메뉴 건너뛰기




Volumn 54, Issue 4, 2003, Pages 275-289

Selective reduction of AKR1C2 in prostate cancer and its role in DHT metabolism

Author keywords

AKR1C1; AKR1C2; Androgen metabolism; Prostate cancer; Real time PCR

Indexed keywords

ALDOKETOREDUCTASE 1C; ANDROSTANEDIOL; ANDROSTANOLONE; MESSENGER RNA; OXIDOREDUCTASE; STEROID 5ALPHA REDUCTASE; UNCLASSIFIED DRUG;

EID: 0037372349     PISSN: 02704137     EISSN: None     Source Type: Journal    
DOI: 10.1002/pros.10192     Document Type: Article
Times cited : (76)

References (65)
  • 4
    • 0027304028 scopus 로고
    • Estrogens, progestogens, normal breast cell proliferation, and breast cancer risk
    • Pike MC, Spicer DV, Dahmoush L, Press MF. Estrogens, progestogens, normal breast cell proliferation, and breast cancer risk. Epidemiol Rev 1993;15:17-35.
    • (1993) Epidemiol Rev , vol.15 , pp. 17-35
    • Pike, M.C.1    Spicer, D.V.2    Dahmoush, L.3    Press, M.F.4
  • 5
    • 0027450031 scopus 로고
    • Hormonal chemoprevention of cancer in women
    • Henderson BE, Ross RK, Pike MC. Hormonal chemoprevention of cancer in women. Science 1993;259:633-638.
    • (1993) Science , vol.259 , pp. 633-638
    • Henderson, B.E.1    Ross, R.K.2    Pike, M.C.3
  • 8
    • 0028696273 scopus 로고
    • Role of androgens in prostatic cancer
    • Isaacs JT. Role of androgens in prostatic cancer. Vitamin Horm 1994;49:433-502.
    • (1994) Vitamin Horm , vol.49 , pp. 433-502
    • Isaacs, J.T.1
  • 10
    • 0031077802 scopus 로고    scopus 로고
    • Basic science aspects of prostate cancer
    • Dorkin TJ, Neal DE. Basic science aspects of prostate cancer. Semin Cancer Biol 1997;8:21-27.
    • (1997) Semin Cancer Biol , vol.8 , pp. 21-27
    • Dorkin, T.J.1    Neal, D.E.2
  • 11
    • 0029684749 scopus 로고    scopus 로고
    • Provocative aspects of androgen genetics
    • Brown TR. Provocative aspects of androgen genetics. Prostate Suppl 1996;6:9-12.
    • (1996) Prostate Suppl , vol.6 , pp. 9-12
    • Brown, T.R.1
  • 12
    • 0030995035 scopus 로고    scopus 로고
    • Androgens and prostate cancer: Biology, pathology and hormonal therapy
    • Galbraith SM, Duchesne GM. Androgens and prostate cancer: Biology, pathology and hormonal therapy. Eur J Cancer 1997;33:545-554.
    • (1997) Eur J Cancer , vol.33 , pp. 545-554
    • Galbraith, S.M.1    Duchesne, G.M.2
  • 16
    • 0027376310 scopus 로고
    • Intracrinology: The basis for the rational design of endocrine therapy at all stages of prostate cancer
    • Labrie F, Dupont A, Simard J, Luu-The V, Belanger A. Intracrinology: the basis for the rational design of endocrine therapy at all stages of prostate cancer. Eur Urol 1993;24:94-105.
    • (1993) Eur Urol , vol.24 , pp. 94-105
    • Labrie, F.1    Dupont, A.2    Simard, J.3    Luu-The, V.4    Belanger, A.5
  • 18
    • 0033565113 scopus 로고    scopus 로고
    • GEN GEN: The genomic genetic analysis of androgen-metabolic genes and prostate cancer as a paradigm for the dissection of complex phenotypes
    • Reichardt JK. GEN GEN: The genomic genetic analysis of androgen-metabolic genes and prostate cancer as a paradigm for the dissection of complex phenotypes. Front Biosci 1999;4:D596-D600.
    • (1999) Front Biosci , vol.4
    • Reichardt, J.K.1
  • 20
    • 0034652715 scopus 로고    scopus 로고
    • Susceptibility to prostate cancer: Interaction between genotypes at the androgen receptor and prostate-specific antigen loci
    • Xue W, Irvine RA, Yu MC, Ross RK, Coetzee GA, Ingles SA. Susceptibility to prostate cancer: Interaction between genotypes at the androgen receptor and prostate-specific antigen loci. Cancer Res 2000;60:839-841.
    • (2000) Cancer Res , vol.60 , pp. 839-841
    • Xue, W.1    Irvine, R.A.2    Yu, M.C.3    Ross, R.K.4    Coetzee, G.A.5    Ingles, S.A.6
  • 23
    • 0030784509 scopus 로고    scopus 로고
    • Expression and characterization of recombinant type-2 3 alpha hydroxysteroid dehydrogenase (HSD) from human postate - Demonstration of bifunctional 3-alpha/17-beta-HSD activity and cellular distribution
    • Lin H-K, Jez JM, Schlegel BP, Peehl DM, Pachter JA, Penning TM. Expression and characterization of recombinant type-2 3 alpha hydroxysteroid dehydrogenase (HSD) from human postate - Demonstration of bifunctional 3-alpha/17-beta-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
  • 24
    • 0035093784 scopus 로고    scopus 로고
    • Human types 1 and 3 alpha-hydroxysteroid dehydrogenases: Differential lability and tissue distribution
    • Dufort I, Labrie F, Luu-The V. Human types 1 and 3 alpha-hydroxysteroid dehydrogenases: Differential lability and tissue distribution. J Clin Endocrinol Metab 2001;86:841-886.
    • (2001) J Clin Endocrinol Metab , vol.86 , pp. 841-886
    • Dufort, I.1    Labrie, F.2    Luu-The, V.3
  • 25
    • 0001429526 scopus 로고    scopus 로고
    • Characteristics of a highly labile human type 5 17beta-hydroxysteroid dehydrogenase
    • Dufort I, Rheault P, Huang XF, Soucy P, Luu-The V. Characteristics of a highly labile human type 5 17beta-hydroxysteroid dehydrogenase. Endocrinology 1999;140:568-5674.
    • (1999) Endocrinology , vol.140 , pp. 568-5674
    • Dufort, I.1    Rheault, P.2    Huang, X.F.3    Soucy, P.4    Luu-The, V.5
  • 26
    • 0029091370 scopus 로고
    • Substrate specificity, gene structure, and tissue-specific distribution of multiple human 3 alpha-hydroxysteroid dehydrogenases
    • 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 1995;270:20162-20168.
    • (1995) J Biol Chem , vol.270 , pp. 20162-20168
    • Khanna, M.1    Qin, K.N.2    Wang, R.W.3    Cheng, K.C.4
  • 27
    • 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
  • 28
    • 0030034858 scopus 로고    scopus 로고
    • Relationship of human liver dihydrodiol dehydrogenases to hepatic bile- acid-binding protein and an oxidoreductase of human colon cells
    • Hara A, Matsuura K, Tamada Y, Sato K, Miyabe Y, Deyashiki Y, Ishida N. Relationship of human liver dihydrodiol dehydrogenases to hepatic bile- acid-binding protein and an oxidoreductase of human colon cells. Biochem J 1996;313:373-376.
    • (1996) Biochem J , vol.313 , pp. 373-376
    • Hara, A.1    Matsuura, K.2    Tamada, Y.3    Sato, K.4    Miyabe, Y.5    Deyashiki, Y.6    Ishida, N.7
  • 29
    • 0028269192 scopus 로고
    • Molecular cloning of two human liver 3 alpha-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 3 alpha-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
    • 0021689219 scopus 로고
    • Identification and purification of a 36 kDa bile acid binder in human hepatic cytosol
    • Stolz A, Sugiyama Y, Kuhlenkamp J, Kaplowitz N. Identification and purification of a 36 kDa bile acid binder in human hepatic cytosol. FEBS Lett 1984;177:31-35.
    • (1984) FEBS Lett , vol.177 , pp. 31-35
    • Stolz, A.1    Sugiyama, Y.2    Kuhlenkamp, J.3    Kaplowitz, N.4
  • 32
    • 0030876351 scopus 로고    scopus 로고
    • A new nomenclature for the aldoketo reductase superfamily
    • Jez JM, Flynn TG, Penning TM. A new nomenclature for the aldoketo reductase superfamily. Biochem Pharmacol 1997;54:639-647.
    • (1997) Biochem Pharmacol , vol.54 , pp. 639-647
    • Jez, J.M.1    Flynn, T.G.2    Penning, T.M.3
  • 33
    • 0027158606 scopus 로고
    • cDNA cloning and expression of the human hepatic bile acid-binding protein. A member of the monomeric reductase gene family
    • Stolz A, Hammond L, Lou H, Takikawa H, Ronk M, 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 1993;268:10448-10457.
    • (1993) J Biol Chem , vol.268 , pp. 10448-10457
    • Stolz, A.1    Hammond, L.2    Lou, H.3    Takikawa, H.4    Ronk, M.5    Shively, J.E.6
  • 34
    • 0025308540 scopus 로고
    • Purification and properties of multiple forms of dihydrodiol dehydrogenase from human liver
    • Hara A, Taniguchi H, Nakayama T, Sawada H. Purification and properties of multiple forms of dihydrodiol dehydrogenase from human liver. J Biochem (Tokyo) 1990;108:250-254.
    • (1990) J Biochem (Tokyo) , vol.108 , pp. 250-254
    • Hara, A.1    Taniguchi, H.2    Nakayama, T.3    Sawada, H.4
  • 35
    • 0034287545 scopus 로고    scopus 로고
    • Human 3alpha-hydroxysteroid dehydrogenase isoforms (AKR1C1-AKR1C4) of the aldo-keto reductase superfamily: Functional plasticity and tissue distribution reveals roles in the inactivation and formation of male and female sex hormones
    • Penning TM, Burczynski ME, Jez JM, Hung CF, Lin HK, Ma H, Moore M, Palackal N, Ratnam K. Human 3alpha-hydroxysteroid dehydrogenase isoforms (AKR1C1-AKR1C4) of the aldo-keto reductase superfamily: Functional plasticity and tissue distribution reveals roles in the inactivation and formation of male and female sex hormones. Biochem J 2000;351:67-77.
    • (2000) Biochem J , vol.351 , pp. 67-77
    • Penning, T.M.1    Burczynski, M.E.2    Jez, J.M.3    Hung, C.F.4    Lin, H.K.5    Ma, H.6    Moore, M.7    Palackal, N.8    Ratnam, K.9
  • 36
    • 0032168199 scopus 로고    scopus 로고
    • Sequence of the cDNA of a human dihydrodiol dehydrogenase isoform (AKR1C2) and tissue distribution of its mRNA
    • Shiraishi H, Ishikura S, Matsuura K, Deyashiki Y, Ninomiya M, Sakai S, Hara A. Sequence of the cDNA of a human dihydrodiol dehydrogenase isoform (AKR1C2) and tissue distribution of its mRNA. Biochem J 1998;334:399-405.
    • (1998) Biochem J , vol.334 , pp. 399-405
    • Shiraishi, H.1    Ishikura, S.2    Matsuura, K.3    Deyashiki, Y.4    Ninomiya, M.5    Sakai, S.6    Hara, A.7
  • 37
    • 0030925341 scopus 로고    scopus 로고
    • Molecular endocrinology of hydroxysteroid dehydrogenases
    • Penning TM. Molecular endocrinology of hydroxysteroid dehydrogenases. Endocr Rev 1997;18:281-305.
    • (1997) Endocr Rev , vol.18 , pp. 281-305
    • Penning, T.M.1
  • 38
    • 0028366074 scopus 로고
    • Genomic organization and chromosomal localization of a novel human hepatic dihydrodiol dehydrogenase with high affinity bile acid binding
    • Lou H, Hammond L, Sharma V, Sparkes RS, Lusis AJ, Stolz A. Genomic organization and chromosomal localization of a novel human hepatic dihydrodiol dehydrogenase with high affinity bile acid binding. J Biol Chem 1994;269:8416-8422.
    • (1994) J Biol Chem , vol.269 , pp. 8416-8422
    • Lou, H.1    Hammond, L.2    Sharma, V.3    Sparkes, R.S.4    Lusis, A.J.5    Stolz, A.6
  • 39
    • 0021999084 scopus 로고
    • 5 alpha-Reductase activity in the genital skin of hirsute women
    • Serafini P, Ablan F, Lobo RA. 5 alpha-Reductase activity in the genital skin of hirsute women. J Clin Endocrinol Metab 1985;60:349-355.
    • (1985) J Clin Endocrinol Metab , vol.60 , pp. 349-355
    • Serafini, P.1    Ablan, F.2    Lobo, R.A.3
  • 40
    • 0034013724 scopus 로고    scopus 로고
    • Analysis of cyclin-dependent kinase inhibitor expression and methylation patterns in human prostate cancers
    • Nguyen TT, Nguyen CT, Gonzales FA, Nichols PW, Yu MC, Jones PA. Analysis of cyclin-dependent kinase inhibitor expression and methylation patterns in human prostate cancers. Prostate 2000;43:233-242.
    • (2000) Prostate , vol.43 , pp. 233-242
    • Nguyen, T.T.1    Nguyen, C.T.2    Gonzales, F.A.3    Nichols, P.W.4    Yu, M.C.5    Jones, P.A.6
  • 41
    • 0032931896 scopus 로고    scopus 로고
    • Expression of the androgen metabolizing enzyme UGT2B15 in adipose tissue and relative expression measurement using a competitive RT-PCR method
    • Tchernof A, Levesque E, Beaulieu M, Couture P, Despres JP, Hum DW, Belanger A. Expression of the androgen metabolizing enzyme UGT2B15 in adipose tissue and relative expression measurement using a competitive RT-PCR method. Clin Endocrinol (Oxf) 1999;50:637-642.
    • (1999) Clin Endocrinol (Oxf) , vol.50 , pp. 637-642
    • Tchernof, A.1    Levesque, E.2    Beaulieu, M.3    Couture, P.4    Despres, J.P.5    Hum, D.W.6    Belanger, A.7
  • 42
    • 0035266404 scopus 로고    scopus 로고
    • Evaluation of androgen, estrogen (ER alpha and ER beta), and progesterone receptor expression in human prostate cancer by real-time quantitative reverse transcription-polymerase chain reaction assays
    • Latil A, Bieche I, Vidaud D, Lidereau R, Berthon P, Cussenot O, Vidaud M. Evaluation of androgen, estrogen (ER alpha and ER beta), and progesterone receptor expression in human prostate cancer by real-time quantitative reverse transcription-polymerase chain reaction assays. Cancer Res 2001;61:1919-1926.
    • (2001) Cancer Res , vol.61 , pp. 1919-1926
    • Latil, A.1    Bieche, I.2    Vidaud, D.3    Lidereau, R.4    Berthon, P.5    Cussenot, O.6    Vidaud, M.7
  • 43
    • 0033872068 scopus 로고    scopus 로고
    • Detection of gene amplification in archival breast cancer specimens by laser-assisted microdissection and quantitative real-time polymerase chain reaction
    • Lehmann U, Glockner S, Kleeberger W, von Wasielewski HF, Kreipe H. Detection of gene amplification in archival breast cancer specimens by laser-assisted microdissection and quantitative real-time polymerase chain reaction. Am J Pathol 2000;156:1855-1864.
    • (2000) Am J Pathol , vol.156 , pp. 1855-1864
    • Lehmann, U.1    Glockner, S.2    Kleeberger, W.3    Von Wasielewski, H.F.4    Kreipe, H.5
  • 44
    • 0030033679 scopus 로고    scopus 로고
    • Vicia faba root tip micronucleus test on the mutagenicity of water-soluble contents of cigarette smoke
    • Ji Q, Chen Y. Vicia faba root tip micronucleus test on the mutagenicity of water-soluble contents of cigarette smoke. Mutat Res 1996;359:1-6.
    • (1996) Mutat Res , vol.359 , pp. 1-6
    • Ji, Q.1    Chen, Y.2
  • 45
    • 0031028190 scopus 로고    scopus 로고
    • Immortalized and tumorigenic adult human prostatic epithelial cell lines: Characteristics and applications. Part 3. Oncogenes, suppressor genes, and applications
    • Webber MM, Bello D, Quader S. Immortalized and tumorigenic adult human prostatic epithelial cell lines: Characteristics and applications. Part 3. Oncogenes, suppressor genes, and applications. Prostate 1997;30:136-142.
    • (1997) Prostate , vol.30 , pp. 136-142
    • Webber, M.M.1    Bello, D.2    Quader, S.3
  • 47
    • 0023483150 scopus 로고
    • Cyclical oxidation-reduction of the C3 position on bile acids catalyzed by rat hepatic 3 alpha-hydroxysteroid dehydrogenase. I. Studies with the purified enzyme, isolated rat hepatocytes, and inhibition by indomethacin
    • Takikawa H, Stolz A, Kaplowitz N. Cyclical oxidation-reduction of the C3 position on bile acids catalyzed by rat hepatic 3 alpha-hydroxysteroid dehydrogenase. I. Studies with the purified enzyme, isolated rat hepatocytes, and inhibition by indomethacin. J Clin Invest 1987;80:852-860.
    • (1987) J Clin Invest , vol.80 , pp. 852-860
    • Takikawa, H.1    Stolz, A.2    Kaplowitz, N.3
  • 48
    • 0023138036 scopus 로고
    • 3 alpha-hydroxysteroid dehydrogenase activity of the Y′ bile acid binders in rat liver cytosol. Identification, kinetics, and physiologic significance
    • Stolz A, Takikawa H, Sugiyama Y, Kuhlenkamp J, Kaplowitz N. 3 alpha-hydroxysteroid dehydrogenase activity of the Y′ bile acid binders in rat liver cytosol. Identification, kinetics, and physiologic significance. J Clin Invest 1987;79:427-434.
    • (1987) J Clin Invest , vol.79 , pp. 427-434
    • Stolz, A.1    Takikawa, H.2    Sugiyama, Y.3    Kuhlenkamp, J.4    Kaplowitz, N.5
  • 49
    • 0028949229 scopus 로고
    • Localization of multiple human dihydrodiol dehydrogenase (DDH1 and DDH2) and chlordecone reductase (CHDR) genes in chromosome 10 by the polymerase chain reaction and fluorescence in situ hybridization
    • Khanna M, Qin KN, Klisak I, Belkin S, Sparkes RS, Cheng KC. Localization of multiple human dihydrodiol dehydrogenase (DDH1 and DDH2) and chlordecone reductase (CHDR) genes in chromosome 10 by the polymerase chain reaction and fluorescence in situ hybridization. Genomics 1995;25:588-590.
    • (1995) Genomics , vol.25 , pp. 588-590
    • Khanna, M.1    Qin, K.N.2    Klisak, I.3    Belkin, S.4    Sparkes, R.S.5    Cheng, K.C.6
  • 50
    • 0031936948 scopus 로고    scopus 로고
    • Molecular evolution of the aldo-keto reductase gene superfamily
    • Seery LT, Nestor PV, FitzGerald GA. Molecular evolution of the aldo-keto reductase gene superfamily. J Mol Evol 1998;46:139-146.
    • (1998) J Mol Evol , vol.46 , pp. 139-146
    • Seery, L.T.1    Nestor, P.V.2    FitzGerald, G.A.3
  • 52
    • 0028970887 scopus 로고
    • 1.7 A structure of FR-1, a fibroblast growth factor-induced member of the aldo-keto reductase family, complexed with coenzyme and inhibitor
    • Wilson DK, Nakano T, Petrash JM, Quiocho FA. 1.7 A structure of FR-1, a fibroblast growth factor-induced member of the aldo-keto reductase family, complexed with coenzyme and inhibitor. Biochemistry 1995;34:14323-14330.
    • (1995) Biochemistry , vol.34 , pp. 14323-14330
    • Wilson, D.K.1    Nakano, T.2    Petrash, J.M.3    Quiocho, F.A.4
  • 53
    • 0028037576 scopus 로고
    • Aldose reductase catalysis and crystallography. Insights from recent advances in enzyme structure and function
    • Petrash JM, Tarle I, Wilson DK, Quiocho FA. Aldose reductase catalysis and crystallography. Insights from recent advances in enzyme structure and function. Diabetes 1994;8:955-959.
    • (1994) Diabetes , vol.8 , pp. 955-959
    • Petrash, J.M.1    Tarle, I.2    Wilson, D.K.3    Quiocho, F.A.4
  • 54
    • 0031570663 scopus 로고    scopus 로고
    • Steroid recognition and regulation of hormone action: Crystal structure of testosterone and NADP+ bound to 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase
    • Bennett MJ, Albert RH, Jez JM, Ma H, Penning TM, Lewis M. Steroid recognition and regulation of hormone action: crystal structure of testosterone and NADP+ bound to 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase. Structure 1997;5:799-812.
    • (1997) Structure , vol.5 , pp. 799-812
    • Bennett, M.J.1    Albert, R.H.2    Jez, J.M.3    Ma, H.4    Penning, T.M.5    Lewis, M.6
  • 55
    • 0035964182 scopus 로고    scopus 로고
    • Crystal structure of human type III 3alpha-hydroxysteroid dehydrogenase/bile acid binding protein complexed with NADP(+) and ursodeoxycholate
    • Jin Y, Stayrook SE, Albert RH, Palackal NT, Penning TM, Lewis M. Crystal structure of human type III 3alpha-hydroxysteroid dehydrogenase/bile acid binding protein complexed with NADP(+) and ursodeoxycholate. Biochemistry 2001;40:10161-10168.
    • (2001) Biochemistry , vol.40 , pp. 10161-10168
    • Jin, Y.1    Stayrook, S.E.2    Albert, R.H.3    Palackal, N.T.4    Penning, T.M.5    Lewis, M.6
  • 56
    • 0022531009 scopus 로고
    • Cytosolic bile acid binding protein in rat liver: Radioimmunoassay, molecular forms, developmental characteristics and organ distribution
    • Stolz A, Sugiyama Y, Kuhlenkamp J, Osadchey B, Yamada T, Belknap W, Balistreri W, Kaplowitz N. Cytosolic bile acid binding protein in rat liver: Radioimmunoassay, molecular forms, developmental characteristics and organ distribution. Hepatology 1986;6:433-439.
    • (1986) Hepatology , vol.6 , pp. 433-439
    • Stolz, A.1    Sugiyama, Y.2    Kuhlenkamp, J.3    Osadchey, B.4    Yamada, T.5    Belknap, W.6    Balistreri, W.7    Kaplowitz, N.8
  • 57
    • 0022479074 scopus 로고
    • Comparison of the affinities of newly identified human bile acid binder and cationic glutathione S-transferase for bile acids
    • Takikawa H, Stolz A, Sugimoto M, Sugiyama Y, Kaplowitz N. Comparison of the affinities of newly identified human bile acid binder and cationic glutathione S-transferase for bile acids. J Lipid Res 1986;27:652-657.
    • (1986) J Lipid Res , vol.27 , pp. 652-657
    • Takikawa, H.1    Stolz, A.2    Sugimoto, M.3    Sugiyama, Y.4    Kaplowitz, N.5
  • 58
    • 0025071722 scopus 로고
    • Relationship between the newly identified bile acid binder and bile acid oxidoreductases in human liver
    • Takikawa H, Stolz A, Sugiyama Y, Yoshida H, Yamanaka M, Kaplowitz N. Relationship between the newly identified bile acid binder and bile acid oxidoreductases in human liver. J Biol Chem 1990;265:2132-2136.
    • (1990) J Biol Chem , vol.265 , pp. 2132-2136
    • Takikawa, H.1    Stolz, A.2    Sugiyama, Y.3    Yoshida, H.4    Yamanaka, M.5    Kaplowitz, N.6
  • 59
    • 0029953793 scopus 로고    scopus 로고
    • Regulation of steroid glucuronosyltransferase activities and transcripts by androgen in the human prostatic cancer LNCaP cell line
    • Guillemette C, Hum DW, Belanger A. Regulation of steroid glucuronosyltransferase activities and transcripts by androgen in the human prostatic cancer LNCaP cell line. Endocrinology 1996;137:2872-2879.
    • (1996) Endocrinology , vol.137 , pp. 2872-2879
    • Guillemette, C.1    Hum, D.W.2    Belanger, A.3
  • 60
    • 0033057937 scopus 로고    scopus 로고
    • Immunocytochemical localization of type 5 17beta-hydroxysteroid dehydrogenase in human reproductive tissues
    • Pelletier G, Luu-The V, Tetu B, Labrie F. Immunocytochemical localization of type 5 17beta-hydroxysteroid dehydrogenase in human reproductive tissues. J Histochem Cytochem 1999;47:731-738.
    • (1999) J Histochem Cytochem , vol.47 , pp. 731-738
    • Pelletier, G.1    Luu-The, V.2    Tetu, B.3    Labrie, F.4
  • 64
    • 0032862564 scopus 로고    scopus 로고
    • Somatic mutations at the SRD5A2 locus encoding prostatic steroid 5alpha-reductase during prostate cancer progression
    • Akalu A, Dlmajian DA, Highshaw RA, Nichols PW, Reichardt JK. Somatic mutations at the SRD5A2 locus encoding prostatic steroid 5alpha-reductase during prostate cancer progression. Journal of Urology 1999;161:1355-1358.
    • (1999) Journal of Urology , vol.161 , pp. 1355-1358
    • Akalu, A.1    Dlmajian, D.A.2    Highshaw, R.A.3    Nichols, P.W.4    Reichardt, J.K.5
  • 65
    • 0035341589 scopus 로고    scopus 로고
    • Identification of differentially expressed genes in organ-confined prostate cancer by gene expression array
    • Chetcuti A, Margan S, Mann S, Russell P, Handelsman D, Rogers J, Dong Q. Identification of differentially expressed genes in organ-confined prostate cancer by gene expression array. Prostate 2001;47:132-140.
    • (2001) Prostate , vol.47 , pp. 132-140
    • Chetcuti, A.1    Margan, S.2    Mann, S.3    Russell, P.4    Handelsman, D.5    Rogers, J.6    Dong, Q.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.