메뉴 건너뛰기




Volumn 151, Issue 4, 2010, Pages 1677-1684

Human cytochrome P450c17: Single step purification and phosphorylation of serine 258 by protein kinase A

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC ACID; CYCLIC AMP DEPENDENT PROTEIN KINASE; CYTOCHROME P450C17; GLUTAMIC ACID; HYDROLASE; LYASE; NICKEL; OXYGENASE; SERINE; SERINE 258; UNCLASSIFIED DRUG;

EID: 77950233252     PISSN: 00137227     EISSN: 00137227     Source Type: Journal    
DOI: 10.1210/en.2009-1247     Document Type: Article
Times cited : (28)

References (47)
  • 1
    • 0019874673 scopus 로고
    • Microsomal cytochrome P450 from neonatal pig testis: Two enzymatic activities (17α-hydroxylase and C17,20-lyase) associated with one protein
    • Nakajin S, Shively JE, Yuan PM, Hall PF 1981 Microsomal cytochrome P450 from neonatal pig testis: two enzymatic activities (17α-hydroxylase and C17,20-lyase) associated with one protein. Biochemistry 20:4037-4042
    • (1981) Biochemistry , vol.20 , pp. 4037-4042
    • Nakajin, S.1    Shively, J.E.2    Yuan, P.M.3    Hall, P.F.4
  • 4
    • 0012293592 scopus 로고
    • Cytochrome P450c17 (steroid 17α-hydroxylase/17,20 lyase): Cloning of human adrenal and testis cDNAs indicates the same gene is expressed in both tissues
    • Chung BC, Picado-Leonard J, Haniu M, Bienkowski M, Hall PF, Shively JE, Miller WL 1987 Cytochrome P450c17 (steroid 17α-hydroxylase/17,20 lyase): cloning of human adrenal and testis cDNAs indicates the same gene is expressed in both tissues. Proc Natl Acad Sci USA 84:407-411
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 407-411
    • Chung, B.C.1    Picado-Leonard, J.2    Haniu, M.3    Bienkowski, M.4    Hall, P.F.5    Shively, J.E.6    Miller, W.L.7
  • 5
    • 0023550055 scopus 로고
    • Cloning and sequence of the human gene encoding P450c17 (steroid 17α-hydroxylase/17,20 lyase): Similarity to the gene for P450c21
    • Picado-Leonard J, Miller WL 1987 Cloning and sequence of the human gene encoding P450c17 (steroid 17α-hydroxylase/17,20 lyase): similarity to the gene for P450c21. DNA 6:439-448
    • (1987) DNA , vol.6 , pp. 439-448
    • Picado-Leonard, J.1    Miller, W.L.2
  • 6
    • 0022578632 scopus 로고
    • Hormonal regulation of P450scc (20,22-desmolase) and P450c17 (17α-hydroxylase/17,20-lyase) in cultured human granulosa cells
    • Voutilainen R, Tapanainen J, Chung BC, Matteson KJ, Miller WL 1986 Hormonal regulation of P450scc (20,22-desmolase) and P450c17 (17α-hydroxylase/17,20-lyase) in cultured human granulosa cells. J Clin Endocrinol Metab 63:202-207
    • (1986) J Clin Endocrinol Metab , vol.63 , pp. 202-207
    • Voutilainen, R.1    Tapanainen, J.2    Chung, B.C.3    Matteson, K.J.4    Miller, W.L.5
  • 7
    • 0028786656 scopus 로고
    • Serine phosphorylation of human P450c17 increases 17,20 lyase activity: Implications for adrenarche and for the polycystic ovary syndrome
    • Zhang LH, Rodriguez H, Ohno S, Miller WL 1995 Serine phosphorylation of human P450c17 increases 17,20 lyase activity: Implications for adrenarche and for the polycystic ovary syndrome. Proc Natl Acad Sci USA 92:10619-10623
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 10619-10623
    • Zhang, L.H.1    Rodriguez, H.2    Ohno, S.3    Miller, W.L.4
  • 8
    • 0037474198 scopus 로고    scopus 로고
    • Protein phosphatase 2A and phosphoprotein SET regulate androgen production by P450c17
    • Pandey AV, Mellon SH, Miller WL 2003 Protein phosphatase 2A and phosphoprotein SET regulate androgen production by P450c17. J Biol Chem 278:2837-2844
    • (2003) J Biol Chem , vol.278 , pp. 2837-2844
    • Pandey, A.V.1    Mellon, S.H.2    Miller, W.L.3
  • 9
    • 17144426051 scopus 로고    scopus 로고
    • 5 and by serine phosphorylation of P450c17
    • 5 and by serine phosphorylation of P450c17. J Biol Chem 280:13265-13271
    • (2005) J Biol Chem , vol.280 , pp. 13265-13271
    • Pandey, A.V.1    Miller, W.L.2
  • 10
    • 42449129236 scopus 로고    scopus 로고
    • Pathways leading to the phosphorylation of P450c17 and to the post-translational regulation of androgen biosynthesis
    • Tee MK, Dong Q, Miller WL 2008 Pathways leading to the phosphorylation of P450c17 and to the post-translational regulation of androgen biosynthesis. Endocrinology 149:2667-2677
    • (2008) Endocrinology , vol.149 , pp. 2667-2677
    • Tee, M.K.1    Dong, Q.2    Miller, W.L.3
  • 11
    • 0027198401 scopus 로고
    • Expression and purification of functional human 17α-hydroxylase/ 17,20 lyase (P450c17) in Escherichia coli
    • Imai T, Globerman H, Gertner JM,KagawaN, WatermanMR1993 Expression and purification of functional human 17α-hydroxylase/ 17,20 lyase (P450c17) in Escherichia coli. J Biol Chem 268:19681-19689
    • (1993) J Biol Chem , vol.268 , pp. 19681-19689
    • Imai, T.1    Globerman, H.2    Gertner, J.M.3    Kagawa, N.4    Waterman, M.R.5
  • 13
    • 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
    • (1998) J Biol Chem , vol.273 , pp. 3158-3165
    • Auchus, R.J.1    Lee, T.C.2    Miller, W.L.3
  • 14
    • 0035450155 scopus 로고    scopus 로고
    • N-terminal deletions and Histag fusions dramatically affect expression of cytochrome P450 2C2 in bacteria
    • Doray B, Chen CD, Kemper B 2001 N-terminal deletions and Histag fusions dramatically affect expression of cytochrome P450 2C2 in bacteria. Arch Biochem Biophys 393:143-153
    • (2001) Arch Biochem Biophys , vol.393 , pp. 143-153
    • Doray, B.1    Chen, C.D.2    Kemper, B.3
  • 15
    • 0036348808 scopus 로고    scopus 로고
    • Membrane reconstitution of recombinant guinea pig cytochrome P45017α and the effects of site-directed mutagenesis on androgen formation
    • Owaki A, Takamasa A, Yamazaki T, Kominami S 2002 Membrane reconstitution of recombinant guinea pig cytochrome P45017α and the effects of site-directed mutagenesis on androgen formation. J Steroid Biochem Mol Biol 81:255-262
    • (2002) J Steroid Biochem Mol Biol , vol.81 , pp. 255-262
    • Owaki, A.1    Takamasa, A.2    Yamazaki, T.3    Kominami, S.4
  • 16
    • 0012697772 scopus 로고    scopus 로고
    • Human CYP1A1 allelic variants: Baculovirus expression and purification, hydrodynamic, spectral, and catalytical properties and their potency in the formation of all-trans-retinoic acid
    • Chernogolov A, Behlke J, Schunck WH, Roots I, Schwarz D 2003 Human CYP1A1 allelic variants: baculovirus expression and purification, hydrodynamic, spectral, and catalytical properties and their potency in the formation of all-trans-retinoic acid. Protein Expr Purif 28:259-269
    • (2003) Protein Expr Purif , vol.28 , pp. 259-269
    • Chernogolov, A.1    Behlke, J.2    Schunck, W.H.3    Roots, I.4    Schwarz, D.5
  • 17
    • 0642369727 scopus 로고    scopus 로고
    • Molecular cloning and heterologous expression in E. coli of cytochrome P45017α. Comparison of structural and functional properties of substrate-specific cytochromes P450 from different species
    • Mosc
    • Gilep AA, Estabrook RW, Usanov SA 2003 Molecular cloning and heterologous expression in E. coli of cytochrome P45017α. Comparison of structural and functional properties of substrate-specific cytochromes P450 from different species. Biochemistry (Mosc) 68: 86-98
    • (2003) Biochemistry , vol.68 , pp. 86-98
    • Gilep, A.A.1    Estabrook, R.W.2    Usanov, S.A.3
  • 18
    • 3042683304 scopus 로고    scopus 로고
    • Expression of human cytochrome P450 46A1 in Escherichia coli: Effects of N- And C-terminal modifications
    • Mast N, Andersson U, Nakayama K, Bjorkhem I, Pikuleva IA 2004 Expression of human cytochrome P450 46A1 in Escherichia coli: effects of N- and C-terminal modifications. Arch Biochem Biophys 428:99-108
    • (2004) Arch Biochem Biophys , vol.428 , pp. 99-108
    • Mast, N.1    Andersson, U.2    Nakayama, K.3    Bjorkhem, I.4    Pikuleva, I.A.5
  • 19
    • 33745173496 scopus 로고    scopus 로고
    • Purification of cytochromes P450: Products of bacterial recombinant expression systems
    • Guengerich FP, MartinMV2006 Purification of cytochromes P450: products of bacterial recombinant expression systems. Methods Mol Biol 320:31-37
    • (2006) Methods Mol Biol , vol.320 , pp. 31-37
    • Guengerich, F.P.1    Martin, M.V.2
  • 20
    • 68349152778 scopus 로고    scopus 로고
    • Functional expression of N-terminally tagged membrane bound cytochrome P450
    • Hamann T, Laursen T, Møller BL 2009 Functional expression of N-terminally tagged membrane bound cytochrome P450. Protein Expr Purif 68:18-21
    • (2009) Protein Expr Purif , vol.68 , pp. 18-21
    • Hamann, T.1    Laursen, T.2    Møller, B.L.3
  • 21
    • 74749103579 scopus 로고    scopus 로고
    • Effects of histidine-tag on recombinant human cytochrome P450 3A5 catalytic activity in reconstitution systems
    • Emoto C, Murayama N, Wakiya S, Yamazaki H 2009 Effects of histidine-tag on recombinant human cytochrome P450 3A5 catalytic activity in reconstitution systems. Drug Metab Lett 3:207-211
    • (2009) Drug Metab Lett , vol.3 , pp. 207-211
    • Emoto, C.1    Murayama, N.2    Wakiya, S.3    Yamazaki, H.4
  • 22
    • 0031252385 scopus 로고    scopus 로고
    • The genetic and functional basis of isolated 17,20 lyase deficiency
    • Geller DH, Auchus RJ, Mendonça BB, MillerWL1997 The genetic and functional basis of isolated 17,20 lyase deficiency. Nat Genet 17:201-205
    • (1997) Nat Genet , vol.17 , pp. 201-205
    • Geller, D.H.1    Auchus, R.J.2    Mendonça, B.B.3    Miller, W.L.4
  • 23
    • 0032893922 scopus 로고    scopus 로고
    • 5
    • Geller DH, Auchus RJ, Miller WL 1999 P450c17 mutations R347H and R358Q selectively disrupt 17,20-lyase activity by disrupting interactions with P450 oxidoreductase and cytochrome b5. Mol Endocrinol 13:167-175
    • (1999) Mol Endocrinol , vol.13 , pp. 167-175
    • Geller, D.H.1    Auchus, R.J.2    Miller, W.L.3
  • 24
    • 1542782363 scopus 로고    scopus 로고
    • CYP17 mutation E305G causes isolated 17,20 lyase deficiency by selectively altering substrate binding
    • Sherbet DP, Tiosano D, Kwist KM, Hochberg Z, Auchus RJ 2003 CYP17 mutation E305G causes isolated 17,20 lyase deficiency by selectively altering substrate binding. J Biol Chem 278:48563-48569
    • (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
  • 25
    • 31044440024 scopus 로고    scopus 로고
    • Human cytochrome b5 requires residues E48 and E49 to stimulate the 17,20-lyase activity of cytochrome P450c17
    • Naffin-Olivos JL, Auchus RJ 2006 Human cytochrome b5 requires residues E48 and E49 to stimulate the 17,20-lyase activity of cytochrome P450c17. Biochemistry 45:755-762
    • (2006) Biochemistry , vol.45 , pp. 755-762
    • Naffin-Olivos, J.L.1    Auchus, R.J.2
  • 26
    • 0032479307 scopus 로고    scopus 로고
    • Identification of the binding site on cytochrome P450 2B4 for cytochrome b5 and cytochrome P450 reductase
    • Bridges A, Gruenke L, Chang YT, Vakser IA, Loew G, Waskell L 1998 Identification of the binding site on cytochrome P450 2B4 for cytochrome b5 and cytochrome P450 reductase. J Biol Chem 273: 17036-17049
    • (1998) J Biol Chem , vol.273 , pp. 17036-17049
    • Bridges, A.1    Gruenke, L.2    Chang, Y.T.3    Vakser, I.A.4    Loew, G.5    Waskell, L.6
  • 27
    • 0030972807 scopus 로고    scopus 로고
    • Transcriptional regulation by cyclic AMP
    • Montminy MR 1997 Transcriptional regulation by cyclic AMP. Annu Rev Biochem 66:807-822
    • (1997) Annu Rev Biochem , vol.66 , pp. 807-822
    • Montminy, M.R.1
  • 28
    • 0033346398 scopus 로고    scopus 로고
    • Molecular modeling ofhumanP450c17 (17α-hydroxylase/17,20-lyase): Insights into reaction mechanisms and effects of mutations
    • Auchus RJ, MillerWL 1999 Molecular modeling ofhumanP450c17 (17α-hydroxylase/17,20-lyase): Insights into reaction mechanisms and effects of mutations. Mol Endocrinol 13:1169-1182
    • (1999) Mol Endocrinol , vol.13 , pp. 1169-1182
    • Auchus, R.J.1    Miller, W.L.2
  • 30
    • 33645843055 scopus 로고    scopus 로고
    • Mutagenesis of putative serine-threonine phosphorylation sites proximal to Arg255 of human cytochrome P450c17 does not selectively promote its 17,20 lyase activity
    • Souter I, Munir I, Mallick P, Weitsman SR, Geller DH, Magoffin DA 2006 Mutagenesis of putative serine-threonine phosphorylation sites proximal to Arg255 of human cytochrome P450c17 does not selectively promote its 17,20 lyase activity. Ferti Steril 85(Suppl 1):1290-1299
    • (2006) Ferti Steril , vol.85 , Issue.SUPPL. 1 , pp. 1290-1299
    • Souter, I.1    Munir, I.2    Mallick, P.3    Weitsman, S.R.4    Geller, D.H.5    Magoffin, D.A.6
  • 32
    • 0035032081 scopus 로고    scopus 로고
    • The genetics, pathophysiology, and management of human deficiencies of P450c17
    • vii
    • Auchus RJ 2001 The genetics, pathophysiology, and management of human deficiencies of P450c17. Endocrinol Metab Clin North Am 30:101-119, vii
    • (2001) Endocrinol Metab Clin North Am , vol.30 , pp. 101-119
    • Auchus, R.J.1
  • 33
    • 0019450470 scopus 로고
    • The developmental changes in plasma adrenal androgens during infancy and adrenarche are associated with changing activities of adrenal microsomal 17-hydroxylase and 17,20 desmolase
    • Schiebinger RJ, Albertson BD, Cassorla FG, Bowyer DW, Geelhoed GW, Cutler Jr GB, Loriaux DL 1981 The developmental changes in plasma adrenal androgens during infancy and adrenarche are associated with changing activities of adrenal microsomal 17-hydroxylase and 17,20 desmolase. J Clin Invest 67:1177-1182
    • (1981) J Clin Invest , vol.67 , pp. 1177-1182
    • Schiebinger, R.J.1    Albertson, B.D.2    Cassorla, F.G.3    Bowyer, D.W.4    Geelhoed, G.W.5    Cutler Jr., G.B.6    Loriaux, D.L.7
  • 34
    • 0022537568 scopus 로고
    • Regulation of the activities of 17α-hydroxylase and 17,20-desmolase in the human adrenal cortex: Kinetic analysis and inhibition by endogenous steroids
    • Couch RM, Muller J, Winter JSD 1986 Regulation of the activities of 17α-hydroxylase and 17,20-desmolase in the human adrenal cortex: kinetic analysis and inhibition by endogenous steroids. J Clin Endocrinol Metab 63:613-618
    • (1986) J Clin Endocrinol Metab , vol.63 , pp. 613-618
    • Couch, R.M.1    Muller, J.2    Winter, J.S.D.3
  • 35
    • 0036893558 scopus 로고    scopus 로고
    • Molecular evolution of adrenarche: Structural and functional analysis of P450c17 from four primate species
    • Arlt W, Martens JW, Song M, Wang JT, Auchus RJ, Miller WL 2002 Molecular evolution of adrenarche: structural and functional analysis of P450c17 from four primate species. Endocrinology 143:4665-4672
    • (2002) Endocrinology , vol.143 , pp. 4665-4672
    • Arlt, W.1    Martens, J.W.2    Song, M.3    Wang, J.T.4    Auchus, R.J.5    Miller, W.L.6
  • 36
    • 63849311167 scopus 로고    scopus 로고
    • The developmental increase in adrenocortical 17,20-lyase activity (biochemical adrenarche) is driven primarily by increasing cytochrome b5 in neonatal rhesus macaques
    • Nguyen AD, Corbin CJ, Pattison JC, Bird IM, Conley AJ 2009 The developmental increase in adrenocortical 17,20-lyase activity (biochemical adrenarche) is driven primarily by increasing cytochrome b5 in neonatal rhesus macaques. Endocrinology 150:1748-1756
    • (2009) Endocrinology , vol.150 , pp. 1748-1756
    • Nguyen, A.D.1    Corbin, C.J.2    Pattison, J.C.3    Bird, I.M.4    Conley, A.J.5
  • 37
    • 1542327554 scopus 로고    scopus 로고
    • Increased cytochrome P450 17α-hydroxylase promoter function in theca cells isolated from patients with polycystic ovary syndrome involves nuclear factor-1
    • Wickenheisser JK, Nelson-DeGrave VL, Quinn PG, McAllister JM 2004 Increased cytochrome P450 17α-hydroxylase promoter function in theca cells isolated from patients with polycystic ovary syndrome involves nuclear factor-1. Mol Endocrinol 18:588-605
    • (2004) Mol Endocrinol , vol.18 , pp. 588-605
    • Wickenheisser, J.K.1    Nelson-DeGrave, V.L.2    Quinn, P.G.3    McAllister, J.M.4
  • 38
    • 15944407338 scopus 로고    scopus 로고
    • Dysregulation of cytochrome P450 17α-hydroxylase messenger ribonucleic acid stability in theca cells isolated from women with polycystic ovary syndrome
    • Wickenheisser JK, Nelson-Degrave VL, McAllister JM 2005 Dysregulation of cytochrome P450 17α-hydroxylase messenger ribonucleic acid stability in theca cells isolated from women with polycystic ovary syndrome. J Clin Endocrinol Metab 90:1720-1727
    • (2005) J Clin Endocrinol Metab , vol.90 , pp. 1720-1727
    • Wickenheisser, J.K.1    Nelson-Degrave, V.L.2    McAllister, J.M.3
  • 39
    • 0030892697 scopus 로고    scopus 로고
    • Characterization of the adrenal cytochrome P450c17 in the hamster, a small animal model for the study of adrenal dehydroepiandrosterone biosynthesis
    • Cloutier M, Fleury A, Courtemanche J, Ducharme L, Mason JI, LeHoux JG 1997 Characterization of the adrenal cytochrome P450c17 in the hamster, a small animal model for the study of adrenal dehydroepiandrosterone biosynthesis.DNACell Biol 16: 357-368
    • (1997) DNA Cell Biol , vol.16 , pp. 357-368
    • Cloutier, M.1    Fleury, A.2    Courtemanche, J.3    Ducharme, L.4    Mason, J.I.5    Lehoux, J.G.6
  • 40
    • 0033514376 scopus 로고    scopus 로고
    • Biochemical differences between rat and human cytochrome P450c17 support the different steroidogenic needs of these two species
    • Brock BJ, WatermanMR1999 Biochemical differences between rat and human cytochrome P450c17 support the different steroidogenic needs of these two species. Biochemistry 38:1598-1606
    • (1999) Biochemistry , vol.38 , pp. 1598-1606
    • Brock, B.J.1    Waterman, M.R.2
  • 41
    • 0026576703 scopus 로고
    • Rainbow trout cytochrome P450c17 (17α-hydroxylase/17,20 lyase) cDNA cloning, enzymatic properties and temporal pattern of ovarian P450c17 mRNA expression during oogenesis
    • SakaiN,TanakaM,AdachiS, MillerWL,NagahamaY1992Rainbow trout cytochrome P450c17 (17α-hydroxylase/17,20 lyase) cDNA cloning, enzymatic properties and temporal pattern of ovarian P450c17 mRNA expression during oogenesis. FEBS Lett 301:60-64
    • (1992) FEBS Lett , vol.301 , pp. 60-64
    • Sakai, N.1    Tanaka, M.2    Adachi, S.3    Miller, W.L.4    Nagahama, Y.5
  • 42
    • 0028575930 scopus 로고
    • Molecular cloning and expression of guinea pig cytochrome P450c17 cDNA (steroid 17α-hydroxylase/17,20 lyase): Tissue distribution, regulation, and substrate specificity of the expressed enzyme
    • Tremblay Y, Fleury A, Beaudoin C, Valée M, Bélanger A 1994 Molecular cloning and expression of guinea pig cytochrome P450c17 cDNA (steroid 17α-hydroxylase/17,20 lyase): tissue distribution, regulation, and substrate specificity of the expressed enzyme. DNA Cell Biol 13:1199-1212
    • (1994) DNA Cell Biol , vol.13 , pp. 1199-1212
    • Tremblay, Y.1    Fleury, A.2    Beaudoin, C.3    Valée, M.4    Bélanger, A.5
  • 44
    • 0022997597 scopus 로고
    • Role of electron transport in the regulation of the lyase activity of C-21 side-chain cleavage P450 from porcine adrenal and testicular microsomes
    • Yanagibashi K, Hall PF 1986 Role of electron transport in the regulation of the lyase activity of C-21 side-chain cleavage P450 from porcine adrenal and testicular microsomes. J Biol Chem 261:8429-8433
    • (1986) J Biol Chem , vol.261 , pp. 8429-8433
    • Yanagibashi, K.1    Hall, P.F.2
  • 46
    • 18844367746 scopus 로고    scopus 로고
    • Regulation of steroidogenesis by electron transfer
    • Miller WL 2005 Regulation of steroidogenesis by electron transfer. Endocrinology 146:2544-2550
    • (2005) Endocrinology , vol.146 , pp. 2544-2550
    • Miller, W.L.1
  • 47
    • 0028567874 scopus 로고
    • Constitutive activation of Mek1 by mutation of serine phosphorylation sites
    • Huang W, Erickson RL 1994 Constitutive activation of Mek1 by mutation of serine phosphorylation sites. Proc Natl Acad Sci USA 91:8960-8963
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 8960-8963
    • Huang, W.1    Erickson, R.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.