메뉴 건너뛰기




Volumn 145, Issue 4, 2004, Pages 1700-1707

Molten globule structure and steroidogenic activity of N-218 MLN64 in human placental mitochondria

Author keywords

[No Author keywords available]

Indexed keywords

20ALPHA HYDROXYCHOLESTEROL; 8 BROMO CYCLIC AMP; CARRIER PROTEIN; CHOLESTEROL; CHOLESTEROL DERIVATIVE; CYTOCHROME P450; N 218 MLN64 PROTEIN; N 62 STEROIDOGENIC ACUTE REGULATORY PROTEIN; PLACENTA MITOCHONDRION; PLACENTA PROTEIN; PREGNENOLONE; STEROIDOGENIC ACUTE REGULATORY PROTEIN; UNCLASSIFIED DRUG; UREA;

EID: 1642464921     PISSN: 00137227     EISSN: None     Source Type: Journal    
DOI: 10.1210/en.2003-1034     Document Type: Article
Times cited : (54)

References (46)
  • 1
    • 0031794582 scopus 로고    scopus 로고
    • Steroid hormone biosynthesis and actions in the maternofeto-placental unit
    • Miller WL 1998 Steroid hormone biosynthesis and actions in the maternofeto-placental unit. Clin Perinatol 25:799-817
    • (1998) Clin Perinatol , vol.25 , pp. 799-817
    • Miller, W.L.1
  • 2
    • 0028170204 scopus 로고
    • Cytochrome P-450scc activity and substrate supply in human placental trophoblasts
    • Tuckey RC, Kostadinovic Z, Cameron KJ 1994 Cytochrome P-450scc activity and substrate supply in human placental trophoblasts. Mol Cell Endocrinol 105:103-109
    • (1994) Mol Cell Endocrinol , vol.105 , pp. 103-109
    • Tuckey, R.C.1    Kostadinovic, Z.2    Cameron, K.J.3
  • 3
    • 0342618479 scopus 로고    scopus 로고
    • Structure-function relationships of 3β-hydroxysteroid dehydrogenase: Contribution made by the molecular genetics of 3β-hydroxysteroid dehydrogenase deficiency
    • Morel Y, Mébarke F, Rhéaume E, Sanchez R, Forest MG, Simard J 1997 Structure-function relationships of 3β-hydroxysteroid dehydrogenase: contribution made by the molecular genetics of 3β-hydroxysteroid dehydrogenase deficiency. Steroids 62:176-184
    • (1997) Steroids , vol.62 , pp. 176-184
    • Morel, Y.1    Mébarke, F.2    Rhéaume, E.3    Sanchez, R.4    Forest, M.G.5    Simard, J.6
  • 4
    • 0030665210 scopus 로고    scopus 로고
    • Regulation of cytochrome P450 cholesterol side-chain cleavage, 3β-hydroxysteroid dehydrogenase/Δ5-Δ4 isomerase type 1 and estradiol-17 β-hydroxysteroid dehydrogenase mRNA levels by calcium in human choriocarcinoma JEG-3 cells
    • Beaudoin C, Bonenfant M, Tremblay Y 1997 Regulation of cytochrome P450 cholesterol side-chain cleavage, 3β-hydroxysteroid dehydrogenase/Δ5- Δ4 isomerase type 1 and estradiol-17 β-hydroxysteroid dehydrogenase mRNA levels by calcium in human choriocarcinoma JEG-3 cells. Mol Cell Endocrinol 133:63-71
    • (1997) Mol Cell Endocrinol , vol.133 , pp. 63-71
    • Beaudoin, C.1    Bonenfant, M.2    Tremblay, Y.3
  • 5
    • 0030047248 scopus 로고    scopus 로고
    • Regulation of the acute production of steroids in steroidogenic cells
    • Stocco DM, Clark BJ 1996 Regulation of the acute production of steroids in steroidogenic cells. Endocr Rev 17:221-244
    • (1996) Endocr Rev , vol.17 , pp. 221-244
    • Stocco, D.M.1    Clark, B.J.2
  • 6
    • 0033051733 scopus 로고    scopus 로고
    • Molecular pathology and mechanism of action of the steroidogenic acute regulatory protein, StAR
    • Miller WL, Strauss III JF 1999 Molecular pathology and mechanism of action of the steroidogenic acute regulatory protein, StAR. J Steroid Biochem Mol Biol 69:131-141
    • (1999) J Steroid Biochem Mol Biol , vol.69 , pp. 131-141
    • Miller, W.L.1    Strauss III, J.F.2
  • 7
    • 0024384105 scopus 로고
    • Diurnal variation of plasma and saliva oestrogen, progesterone, cortisol and plasma dehydroepiandrosterone sulphate in late pregnancy
    • Darne FJ, McGarrigle HH, Lachelin GC 1989 Diurnal variation of plasma and saliva oestrogen, progesterone, cortisol and plasma dehydroepiandrosterone sulphate in late pregnancy. Eur J Obstet Gynecol Reprod Biol 32:57-66
    • (1989) Eur J Obstet Gynecol Reprod Biol , vol.32 , pp. 57-66
    • Darne, F.J.1    McGarrigle, H.H.2    Lachelin, G.C.3
  • 8
    • 0033642725 scopus 로고    scopus 로고
    • Providing progesterone for pregnancy: Control of cholesterol flux to the side-chain cleavage system
    • Strauss III JF, Christenson LK, Devoto L, Martinez F 2000 Providing progesterone for pregnancy: control of cholesterol flux to the side-chain cleavage system. J Reprod Fertil Suppl 55:3-12
    • (2000) J Reprod Fertil Suppl , vol.55 , pp. 3-12
    • Strauss III, J.F.1    Christenson, L.K.2    Devoto, L.3    Martinez, F.4
  • 9
    • 0035014486 scopus 로고    scopus 로고
    • Oxidized adrenodoxin acts as a competitive inhibitor of cytochrome P450scc in mitochondria from the human placenta
    • Tuckey RC, McKinley AJ, Headlam MJ 2001 Oxidized adrenodoxin acts as a competitive inhibitor of cytochrome P450scc in mitochondria from the human placenta. Eur J Biochem 268:2338-2343
    • (2001) Eur J Biochem , vol.268 , pp. 2338-2343
    • Tuckey, R.C.1    McKinley, A.J.2    Headlam, M.J.3
  • 10
    • 0036348255 scopus 로고    scopus 로고
    • Placental cytochrome P450scc (CYP11A1): Comparison of catalytic properties between conditions of limiting and saturating adrenodoxin reductase
    • Tuckey RC, Headlam MJ 2002 Placental cytochrome P450scc (CYP11A1): comparison of catalytic properties between conditions of limiting and saturating adrenodoxin reductase. J Steroid Biochem Mol Biol 81:153-158
    • (2002) J Steroid Biochem Mol Biol , vol.81 , pp. 153-158
    • Tuckey, R.C.1    Headlam, M.J.2
  • 11
    • 0029030626 scopus 로고
    • Human steroidogenic acute regulatory protein (StAR): Functional activity in COS-1 cells, tissue-specific expression, and mapping of the structural gene to 8p11.2 and an expressed pseudogene to chromosome 13
    • Sugawara T, Holt JA, Driscoll D, Strauss III JF, Lin D, Miller WL, Patterson D, Clancy KP, Hart IM, Clark BJ, Stocco DM 1995 Human steroidogenic acute regulatory protein (StAR): functional activity in COS-1 cells, tissue-specific expression, and mapping of the structural gene to 8p11.2 and an expressed pseudogene to chromosome 13. Proc Natl Acad Sci USA 92:4778-4782
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 4778-4782
    • Sugawara, T.1    Holt, J.A.2    Driscoll, D.3    Strauss III, J.F.4    Lin, D.5    Miller, W.L.6    Patterson, D.7    Kp, C.8    Hart, I.M.9    Clark, B.J.10    Stocco, D.M.11
  • 12
    • 0029855881 scopus 로고    scopus 로고
    • The pathophysiology and genetics of congenital lipoid adrenal hyperplasia
    • Bose HS, Sugawara T, Strauss III JF, Miller WL 1996 The pathophysiology and genetics of congenital lipoid adrenal hyperplasia. N Engl J Med 335:1870-1878
    • (1996) N Engl J Med , vol.335 , pp. 1870-1878
    • Bose, H.S.1    Sugawara, T.2    Strauss III, J.F.3    Miller, W.L.4
  • 14
    • 0034718451 scopus 로고    scopus 로고
    • N-218 MLN64, a protein with StAR-like steroidogenic activity is folded and cleaved similarly to StAR
    • Bose HS, Whittal RM, Huang MC, Baldwin MA, Miller WL 2000 N-218 MLN64, a protein with StAR-like steroidogenic activity is folded and cleaved similarly to StAR. Biochemistry 39:11722-11731
    • (2000) Biochemistry , vol.39 , pp. 11722-11731
    • Bose, H.S.1    Whittal, R.M.2    Huang, M.C.3    Baldwin, M.A.4    Miller, W.L.5
  • 15
    • 0034064138 scopus 로고    scopus 로고
    • Structure and lipid transport mechanism of a StAR-related domain
    • Tsujishita Y, Hurley JH 2000 Structure and lipid transport mechanism of a StAR-related domain. Nat Struct Biol 7:408-414
    • (2000) Nat Struct Biol , vol.7 , pp. 408-414
    • Tsujishita, Y.1    Hurley, J.H.2
  • 16
    • 0037076275 scopus 로고    scopus 로고
    • The cholesterol-regulated StarD4 gene encodes a StAR-related lipid transfer protein with two closely related homologues, StarD5 and StarD6
    • Soccio RE, Adams RM, Romanowski MJ, Sehayek E, Burley SK, Breslow JL 2002 The cholesterol-regulated StarD4 gene encodes a StAR-related lipid transfer protein with two closely related homologues, StarD5 and StarD6. Proc Natl Acad Sci USA 99:6943-6948
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 6943-6948
    • Soccio, R.E.1    Adams, R.M.2    Romanowski, M.J.3    Sehayek, E.4    Burley, S.K.5    Breslow, J.L.6
  • 17
    • 0037076327 scopus 로고    scopus 로고
    • Crystal structure of the Mus musculus cholesterol-regulated START protein 4 (StarD4) containing a StAR-related lipid transfer domain
    • Romanowski MJ, Soccio RE, Breslow JL, Burley SK 2002 Crystal structure of the Mus musculus cholesterol-regulated START protein 4 (StarD4) containing a StAR-related lipid transfer domain. Proc Natl Acad Sci USA 99:6949-6954
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 6949-6954
    • Romanowski, M.J.1    Soccio, R.E.2    Breslow, J.L.3    Burley, S.K.4
  • 21
    • 0037184964 scopus 로고    scopus 로고
    • MENTHO, a MLN64 homologue devoid of the START domain
    • Alpy F, Wendling C, Rio MC, Tomasetto C 2002 MENTHO, a MLN64 homologue devoid of the START domain. J Biol Chem 277:50780-50787
    • (2002) J Biol Chem , vol.277 , pp. 50780-50787
    • Alpy, F.1    Wendling, C.2    Rio, M.C.3    Tomasetto, C.4
  • 22
    • 0030459652 scopus 로고    scopus 로고
    • Steroidogenic acute regulatory protein (StAR) retains activity in the absence of its mitochondrial targeting sequence: Implications for the mechanism of StAR action
    • Arakane F, Sugawara T, Nishino H, Liu Z, Holt JA, Pain D, Stocco DM, Miller WL, Strauss III JF 1996 Steroidogenic acute regulatory protein (StAR) retains activity in the absence of its mitochondrial targeting sequence: implications for the mechanism of StAR action. Proc Natl Acad Sci USA 93:13731-13736
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 13731-13736
    • Arakane, F.1    Sugawara, T.2    Nishino, H.3    Liu, Z.4    Holt, J.A.5    Pain, D.6    Stocco, D.M.7    Miller, W.L.8    Strauss III, J.F.9
  • 23
    • 0037007628 scopus 로고    scopus 로고
    • Rapid regulation of steroidogenesis by mitochondrial protein import
    • Bose HS, Lingappa VR, Miller WL 2002 Rapid regulation of steroidogenesis by mitochondrial protein import. Nature 417:87-91
    • (2002) Nature , vol.417 , pp. 87-91
    • Bose, H.S.1    Lingappa, V.R.2    Miller, W.L.3
  • 24
    • 0242501535 scopus 로고    scopus 로고
    • Contact sites from human placental mitochondria: Characterization and role in progesterone synthesis
    • Uribe A, Strauss III JF, Martinez F 2003 Contact sites from human placental mitochondria: characterization and role in progesterone synthesis. Arch Biochem Biophys 413:172-181
    • (2003) Arch Biochem Biophys , vol.413 , pp. 172-181
    • Uribe, A.1    Strauss III, J.F.2    Martinez, F.3
  • 25
    • 0033594958 scopus 로고    scopus 로고
    • The active form of the steroidogenic acute regulatory protein, StAR, appears to be a molten globule
    • Bose HS, Whittal RM, Baldwin MA, Miller WL 1999 The active form of the steroidogenic acute regulatory protein, StAR, appears to be a molten globule. Proc Natl Acad Sci USA 96:7250-7255
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 7250-7255
    • Bose, H.S.1    Whittal, R.M.2    Baldwin, M.A.3    Miller, W.L.4
  • 26
    • 0032493328 scopus 로고    scopus 로고
    • Incorrect folding of steroidogenic acute regulatory protein (StAR) in congenital lipoid adrenal hyperplasia
    • Bose HS, Baldwin MA, Miller WL 1998 Incorrect folding of steroidogenic acute regulatory protein (StAR) in congenital lipoid adrenal hyperplasia. Biochemistry 37:9768-9775
    • (1998) Biochemistry , vol.37 , pp. 9768-9775
    • Bose, H.S.1    Baldwin, M.A.2    Miller, W.L.3
  • 27
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace CN 1986 Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol 131:266-280
    • (1986) Methods Enzymol , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 28
    • 0037033098 scopus 로고    scopus 로고
    • Transfer of cholesterol between phospholipid vesicles mediated by the steroidogenic acute regulatory protein (StAR)
    • Tuckey RC, Headlam MJ, Bose HS, Miller WL 2002 Transfer of cholesterol between phospholipid vesicles mediated by the steroidogenic acute regulatory protein (StAR). J Biol Chem 277:47123-47128
    • (2002) J Biol Chem , vol.277 , pp. 47123-47128
    • Tuckey, R.C.1    Headlam, M.J.2    Bose, H.S.3    Miller, W.L.4
  • 29
    • 0033565694 scopus 로고    scopus 로고
    • The concentration of adrenodoxin reductase limits cytochrome P450scc activity in the human placenta
    • Tuckey RC, Sadleir J 1999 The concentration of adrenodoxin reductase limits cytochrome P450scc activity in the human placenta. Eur J Biochem 263:319-325
    • (1999) Eur J Biochem , vol.263 , pp. 319-325
    • Tuckey, R.C.1    Sadleir, J.2
  • 30
    • 0016175990 scopus 로고
    • The effect of inhibitors of protein synthesis on cholesterol side-chain cleavage in the mitochondria of luteinized rat ovaries
    • Arthur JR, Boyd GS 1974 The effect of inhibitors of protein synthesis on cholesterol side-chain cleavage in the mitochondria of luteinized rat ovaries. Eur J Biochem 49:117-127
    • (1974) Eur J Biochem , vol.49 , pp. 117-127
    • Arthur, J.R.1    Boyd, G.S.2
  • 31
    • 0036404269 scopus 로고    scopus 로고
    • The effect of glycerol on cytochrome P450scc (CYP11A1) spin state, activity, and hydration
    • Headlam MJ, Tuckey RC 2002 The effect of glycerol on cytochrome P450scc (CYP11A1) spin state, activity, and hydration. Arch Biochem Biophys 407:95-102
    • (2002) Arch Biochem Biophys , vol.407 , pp. 95-102
    • Headlam, M.J.1    Tuckey, R.C.2
  • 32
    • 0027429765 scopus 로고
    • Side-chain specificities of human and bovine cytochromes P-450scc
    • Tuckey RC, Cameron KJ 1993 Side-chain specificities of human and bovine cytochromes P-450scc. Eur J Biochem 217:209-215
    • (1993) Eur J Biochem , vol.217 , pp. 209-215
    • Tuckey, R.C.1    Cameron, K.J.2
  • 34
    • 0025195499 scopus 로고
    • Mechanism of acid-induced folding of proteins
    • Goto Y, Takahashi N, Fink AL 1990 Mechanism of acid-induced folding of proteins. Biochemistry 29:3480-3488
    • (1990) Biochemistry , vol.29 , pp. 3480-3488
    • Goto, Y.1    Takahashi, N.2    Fink, A.L.3
  • 35
    • 0026767451 scopus 로고
    • Cholesterol side-chain cleavage by mitochondria from the human placenta. Studies using hydroxycholesterols as substrates
    • Tuckey RC 1992 Cholesterol side-chain cleavage by mitochondria from the human placenta. Studies using hydroxycholesterols as substrates. J Steroid Biochem Mol Biol 42:883-890
    • (1992) J Steroid Biochem Mol Biol , vol.42 , pp. 883-890
    • Tuckey, R.C.1
  • 36
    • 0015994194 scopus 로고
    • Spectral properties of rat adrenal-mitochondrial cytochrome P-450
    • Jefcoate CR, Simpson ER, Boyd GS 1974 Spectral properties of rat adrenal-mitochondrial cytochrome P-450. Eur J Biochem 42:539-551
    • (1974) Eur J Biochem , vol.42 , pp. 539-551
    • Jefcoate, C.R.1    Simpson, E.R.2    Boyd, G.S.3
  • 37
    • 0020389679 scopus 로고
    • Metabolism of 25-hydroxycholesterol by rat luteal mitochondria and dispersed cells
    • Toaff ME, Schleyer H, Strauss III JF 1982 Metabolism of 25-hydroxycholesterol by rat luteal mitochondria and dispersed cells. Endocrinology 111:1785-1790
    • (1982) Endocrinology , vol.111 , pp. 1785-1790
    • Toaff, M.E.1    Schleyer, H.2    Strauss III, J.F.3
  • 38
    • 0020490382 scopus 로고
    • Cytochrome P-450scc-substrate interactions. Studies of binding and catalytic activity using hydroxycholesterols
    • Lambeth JD, Kitchen SE, Farooqui AA, Tuckey R, Kamin H 1982 Cytochrome P-450scc-substrate interactions. Studies of binding and catalytic activity using hydroxycholesterols. J Biol Chem 257:1876-1884
    • (1982) J Biol Chem , vol.257 , pp. 1876-1884
    • Lambeth, J.D.1    Kitchen, S.E.2    Farooqui, A.A.3    Tuckey, R.4    Kamin, H.5
  • 39
    • 0027315471 scopus 로고
    • Catalytic properties of cytochrome P-450scc purified from the human placenta: Comparison to bovine cytochrome P-450scc
    • Tuckey RC, Cameron KJ 1993 Catalytic properties of cytochrome P-450scc purified from the human placenta: comparison to bovine cytochrome P-450scc. Biochim Biophys Acta 1163:185-194
    • (1993) Biochim Biophys Acta , vol.1163 , pp. 185-194
    • Tuckey, R.C.1    Cameron, K.J.2
  • 40
    • 0027192968 scopus 로고
    • Human placental cholesterol side-chain cleavage: Enzymatic synthesis of (22R)-20α,22-dihydroxycholesterol
    • Tuckey RC, Cameron KJ 1993 Human placental cholesterol side-chain cleavage: enzymatic synthesis of (22R)-20α,22-dihydroxycholesterol. Steroids 58:230-233
    • (1993) Steroids , vol.58 , pp. 230-233
    • Tuckey, R.C.1    Cameron, K.J.2
  • 41
    • 0035907262 scopus 로고    scopus 로고
    • Binding of StAR to synthetic membranes suggests an active molten globule
    • Christinsen K, Bose HS, Harris FM, Miller WL, Bell JD 2001 Binding of StAR to synthetic membranes suggests an active molten globule. J Biol Chem 276:17044-17051
    • (2001) J Biol Chem , vol.276 , pp. 17044-17051
    • Christinsen, K.1    Bose, H.S.2    Harris, F.M.3    Miller, W.L.4    Bell, J.D.5
  • 43
    • 0035010663 scopus 로고    scopus 로고
    • Creation and activity of COS-1 cells stably expressing the F2 fusion of the human cholesterol side chain cleavage enzyme system
    • Huang MC, Miller WL 2001 Creation and activity of COS-1 cells stably expressing the F2 fusion of the human cholesterol side chain cleavage enzyme system. Endocrinology 142:2569-2576
    • (2001) Endocrinology , vol.142 , pp. 2569-2576
    • Huang, M.C.1    Miller, W.L.2
  • 44
    • 0027311918 scopus 로고
    • Construction and function of fusion enzymes of the human cytochrome P450scc system
    • Harikrishna JA, Black SM, Szklarz GD, Miller WL 1993 Construction and function of fusion enzymes of the human cytochrome P450scc system. DNA Cell Biol 12:371-379
    • (1993) DNA Cell Biol , vol.12 , pp. 371-379
    • Harikrishna, J.A.1    Black, S.M.2    Szklarz, G.D.3    Miller, W.L.4
  • 45
    • 0033134704 scopus 로고    scopus 로고
    • Differences in cholesterol incorporation into mitochondria from hepatoma AS-30D and human term placenta
    • Navarrete J, Flores-Herrera O, Uribe A, Martinez F 1999 Differences in cholesterol incorporation into mitochondria from hepatoma AS-30D and human term placenta. Placenta 20:285-291
    • (1999) Placenta , vol.20 , pp. 285-291
    • Navarrete, J.1    Flores-Herrera, O.2    Uribe, A.3    Martinez, F.4
  • 46
    • 0018123170 scopus 로고
    • Cholesterol side-chain cleavage, cytochrome P450, and iron-sulfur protein in human placental mitochondria
    • Simpson ER, Miller DA 1978 Cholesterol side-chain cleavage, cytochrome P450, and iron-sulfur protein in human placental mitochondria. Arch Biochem Biophys 190:800-808
    • (1978) Arch Biochem Biophys , vol.190 , pp. 800-808
    • Simpson, E.R.1    Miller, D.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.