메뉴 건너뛰기




Volumn 437, Issue 1, 2011, Pages 53-61

Stereospecific reduction of 5β-reduced steroids by human ketosteroid reductases of the AKR (aldo-keto reductase) superfamily: Role of AKR1C1-AKR1C4 in the metabolism of testosterone and progesterone via the 5β-reductase pathway

Author keywords

Dihydrosteroid; Hydroxysteroid dehydrogenases; Liquid chromatography MS (LC MS); Steroid metabolism; Tetrahydrosteroid

Indexed keywords

5BETA ANDROSTANOLONE; 5BETA PREGNAN 20ALPHA OL 3 ONE; ALDO KETO REDUCTASE 1C1; ALDO KETO REDUCTASE 1C2; ALDO KETO REDUCTASE 1C3; ALDO KETO REDUCTASE 1C4; OXIDOREDUCTASE; PREGNANEDIONE; PROGESTERONE; STEROID 5BETA REDUCTASE; TESTOSTERONE; UNCLASSIFIED DRUG;

EID: 79958862747     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20101804     Document Type: Article
Times cited : (36)

References (42)
  • 1
    • 77049241343 scopus 로고
    • Biochemistry of the steroid hormones
    • Roberts, S. and Szego, C. M. (1955) Biochemistry of the steroid hormones. Annu. Rev. Biochem. 24, 543-596
    • (1955) Annu. Rev. Biochem. , vol.24 , pp. 543-596
    • Roberts, S.1    Szego, C.M.2
  • 2
    • 0000776123 scopus 로고
    • Enzymatic mechanisms of hormone metabolism. I. Oxidation-reduction of the steroid nucleus
    • Tomkins, G. M. (1956) Enzymatic mechanisms of hormone metabolism. I. Oxidation-reduction of the steroid nucleus. Recent Prog. Horm. Res. 12, 125-133
    • (1956) Recent Prog. Horm. Res. , vol.12 , pp. 125-133
    • Tomkins, G.M.1
  • 3
    • 0028173882 scopus 로고
    • Steroid 5α-reductase: Two genes/two enzymes
    • Russell, D. W. and Wilson, J. D. (1994) Steroid 5α-reductase: two genes/two enzymes. Annu. Rev. Biochem. 63, 25-61
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 25-61
    • Russell, D.W.1    Wilson, J.D.2
  • 4
    • 1642305724 scopus 로고    scopus 로고
    • Human cytosolic 3α-hydroxysteroid dehydrogenases of the aldo-keto reductase superfamily display significant 3β-hydroxysteroid dehydrogenase activity: Implications for steroid hormone metabolism and action
    • Steckelbroeck, S., Jin, Y., Gopishetty, S., Oyesanmi, B. and Penning, T. M. (2004) Human cytosolic 3α-hydroxysteroid dehydrogenases of the aldo-keto reductase superfamily display significant 3β-hydroxysteroid dehydrogenase activity: implications for steroid hormone metabolism and action. J. Biol. Chem. 279, 10784-10795
    • (2004) J. Biol. Chem. , vol.279 , pp. 10784-10795
    • Steckelbroeck, S.1    Jin, Y.2    Gopishetty, S.3    Oyesanmi, B.4    Penning, T.M.5
  • 5
    • 0030876351 scopus 로고    scopus 로고
    • A new nomenclature for the aldo-keto reductase superfamily
    • Jez, J. M., Flynn, T. G. and Penning, T. M. (1997) A new nomenclature for the aldo-keto reductase superfamily. Biochem. Pharmacol. 54, 639-647
    • (1997) Biochem. Pharmacol. , vol.54 , pp. 639-647
    • Jez, J.M.1    Flynn, T.G.2    Penning, T.M.3
  • 9
    • 34548567317 scopus 로고    scopus 로고
    • The modulatory role of androgens and progestins in the induction of vasorelaxation in human umbilical artery
    • Perusquia, M., Navarrete, E., Gonzalez, L. and Villalon, C. M. (2007) The modulatory role of androgens and progestins in the induction of vasorelaxation in human umbilical artery. Life Sci. 81, 993-1002
    • (2007) Life Sci. , vol.81 , pp. 993-1002
    • Perusquia, M.1    Navarrete, E.2    Gonzalez, L.3    Villalon, C.M.4
  • 10
    • 33645356692 scopus 로고    scopus 로고
    • A possible role for progesterone metabolites in human parturition
    • Sheehan, P. M. (2006) A possible role for progesterone metabolites in human parturition. Aust. N.Z. J. Obstet. Gynaecol. 46, 159-163
    • (2006) Aust. N.Z. J. Obstet. Gynaecol. , vol.46 , pp. 159-163
    • Sheehan, P.M.1
  • 11
    • 24344456508 scopus 로고    scopus 로고
    • 5β-Dihydroprogesterone and steroid 5β-reductase decrease in association with human parturition at term
    • Sheehan, P. M., Rice, G. E., Moses, E. K. and Brennecke, S. P. (2005) 5β-Dihydroprogesterone and steroid 5β-reductase decrease in association with human parturition at term. Mol. Hum. Reprod. 11, 495-501
    • (2005) Mol. Hum. Reprod. , vol.11 , pp. 495-501
    • Sheehan, P.M.1    Rice, G.E.2    Moses, E.K.3    Brennecke, S.P.4
  • 12
    • 0038013585 scopus 로고    scopus 로고
    • Hydroxysteroid dehydrogenases and pre-receptor regulation of steroid hormone action
    • Penning, T. M. (2003) Hydroxysteroid dehydrogenases and pre-receptor regulation of steroid hormone action. Hum. Reprod. Update 9, 193-205
    • (2003) Hum. Reprod. Update , vol.9 , pp. 193-205
    • Penning, T.M.1
  • 13
    • 0034287545 scopus 로고    scopus 로고
    • Human 3α-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, T. M., Burczynski, M. E., Jez, J. M., Hung, C. F., Lin, H. K., Ma, H., Moore, M., Palackal, N. and Ratnam, K. (2000) Human 3α- 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. 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
  • 14
    • 65649152952 scopus 로고    scopus 로고
    • Human cytosolic hydroxysteroid dehydrogenases of the aldo-ketoreductase superfamily catalyze reduction of conjugated steroids: Implications for phase I and phase II steroid hormone metabolism
    • Jin, Y., Duan, L., Lee, S. H., Kloosterboer, H. J., Blair, I. A. and Penning, T. M. (2009) Human cytosolic hydroxysteroid dehydrogenases of the aldo-ketoreductase superfamily catalyze reduction of conjugated steroids: implications for phase I and phase II steroid hormone metabolism. J. Biol. Chem. 284, 10013-10022
    • (2009) J. Biol. Chem. , vol.284 , pp. 10013-10022
    • Jin, Y.1    Duan, L.2    Lee, S.H.3    Kloosterboer, H.J.4    Blair, I.A.5    Penning, T.M.6
  • 16
    • 0026552524 scopus 로고
    • Structural and functional comparison of two human liver dihydrodiol dehydrogenases associated with 3α-hydroxysteroid dehydrogenase activity
    • Deyashiki, Y., Taniguchi, H., Amano, T., Nakayama, T., Hara, A. and Sawada, H. (1992) Structural and functional comparison of two human liver dihydrodiol dehydrogenases associated with 3α-hydroxysteroid dehydrogenase activity. Biochem. J. 282, 741-746
    • (1992) Biochem. J. , vol.282 , pp. 741-746
    • Deyashiki, Y.1    Taniguchi, H.2    Amano, T.3    Nakayama, T.4    Hara, A.5    Sawada, H.6
  • 17
    • 0037324845 scopus 로고    scopus 로고
    • Selective and potent inhibitors of human 20α-hydroxysteroid dehydrogenase (AKR1C1) that metabolizes neurosteroids derived from progesterone
    • Higaki, Y., Usami, N., Shintani, S., Ishikura, S., El-Kabbani, O. and Hara, A. (2003) Selective and potent inhibitors of human 20α- hydroxysteroid dehydrogenase (AKR1C1) that metabolizes neurosteroids derived from progesterone. Chem.-Biol. Interact. 143-144, 503-513
    • (2003) Chem.-Biol. Interact. , vol.143-144 , pp. 503-513
    • Higaki, Y.1    Usami, N.2    Shintani, S.3    Ishikura, S.4    El-Kabbani, O.5    Hara, A.6
  • 18
    • 0031759084 scopus 로고    scopus 로고
    • Identification of a principal mRNA species for human 3α- hydroxysteroid dehydrogenase isoform (AKR1C3) that exhibits high prostaglandin D2 11-ketoreductase activity
    • Matsuura, K., Shiraishi, H., Hara, A., Sato, K., Deyashiki, Y., Ninomiya, M. and Sakai, S. (1998) Identification of a principal mRNA species for human 3α-hydroxysteroid dehydrogenase isoform (AKR1C3) that exhibits high prostaglandin D2 11-ketoreductase activity. J. Biochem. 124, 940-946
    • (1998) J. Biochem. , vol.124 , pp. 940-946
    • Matsuura, K.1    Shiraishi, H.2    Hara, A.3    Sato, K.4    Deyashiki, Y.5    Ninomiya, M.6    Sakai, S.7
  • 19
    • 0037069355 scopus 로고    scopus 로고
    • Kinetics of allopregnanolone formation catalyzed by human 3α-hydroxysteroid dehydrogenase type III (AKR1C2)
    • Trauger, J. W., Jiang, A., Stearns, B. A. and LoGrasso, P. V. (2002) Kinetics of allopregnanolone formation catalyzed by human 3α- hydroxysteroid dehydrogenase type III (AKR1C2). Biochemistry 41, 13451-13459
    • (2002) Biochemistry , vol.41 , pp. 13451-13459
    • Trauger, J.W.1    Jiang, A.2    Stearns, B.A.3    LoGrasso, P.V.4
  • 20
    • 0036547847 scopus 로고    scopus 로고
    • Substrate specificity of human 3(20)α-hydroxysteroid dehydrogenase for neurosteroids and its inhibition by benzodiazepines
    • Usami, N., Yamamoto, T., Shintani, S., Ishikura, S., Higaki, Y., Katagiri, Y. and Hara, A. (2002) Substrate specificity of human 3(20)α-hydroxysteroid dehydrogenase for neurosteroids and its inhibition by benzodiazepines. Biol. Pharm. Bull. 25, 441-445
    • (2002) Biol. Pharm. Bull. , vol.25 , pp. 441-445
    • Usami, N.1    Yamamoto, T.2    Shintani, S.3    Ishikura, S.4    Higaki, Y.5    Katagiri, Y.6    Hara, A.7
  • 21
    • 0033543173 scopus 로고    scopus 로고
    • Expression and characterization of four recombinant human dihydrodiol dehydrogenase isoforms: Oxidation of trans-7, 8-dihydroxy-7,8-dihydrobenzo
    • Burczynski, M. E., Harvey, R. G. and Penning, T. M. (1999) Expression and characterization of four recombinant human dihydrodiol dehydrogenase isoforms: oxidation of trans-7, 8-dihydroxy-7,8-dihydrobenzo. Biochemistry 38, 10626
    • (1999) Biochemistry , vol.38 , pp. 10626
    • Burczynski, M.E.1    Harvey, R.G.2    Penning, T.M.3
  • 22
    • 0033564742 scopus 로고    scopus 로고
    • The arginine 276 anchor for NADP(H) dictates fluorescence kinetic transients in 3α-hydroxysteroid dehydrogenase, a representative aldo-keto reductase
    • Ratnam, K., Ma, H. and Penning, T. M. (1999) The arginine 276 anchor for NADP(H) dictates fluorescence kinetic transients in 3α-hydroxysteroid dehydrogenase, a representative aldo-keto reductase. Biochemistry 38, 7856-7864
    • (1999) Biochemistry , vol.38 , pp. 7856-7864
    • Ratnam, K.1    Ma, H.2    Penning, T.M.3
  • 24
    • 0028068828 scopus 로고
    • Role of substrate inhibition kinetics in enzymatic chemical oscillations
    • Shen, P. and Larter, R. (1994) Role of substrate inhibition kinetics in enzymatic chemical oscillations. Biophys. J. 67, 1414-1428 (Pubitemid 24304315)
    • (1994) Biophysical Journal , vol.67 , Issue.4 , pp. 1414-1428
    • Shen, P.1    Larter, R.2
  • 25
    • 33646425832 scopus 로고    scopus 로고
    • Molecular docking simulations of steroid substrates into human cytosolic hydroxysteroid dehydrogenases (AKR1C1 and AKR1C2): Insights into positional and stereochemical preferences
    • Jin, Y. and Penning, T. M. (2006) Molecular docking simulations of steroid substrates into human cytosolic hydroxysteroid dehydrogenases (AKR1C1 and AKR1C2): insights into positional and stereochemical preferences. Steroids 71, 380-391
    • (2006) Steroids , vol.71 , pp. 380-391
    • Jin, Y.1    Penning, T.M.2
  • 27
    • 0035951661 scopus 로고    scopus 로고
    • Genomic organization of a human 5β-reductase and its pseudogene and substrate selectivity of the expressed enzyme
    • Charbonneau, A. and The, V. L. (2001) Genomic organization of a human 5β-reductase and its pseudogene and substrate selectivity of the expressed enzyme. Biochim. Biophys. Acta 1517, 228-235
    • (2001) Biochim. Biophys. Acta , vol.1517 , pp. 228-235
    • Charbonneau, A.1    The, V.L.2
  • 28
    • 0033736883 scopus 로고    scopus 로고
    • Determination of progesterone and some of its neuroactive ring A-reduced metabolites in human serum
    • Pearson Murphy, B. E. and Allison, C. M. (2000) Determination of progesterone and some of its neuroactive ring A-reduced metabolites in human serum. J. Steroid Biochem. Mol. Biol. 74, 137-142
    • (2000) J. Steroid Biochem. Mol. Biol. , vol.74 , pp. 137-142
    • Pearson Murphy, B.E.1    Allison, C.M.2
  • 29
    • 33644749351 scopus 로고    scopus 로고
    • Tibolone metabolism in human liver is catalyzed by 3α/3β- hydroxysteroid dehydrogenase activities of the four isoforms of the aldo-keto reductase (AKR)1C subfamily
    • Steckelbroeck, S., Oyesanmi, B., Jin, Y., Lee, S. H., Kloosterboer, H. J. and Penning, T. M. (2006) Tibolone metabolism in human liver is catalyzed by 3α/3β-hydroxysteroid dehydrogenase activities of the four isoforms of the aldo-keto reductase (AKR)1C subfamily. J. Pharmacol. Exp. Ther. 316, 1300-1309
    • (2006) J. Pharmacol. Exp. Ther. , vol.316 , pp. 1300-1309
    • Steckelbroeck, S.1    Oyesanmi, B.2    Jin, Y.3    Lee, S.H.4    Kloosterboer, H.J.5    Penning, T.M.6
  • 30
    • 2642672840 scopus 로고    scopus 로고
    • Inhibition of oxytocin receptor function by direct binding of progesterone
    • Grazzini, E., Guillon, G., Mouillac, B. and Zingg, H. H. (1998) Inhibition of oxytocin receptor function by direct binding of progesterone. Nature 392, 509-512
    • (1998) Nature , vol.392 , pp. 509-512
    • Grazzini, E.1    Guillon, G.2    Mouillac, B.3    Zingg, H.H.4
  • 32
    • 0032881379 scopus 로고    scopus 로고
    • Differential modulation of the γ-aminobutyric acid type C receptor by neuroactive steroids
    • Morris, K. D., Moorefield, C. N. and Amin, J. (1999) Differential modulation of the γ-aminobutyric acid type C receptor by neuroactive steroids. Mol. Pharmacol. 56, 752-759
    • (1999) Mol. Pharmacol. , vol.56 , pp. 752-759
    • Morris, K.D.1    Moorefield, C.N.2    Amin, J.3
  • 36
    • 62649175282 scopus 로고    scopus 로고
    • Metabolism of neuroactive steroids in day-old chick brain
    • Sujkovic, E., Mileusnic, R. and Fry, J. P. (2009) Metabolism of neuroactive steroids in day-old chick brain. J. Neurochem. 109, 348-359
    • (2009) J. Neurochem. , vol.109 , pp. 348-359
    • Sujkovic, E.1    Mileusnic, R.2    Fry, J.P.3
  • 37
    • 33847021147 scopus 로고    scopus 로고
    • Aldo-keto reductases and bioactivation/detoxication
    • Jin, Y. and Penning, T. M. (2007) Aldo-keto reductases and bioactivation/detoxication. Annu. Rev. Pharmacol. Toxicol. 47, 263-292
    • (2007) Annu. Rev. Pharmacol. Toxicol. , vol.47 , pp. 263-292
    • Jin, Y.1    Penning, T.M.2
  • 38
    • 33645893202 scopus 로고    scopus 로고
    • Induction of AKR1C2 by phase II inducers: Identification of a distal consensus antioxidant response element regulated by NRF2
    • Lou, H., Du, S., Ji, Q. and Stolz, A. (2006) Induction of AKR1C2 by phase II inducers: identification of a distal consensus antioxidant response element regulated by NRF2. Mol. Pharmacol. 69, 1662-1672
    • (2006) Mol. Pharmacol. , vol.69 , pp. 1662-1672
    • Lou, H.1    Du, S.2    Ji, Q.3    Stolz, A.4
  • 41
  • 42
    • 0242321131 scopus 로고    scopus 로고
    • Elevated levels of some neuroactive progesterone metabolites, particularly isopregnanolone, in women with chronic fatigue syndrome
    • Murphy, B. E., Abbott, F. V., Allison, C. M., Watts, C. and Ghadirian, A. M. (2004) Elevated levels of some neuroactive progesterone metabolites, particularly isopregnanolone, in women with chronic fatigue syndrome. Psychoneuroendocrinology 29, 245-268
    • (2004) Psychoneuroendocrinology , vol.29 , pp. 245-268
    • Murphy, B.E.1    Abbott, F.V.2    Allison, C.M.3    Watts, C.4    Ghadirian, A.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.