G, Mauvais-Jarvis P: Androgen production and skin metabolism in hirsutism. J. Endocrinol. 25: 83-91 (1977) 66. Luu-The V, Sugimoto Y, Puy L, Labrie Y, Lopez-Solache I, Singh M, Labrie F: Characterization, expression, and immunochemical localization of 5α-reductase in human skin. J. Invest. Dermatol 102: 221-226 (1994) 67. Thigpen AE, Silver Rl, Guileyardo JM, Vasey ML, Mc-Donnell JD, Russel DW: Tissue distribution and ontogeny of steroid 5α-reductase isozyme expression. J. Clin. Ιnvest. 92: 903-910 (1993) 68. Itami S, Kurata S, Sonoda T: Takayasu S (1991) Characterization of 5α-reductase in cultured human dermal papilla cells from beard and occipital scalp hair. J. invest. Dermatol 96: 57-60 (1991) 69. Sugimoto Y, Lopez-Solache I, Labrie F, Luu-The V: Cations Inhibit specifically type I 5a-reductase found in human skin. J. Invest. Derm. 104: 775-778 (1995) 70. Cheng KC, White PC, Qin K: Molecular cloning and expression of rat 3α-hydroxysteroid dehydrogenase. Mol. Endocrinol. 5: 823-828 (1991) 71. Palowski JE, Huizinga M, Penning TM: Cloning and sequencing of the cDNA for rat liver 3α-hydroxysteroid/dihydrodiol dehydrogenase. J. Biol Chem. 266: 8820- 8825 (1991) 72. Miura R, Shiota K, Noda K, Yagi S, Ogawa T, Takahashi M: Molecular cloning of cDNA for rat ovarian 20α-hydroxysteroid dehydrogenase. Biochem. J. 299: 561-567 (1994) 73. Mao J, Duan WR, Albarracin CT, Parmer TG, Gibori G: Isolation and characterization of rat luteal cDNA encoding 20α-hydroxysteroid dehydrogenase. Biochem. Biophys. Res. Comm. 201: 1289-1295 (1994) 74. Lacy WR, Washenick KJ, Cook RG, Dunbar BS: Molecular cloning and expression of an abundant rabbit ovarian protein with 20a-hydroxysteroid dehydrogenase activity. Mol Endocrinol 7: 58-66 (1993) 75. Warren JC, Murdock GL, Ma Y, Goodman SR, Zimmer WE: Molecular cloning of testicular 20α-hydroxysteroid dehydrogenase: identity with aldose reductase. Biochemistry 32: 1401-1406 (1993) 76. Winters CJ, Molowa DT, Guzelian PS: Isolation and characterization of cloned cDNAs encoding human liver chlordecone reductase. Biochemistry 29:1080-1087 (1990) 77. Deyashiki Y, Ogasawara 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. 299: 545-552 (1994) 78. Watanabe K, Fuji Y, Nakayama K, Ohkubo H( Kuramitsu S, Kagamayama H, Shigetada N, Hayashi O: Structural similarity of bovine Jung prostaglandin F synthase to lens epsilon-crystallin of the european common frog. Proc. Natl. Acad. Sci. USA 85: 11-15 (1988) 79. Tomarev SI, Zinovieva RD, Dolgievich SM, Luchin SV, Krayev AS, Skryabin KG, Gause GG: A novel type of crystallin in the frog eye lens. FEBS Lett 171: 297-302 (1984) 80. Carper D, Nishimura C, Shinohara T, Dietzhold B, Wistow G, Craft C, Kador P, Kinoshita JH: Aldose reductase and rho-crystallin belong to the same protein superfamily as aldehyde reductase. FEBS Lett. 220: 209-213 (1987) 81. Bohren KM, Bullock B, Wermuth B, Gabbay KH: The aldo-keto reductase superfamily cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases. J. Biol. Chem. 264: 9547-9551 (1989) 82. Stolz A, Hammond L, Lou H, Takikawa H, Ronk M, and Shively JE: cDNA cloning and expression of the human hepatic bile acid-binding protein A member of the monomeric reductase gene family. J. Biol. Chem. 268: 10448-10457 (1993) 83. Qin KN, New Ml, Cheng KC: Molecular cloning of human cDNAs encoding proteins structurally related to 3α-hydroxysteroid dehydrogenase. J. Steroid. Biochem. Mot. Biol. 46: 673-679 (1993) 84. Takikawa H, Stolz A, Sugiyama Y, Yoshida H, Yamanaka M. Kaplowit N: Relationship between the newly identified bile acid binder and bile acid oxidoreductases in human liver. J. Biol Chem. 265: 2132-2136 (1990) 85. Khanna M, Qin KN, Wang RW, Cheng KC: Substrate specificity, gene structure, and tissue-specific distribution of multiple human 3 alpha-hydroxysteroid dehydrogenases. J. Biol. Chem. 270: 20162-10168 (1995) 86. 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. 228: 474- 479 (1996) 87. Jakoby WB, Sekura RD, Lyon ES, Marcus CJ, Wang JL: Sulfotransferases. In: Enzymatic Basis of Detoxification (W.B. Jakoby, ed.), vol. 2, pp. 199-228, Academic Press, New York, 1980 88. Payne AH: Gonadal steroid sulfates and sulfatase V. Human testicular steroid sulfatase: partial characterization and possible regulation by free steroids. Biochim. Biophys. Acta 258: 473-483 (1972) 89. Milewich L, Garcia RL, Johnson AR: Steroid sulfatase activity in human lung tissue and in endothelial pulmonary cells in culture. J. Clin. Endocrinol. Metab. 57: 8-14 (1983) 90. Gant NF, Milewich L, Calvert ME, MacDonald PC: Steroid sulfatase activity in human fetal membranes. J. Clin. Endocrinol. Metab. 45: 965-972 (1977) 91. Chibbar R, Hobkirk, R, Mitchell, BF: Sulfohydrolase activity for estrone sulfate and dehydroepiandrosterone sulfate in human fetal membranes and decidua around the tipne of parturition. J. Clin. Endocrinol. Metab. 56: 653-661 (1986) 92. Prost O, Adessi GL: Estrone and dehydroepiandrosterone sulfatase activities in normal and pathological human endometrium biopsies. J. Clin. Endocrinol. Metab. 56: 653- 661 (1983) 93. Farnsworth WE: Human prostatic dehydroepiandrosterone sulfate sulfatase. Steroid 21: 647-664 (1973) 94. Perumal AS, Robins E: Regional and subcellular distribution of aryl- and steroid sulfatases in brain. Brain Res. 59: 349-358 (1973) 95. Ruder HJ, Loriaux L and Lipsett MB (1972) Estrone sulfate: production rate and metabolism in man. J Clin Invest. 51: 1020-1033 96. Poortman J, Andriesse R, Agema A, Donker GH, Scharz F, Thijssen JHH: In: Adrenal Androgens (Genazzani AR, Thijssen JHH and Sliteri PK, eds), pp 219-240, Raven Press, New York, 1980 97. Dao TL, Libby PR: Steroid sulfate formation in human breast tumors and hormone dependency. In: Estrogen Target Tissues and Neoplasia (Dao TL, ed), pp 181-200, The University of Chicago Press, Chicago, 1972 98. Pewnim T, Adams JB, Ho KP: Estrogen sulfurylation as an alternative indicator of hormone dependence in human breast cancer. Steroids 39: 47-52 (1982) 99. Adams JB, Phillips NS, Pewnim T: Expression of hydroxysteroid sulphotransferase is related to estrogen receptor status in human mammary cancer. J. Steroid. Biochem. 33: 637-642 (1989) 100. Nash AR, Glenn WE, Moore J, Kerr AR Thompson, Thompson EOP: Oestrogen sulfotransferase: Molecular cloning and sequencing of cDNA for the bovine placental enzyme. Aust. J. Biol. Sci. 41: 507-516 (1988) 101. Bernier F, Löpez-Solache I, Labrie F, Luu-The V: Cloning and expression of cDNA encoding human placental estrogen sulfotransferase Mol. Cell. Endocrinol. 99: R11-R15 (1994) 102. Bernier F, Leblanc G, Labrie F, Luu-The V: Structure of human estrogen and aryl sulfotransferase gene – Two mRNA species issued from a single gene. J. Biol. Chem. 269: 28200- 28206 (1994) 103. Aksoy IA, Wood TC, Weinshilboum R: Human liver estrogen sulfotransferase: identification by cDNA cloning and expression. Biochem. Biophys. Res. Commun. 200: 1621- 1629 (1994) 104. Falany CN, Vazquez ME, Kalb JM: Purification and characterization of human liver dehydroepiandrosterone sulphotransferase. Biochem. J. 260: 641-646 (1989) 105. Otterness DM, Wieben ED, Wood TC, Watson RWG, Madden BJ, McCormick DJ, Weinshilboum RM: Human liver dehydroepiandrosterone sulfotransferase: molecular cloning and expression of the cDNA. Mol. Pharmac. 41: 865-872 (1992) 106. Comer KA, Falany JL, Falany CN: Cloning and expression of human liver dehydroepiandrosterone. Biochem. J. 289: 233-240 (1993) 107. Luu-The V, Dufort I, Paquet N, Reimnitz G, Labrie F: Structural characterization and expression of the human dehydroepiandrosterone sulfotransferase gene DNA and Cell. Biol. 14: 511-518 (1995) 108. Otterness D, Weinshilboum R: Human dehydroepiandrosterone sulfatransferase: molecular cloning of cDNA and genomic DNA. Chem. Biol. Interact. 92: 145-159 (1994) 109. Durocher F, Morissette J, Dufort I, Simard J, Luu-The V: Genetic Linkage mapping of the dehydroepiandrosterone sulfotransferase (STD) gene on chromosome 19q 13.3 region. Genomics 29: 781-783 (1995) 110. Dufort I, Tremblay Y, Belanger A, Labrie F, Luu-The V: Isolation and characterization of a stereospecific 3β-hydroxysteroid sulfotransferase (pregnenolone sulfotransferase) cDNA. DNA Cell. Biol. 15: 481-487 (1996) |
|
| Relative Papers |
Online ISSN 1011-6575
Άρθρα Δημοσιευμένα σε αυτό το Περιοδικό Καταχωρούνται στα:
- Chemical Abstracts
- Elsevier’s Bibliographic Databases: Scopus, EMBASE, EMBiology, Elsevier BIOBASE SCImago Journal and Country Rank Factor
Articles published in this Journal are Indexed or Abstracted in: • Chemical Abstracts • Elsevier’s Bibliographic Databases: Scopus, EMBASE, EMBiology, Elsevier BIOBASE SCImago Journal and Country Rank Factor
Συντακτικη Επιτροπή-Editorial Board
| ΕΤΗΣΙΑ ΣΥΝΔΡΟΜΗ 1997 – ANNUAL SUBSCRIPTION 1997 | |
| Γλώσσα Πλήρους Κειμένου – Full Text Language | Αγγλικά – English |
| Παραγγελία – Αγορά – Order – Buy | Ηλεκτρονική Μορφή: pdf (70 €) – Digital Type: pdf (70 €)
pharmakonpress[at]pharmakonpress[.]gr |
| Έντυπη Μορφή (70 € + έξοδα αποστολής) – Printed Type (70 € + shipping)
pharmakonpress[at]pharmakonpress[.]gr |
|