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Volumn 55, Issue 31, 2016, Pages 4356-4365

Cytochrome b5 Activates the 17,20-Lyase Activity of Human Cytochrome P450 17A1 by Increasing the Coupling of NADPH Consumption to Androgen Production

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BIOCHEMISTRY; DISEASES;

EID: 84981250372     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/acs.biochem.6b00532     Document Type: Article
Times cited : (41)

References (47)
  • 1
    • 79951665862 scopus 로고    scopus 로고
    • The molecular biology, biochemistry, and physiology of human steroidogenesis and its disorders
    • Miller, W. L. and Auchus, R. J. (2011) The molecular biology, biochemistry, and physiology of human steroidogenesis and its disorders Endocr. Rev. 32, 81-151 10.1210/er.2010-0013
    • (2011) Endocr. Rev. , vol.32 , pp. 81-151
    • Miller, W.L.1    Auchus, R.J.2
  • 2
    • 0032488666 scopus 로고    scopus 로고
    • 5 augments the 17,20 lyase activity of human P450c17 without direct electron transfer
    • 5 augments the 17,20 lyase activity of human P450c17 without direct electron transfer J. Biol. Chem. 273, 3158-3165 10.1074/jbc.273.6.3158
    • (1998) J. Biol. Chem. , vol.273 , pp. 3158-3165
    • Auchus, R.J.1    Lee, T.C.2    Miller, W.L.3
  • 4
    • 0027313314 scopus 로고
    • Progesterone 16α-hydroxylase activity is catalyzed by human cytochrome P450 17α-hydroxylase
    • Swart, P., Swart, A. C., Waterman, M. R., Estabrook, R. W., and Mason, J. I. (1993) Progesterone 16α-hydroxylase activity is catalyzed by human cytochrome P450 17α-hydroxylase J. Clin. Endocrinol. Metab. 77, 98-102 10.1210/jcem.77.1.8325965
    • (1993) J. Clin. Endocrinol. Metab. , vol.77 , pp. 98-102
    • Swart, P.1    Swart, A.C.2    Waterman, M.R.3    Estabrook, R.W.4    Mason, J.I.5
  • 5
    • 1542782363 scopus 로고    scopus 로고
    • CYP17 mutation E305G causes isolated 17,20-lyase deficiency by selectively altering substrate binding
    • Sherbet, D. P., Tiosano, D., Kwist, K. M., Hochberg, Z., and Auchus, R. J. (2003) CYP17 mutation E305G causes isolated 17,20-lyase deficiency by selectively altering substrate binding J. Biol. Chem. 278, 48563-48569 10.1074/jbc.M307586200
    • (2003) J. Biol. Chem. , vol.278 , pp. 48563-48569
    • Sherbet, D.P.1    Tiosano, D.2    Kwist, K.M.3    Hochberg, Z.4    Auchus, R.J.5
  • 6
    • 0031252385 scopus 로고    scopus 로고
    • The genetic and functional basis of isolated 17,20 lyase deficiency
    • Geller, D. H., Auchus, R. J., Mendonça, B. B., and Miller, W. L. (1997) The genetic and functional basis of isolated 17,20 lyase deficiency Nat. Genet. 17, 201-205 10.1038/ng1097-201
    • (1997) Nat. Genet. , vol.17 , pp. 201-205
    • Geller, D.H.1    Auchus, R.J.2    Mendonça, B.B.3    Miller, W.L.4
  • 7
    • 0036885001 scopus 로고    scopus 로고
    • Differential inhibition of 17α-hydroxylase and 17,20-lyase activities by three novel missense CYP17 mutations identified in patients with P450c17 deficiency
    • Van Den Akker, E. L., Koper, J. W., Boehmer, A. L., Themmen, A. P., Verhoef-Post, M., Timmerman, M. A., Otten, B. J., Drop, S. L., and De Jong, F. H. (2002) Differential inhibition of 17α-hydroxylase and 17,20-lyase activities by three novel missense CYP17 mutations identified in patients with P450c17 deficiency J. Clin. Endocrinol. Metab. 87, 5714-5721 10.1210/jc.2001-011880
    • (2002) J. Clin. Endocrinol. Metab. , vol.87 , pp. 5714-5721
    • Van Den Akker, E.L.1    Koper, J.W.2    Boehmer, A.L.3    Themmen, A.P.4    Verhoef-Post, M.5    Timmerman, M.A.6    Otten, B.J.7    Drop, S.L.8    De Jong, F.H.9
  • 8
    • 84879134376 scopus 로고    scopus 로고
    • Molecular pathways: Inhibiting steroid biosynthesis in prostate cancer
    • Ferraldeschi, R., Sharifi, N., Auchus, R. J., and Attard, G. (2013) Molecular pathways: Inhibiting steroid biosynthesis in prostate cancer Clin. Cancer Res. 19, 3353-3359 10.1158/1078-0432.CCR-12-0931
    • (2013) Clin. Cancer Res. , vol.19 , pp. 3353-3359
    • Ferraldeschi, R.1    Sharifi, N.2    Auchus, R.J.3    Attard, G.4
  • 11
    • 84856774377 scopus 로고    scopus 로고
    • Clinical and biochemical consequences of CYP17A1 inhibition with abiraterone given with and without exogenous glucocorticoids in castrate men with advanced prostate cancer
    • Attard, G., Reid, A. H. M., Auchus, R. J., Hughes, B. A., Cassidy, A. M., Thompson, E., Oommen, N. B., Folkerd, E., Dowsett, M., Arlt, W., and de Bono, J. S. (2012) Clinical and biochemical consequences of CYP17A1 inhibition with abiraterone given with and without exogenous glucocorticoids in castrate men with advanced prostate cancer J. Clin. Endocrinol. Metab. 97, 507-516 10.1210/jc.2011-2189
    • (2012) J. Clin. Endocrinol. Metab. , vol.97 , pp. 507-516
    • Attard, G.1    Reid, A.H.M.2    Auchus, R.J.3    Hughes, B.A.4    Cassidy, A.M.5    Thompson, E.6    Oommen, N.B.7    Folkerd, E.8    Dowsett, M.9    Arlt, W.10    De Bono, J.S.11
  • 12
    • 84856700317 scopus 로고    scopus 로고
    • Human steroid biosynthesis for the oncologist
    • Auchus, M. L. and Auchus, R. J. (2012) Human steroid biosynthesis for the oncologist J. Invest. Med. 60, 495-503 10.2310/JIM.0b013e3182408567
    • (2012) J. Invest. Med. , vol.60 , pp. 495-503
    • Auchus, M.L.1    Auchus, R.J.2
  • 13
    • 84919338396 scopus 로고    scopus 로고
    • Use of prednisone with abiraterone acetate in metastatic castration-resistant prostate cancer
    • Auchus, R. J., Yu, M. K., Nguyen, S., and Mundle, S. D. (2014) Use of prednisone with abiraterone acetate in metastatic castration-resistant prostate cancer Oncologist 19, 1231-1240 10.1634/theoncologist.2014-0167
    • (2014) Oncologist , vol.19 , pp. 1231-1240
    • Auchus, R.J.1    Yu, M.K.2    Nguyen, S.3    Mundle, S.D.4
  • 14
    • 84856477784 scopus 로고    scopus 로고
    • Structures of cytochrome P450 17A1 with prostate cancer drugs abiraterone and TOK-001
    • DeVore, N. M. and Scott, E. E. (2012) Structures of cytochrome P450 17A1 with prostate cancer drugs abiraterone and TOK-001 Nature 482, 116-119 10.1038/nature10743
    • (2012) Nature , vol.482 , pp. 116-119
    • DeVore, N.M.1    Scott, E.E.2
  • 15
    • 84911415985 scopus 로고    scopus 로고
    • Structures of human steroidogenic cytochrome P450 17A1 with substrates
    • Petrunak, E. M., DeVore, N. M., Porubsky, P. R., and Scott, E. E. (2014) Structures of human steroidogenic cytochrome P450 17A1 with substrates J. Biol. Chem. 289, 32952-32964 10.1074/jbc.M114.610998
    • (2014) J. Biol. Chem. , vol.289 , pp. 32952-32964
    • Petrunak, E.M.1    DeVore, N.M.2    Porubsky, P.R.3    Scott, E.E.4
  • 16
    • 84922311088 scopus 로고    scopus 로고
    • Structural and kinetic basis of steroid 17α,20-lyase activity in teleost fish cytochrome P450 17A1 and its absence in cytochrome P450 17A2
    • Pallan, P. S., Nagy, L. D., Lei, L., Gonzalez, E., Kramlinger, V. M., Azumaya, C. M., Wawrzak, Z., Waterman, M. R., Guengerich, F. P., and Egli, M. (2015) Structural and kinetic basis of steroid 17α,20-lyase activity in teleost fish cytochrome P450 17A1 and its absence in cytochrome P450 17A2 J. Biol. Chem. 290, 3248-3268 10.1074/jbc.M114.627265
    • (2015) J. Biol. Chem. , vol.290 , pp. 3248-3268
    • Pallan, P.S.1    Nagy, L.D.2    Lei, L.3    Gonzalez, E.4    Kramlinger, V.M.5    Azumaya, C.M.6    Wawrzak, Z.7    Waterman, M.R.8    Guengerich, F.P.9    Egli, M.10
  • 18
    • 31044440024 scopus 로고    scopus 로고
    • 5 requires residues E48 and E49 to stimulate the 17, 20-lyase activity of cytochrome P450c17
    • 5 requires residues E48 and E49 to stimulate the 17, 20-lyase activity of cytochrome P450c17 Biochemistry 45, 755-762 10.1021/bi051623y
    • (2006) Biochemistry , vol.45 , pp. 755-762
    • Naffin-Olivos, J.L.1    Auchus, R.J.2
  • 21
    • 0033514376 scopus 로고    scopus 로고
    • Biochemical differences between rat and human cytochrome P450c17 support the different steroidogenic needs of these two species
    • Brock, B. J. and Waterman, M. R. (1999) Biochemical differences between rat and human cytochrome P450c17 support the different steroidogenic needs of these two species Biochemistry 38, 1598-1606 10.1021/bi9821059
    • (1999) Biochemistry , vol.38 , pp. 1598-1606
    • Brock, B.J.1    Waterman, M.R.2
  • 22
    • 79959408522 scopus 로고    scopus 로고
    • High-yield expression of a catalytically active membrane-bound protein: Human P450 oxidoreductase
    • Sandee, D. and Miller, W. L. (2011) High-yield expression of a catalytically active membrane-bound protein: human P450 oxidoreductase Endocrinology 152, 2904-2908 10.1210/en.2011-0230
    • (2011) Endocrinology , vol.152 , pp. 2904-2908
    • Sandee, D.1    Miller, W.L.2
  • 25
    • 0019249174 scopus 로고
    • Purification of cytochrome P-450, NADPH-cytochrome P-450 reductase, and epoxide hydratase from a single preparation of rat liver microsomes
    • Guengerich, F. P. and Martin, M. V. (1980) Purification of cytochrome P-450, NADPH-cytochrome P-450 reductase, and epoxide hydratase from a single preparation of rat liver microsomes Arch. Biochem. Biophys. 205, 365-379 10.1016/0003-9861(80)90119-8
    • (1980) Arch. Biochem. Biophys. , vol.205 , pp. 365-379
    • Guengerich, F.P.1    Martin, M.V.2
  • 26
    • 78651165715 scopus 로고
    • The carbon monoxide-binding pigment of liver microsomes
    • Omura, T. and Sato, R. (1964) The carbon monoxide-binding pigment of liver microsomes J. Biol. Chem. 239, 2370-2378
    • (1964) J. Biol. Chem. , vol.239 , pp. 2370-2378
    • Omura, T.1    Sato, R.2
  • 28
    • 84872116423 scopus 로고    scopus 로고
    • 5 on CYP2E1 and CYP2C19 activities requires anionic residues D58 and D65
    • 5 on CYP2E1 and CYP2C19 activities requires anionic residues D58 and D65 Biochemistry 52, 210-220 10.1021/bi301384n
    • (2013) Biochemistry , vol.52 , pp. 210-220
    • Peng, H.M.1    Auchus, R.J.2
  • 29
    • 77950233252 scopus 로고    scopus 로고
    • Human cytochrome P450c17: Single step purification and phosphorylation of serine 258 by protein kinase A
    • Wang, Y. H., Tee, M. K., and Miller, W. L. (2010) Human cytochrome P450c17: single step purification and phosphorylation of serine 258 by protein kinase A Endocrinology 151, 1677-1684 10.1210/en.2009-1247
    • (2010) Endocrinology , vol.151 , pp. 1677-1684
    • Wang, Y.H.1    Tee, M.K.2    Miller, W.L.3
  • 32
    • 0141988883 scopus 로고    scopus 로고
    • Determination of the rate of reduction of oxyferrous cytochrome P450 2B4 by 5-deazariboflavin adenine dinucleotide T491V cytochrome P450 reductase
    • Zhang, H., Gruenke, L., Arscott, D., Shen, A., Kasper, C., Harris, D. L., Glavanovich, M., Johnson, R., and Waskell, L. (2003) Determination of the rate of reduction of oxyferrous cytochrome P450 2B4 by 5-deazariboflavin adenine dinucleotide T491V cytochrome P450 reductase Biochemistry 42, 11594-11603 10.1021/bi034968u
    • (2003) Biochemistry , vol.42 , pp. 11594-11603
    • Zhang, H.1    Gruenke, L.2    Arscott, D.3    Shen, A.4    Kasper, C.5    Harris, D.L.6    Glavanovich, M.7    Johnson, R.8    Waskell, L.9
  • 33
    • 35648963202 scopus 로고    scopus 로고
    • 5 increases the rate of product formation by cytochrome P450 2B4 and competes with cytochrome P450 reductase for a binding site on cytochrome P450 2B4
    • 5 increases the rate of product formation by cytochrome P450 2B4 and competes with cytochrome P450 reductase for a binding site on cytochrome P450 2B4 J. Biol. Chem. 282, 29766-29776 10.1074/jbc.M703845200
    • (2007) J. Biol. Chem. , vol.282 , pp. 29766-29776
    • Zhang, H.1    Im, S.C.2    Waskell, L.3
  • 34
    • 40949144759 scopus 로고    scopus 로고
    • Metabolic evidence for impaired 17α-hydroxylase activity in a kindred bearing the E305G mutation for isolate 17,20-lyase activity
    • Tiosano, D., Knopf, C., Koren, I., Levanon, N., Hartmann, M. F., Hochberg, Z., and Wudy, S. A. (2008) Metabolic evidence for impaired 17α-hydroxylase activity in a kindred bearing the E305G mutation for isolate 17,20-lyase activity Eur. J. Endocrinol. 158, 385-392 10.1530/EJE-07-0712
    • (2008) Eur. J. Endocrinol. , vol.158 , pp. 385-392
    • Tiosano, D.1    Knopf, C.2    Koren, I.3    Levanon, N.4    Hartmann, M.F.5    Hochberg, Z.6    Wudy, S.A.7
  • 44
    • 24744459452 scopus 로고    scopus 로고
    • Crystallographic study on the dioxygen complex of wild-type and mutant cytochrome P450cam. Implications for the dioxygen activation mechanism
    • Nagano, S. and Poulos, T. L. (2005) Crystallographic study on the dioxygen complex of wild-type and mutant cytochrome P450cam. Implications for the dioxygen activation mechanism J. Biol. Chem. 280, 31659-31663 10.1074/jbc.M505261200
    • (2005) J. Biol. Chem. , vol.280 , pp. 31659-31663
    • Nagano, S.1    Poulos, T.L.2
  • 47
    • 3042553224 scopus 로고    scopus 로고
    • Structure of mammalian cytochrome P450 2B4 complexed with 4-(4-chlorophenyl)imidazole at 1.9-Å resolution: Insight into the range of P450 conformations and the coordination of redox partner binding
    • Scott, E. E., White, M. A., He, Y. A., Johnson, E. F., Stout, C. D., and Halpert, J. R. (2004) Structure of mammalian cytochrome P450 2B4 complexed with 4-(4-chlorophenyl)imidazole at 1.9-Å resolution: insight into the range of P450 conformations and the coordination of redox partner binding J. Biol. Chem. 279, 27294-27301 10.1074/jbc.M403349200
    • (2004) J. Biol. Chem. , vol.279 , pp. 27294-27301
    • Scott, E.E.1    White, M.A.2    He, Y.A.3    Johnson, E.F.4    Stout, C.D.5    Halpert, J.R.6


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