메뉴 건너뛰기




Volumn 16, Issue , 1996, Pages 443-470

Molecular biology of mineralocorticoid metabolism

Author keywords

aldosterone; hypertension; salt; steroids

Indexed keywords

11BETA HYDROXYSTEROID DEHYDROGENASE; 3(OR 17)BETA HYDROXYSTEROID DEHYDROGENASE; CORTISONE; GLUCOCORTICOID RECEPTOR; HYDROCORTISONE; MINERALOCORTICOID; MINERALOCORTICOID RECEPTOR; STEROID 11BETA MONOOXYGENASE; STEROID 17ALPHA MONOOXYGENASE; STEROID 21 MONOOXYGENASE;

EID: 0029799269     PISSN: 01999885     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.nu.16.070196.002303     Document Type: Review
Times cited : (61)

References (130)
  • 1
    • 0029095113 scopus 로고
    • Gene structure and chromosomal localization of the human HSD11K gene encoding the kidney (type 2) isozyme of 11β-hydroxysteroid dehydrogenase
    • Agarwal AK, Rogerson FM, Mune T, White PC. 1995. Gene structure and chromosomal localization of the human HSD11K gene encoding the kidney (type 2) isozyme of 11β-hydroxysteroid dehydrogenase. Genomics 29:195-99
    • (1995) Genomics , vol.29 , pp. 195-199
    • Agarwal, A.K.1    Rogerson, F.M.2    Mune, T.3    White, P.C.4
  • 2
    • 0025611952 scopus 로고
    • Expression of 11β-hydroxysteroid dehydrogenase using recombinant vaccinia virus
    • Agarwal AK, Tusie-Luna M, Monder C, White PC. 1990. Expression of 11β-hydroxysteroid dehydrogenase using recombinant vaccinia virus. Mol. Endocrinol. 4:1827-32
    • (1990) Mol. Endocrinol. , vol.4 , pp. 1827-1832
    • Agarwal, A.K.1    Tusie-Luna, M.2    Monder, C.3    White, P.C.4
  • 4
    • 0026079736 scopus 로고
    • Overexpression and characterization of the human mineralocorticoid receptor
    • Alnemri ES, Maksymowych AB, Robertson NM, Litwach G. 1991. Overexpression and characterization of the human mineralocorticoid receptor. J. Biol. Chem. 266:18072-81
    • (1991) J. Biol. Chem. , vol.266 , pp. 18072-18081
    • Alnemri, E.S.1    Maksymowych, A.B.2    Robertson, N.M.3    Litwach, G.4
  • 5
    • 0023221667 scopus 로고
    • Cloning of human mineralocorticoid receptor DNA: Structural and functional kinship with the glucocorticoid receptor
    • Arriza JL, Weinberger C, Cerelli G, Glaser TM, Handelin BL, et al. 1987. Cloning of human mineralocorticoid receptor DNA: structural and functional kinship with the glucocorticoid receptor. Science 237:268-75
    • (1987) Science , vol.237 , pp. 268-275
    • Arriza, J.L.1    Weinberger, C.2    Cerelli, G.3    Glaser, T.M.4    Handelin, B.L.5
  • 6
    • 0042562091 scopus 로고
    • The endocrinology of hypertension
    • ed. P Felig, JD Baxter, LA Frohman, New York: McGraw-Hill. 3rd ed.
    • Baxter JD, Perloff D, Hsueh W, Biglieri EG. 1995. The endocrinology of hypertension. In Endocrinology and Metabolism, ed. P Felig, JD Baxter, LA Frohman, pp. 749-853. New York: McGraw-Hill. 3rd ed.
    • (1995) Endocrinology and Metabolism , pp. 749-853
    • Baxter, J.D.1    Perloff, D.2    Hsueh, W.3    Biglieri, E.G.4
  • 7
    • 0024545638 scopus 로고
    • Gene regulation by steroid hormones
    • Beato M. 1989. Gene regulation by steroid hormones. Cell 56:335-44
    • (1989) Cell , vol.56 , pp. 335-344
    • Beato, M.1
  • 8
    • 0024949775 scopus 로고
    • Assignment of the human 3β-hydroxysteroid dehydrogenase gene (HSDB3) to the p13 band of chromosome 1
    • Bérubé D, Luu-The V, Lachance Y, Gagne R, Labrie F. 1989. Assignment of the human 3β-hydroxysteroid dehydrogenase gene (HSDB3) to the p13 band of chromosome 1. Cytogenet. Cell. Genet. 52:199-200
    • (1989) Cytogenet. Cell. Genet. , vol.52 , pp. 199-200
    • Bérubé, D.1    Luu-The, V.2    Lachance, Y.3    Gagne, R.4    Labrie, F.5
  • 9
  • 11
    • 0022257349 scopus 로고
    • Elevated 17-hydroxy-progesterone and testosterone in a newborn with 3β-hydroxysteroid dehydrogenase deficiency
    • Cara JF, Moshang T Jr, Bongiovanni AM, Marx BS. 1985. Elevated 17-hydroxy-progesterone and testosterone in a newborn with 3β-hydroxysteroid dehydrogenase deficiency. N. Engl. J. Med. 313:618-21
    • (1985) N. Engl. J. Med. , vol.313 , pp. 618-621
    • Cara, J.F.1    Moshang Jr., T.2    Bongiovanni, A.M.3    Marx, B.S.4
  • 12
    • 0019818348 scopus 로고
    • The relationship between plasma 18 - Hydroxy - 11 - deoxycorticosterone levels and production of hypertension in the rat
    • Carroll J, Komanicky P, Melby JC. 1981. The relationship between plasma 18 - hydroxy - 11 - deoxycorticosterone levels and production of hypertension in the rat. J. Steroid Biochem. 14:989-95
    • (1981) J. Steroid Biochem. , vol.14 , pp. 989-995
    • Carroll, J.1    Komanicky, P.2    Melby, J.C.3
  • 14
    • 0021950117 scopus 로고
    • Origin of urinary non-conjugated 19-nor-deoxycorticosterone and metabolism of infused radio-labeled 19-nordeoxycorticosterone in men and women
    • Casey ML, Guerami A, Milewich L, Gomer-Sanchez CE, MacDonald PC. 1985. Origin of urinary non-conjugated 19-nor-deoxycorticosterone and metabolism of infused radio-labeled 19-nordeoxycorticosterone in men and women. J. Clin. Invest. 75:1335-38
    • (1985) J. Clin. Invest. , vol.75 , pp. 1335-1338
    • Casey, M.L.1    Guerami, A.2    Milewich, L.3    Gomer-Sanchez, C.E.4    MacDonald, P.C.5
  • 15
    • 0020188787 scopus 로고
    • Extra-adrenal formation of a mineralocorticoid: Deoxycorticosterone and deoxycorticosterone sulfate biosynthesis and metabolism
    • Casey ML, MacDonald PC. 1982. Extra-adrenal formation of a mineralocorticoid: deoxycorticosterone and deoxycorticosterone sulfate biosynthesis and metabolism. Endocrin. Rev. 3:396-403
    • (1982) Endocrin. Rev. , vol.3 , pp. 396-403
    • Casey, M.L.1    MacDonald, P.C.2
  • 16
    • 0027428111 scopus 로고
    • Mutations in the type II 3β-hydroxysteroid dehydrogenase gene in a patient with classic salt-wasting 3β-HSD deficiency congenital adrenal hyperplasia
    • Chang YT, Kappy MS, Iwamoto K, Wang X, Pang S. 1993. Mutations in the type II 3β-hydroxysteroid dehydrogenase gene in a patient with classic salt-wasting 3β-HSD deficiency congenital adrenal hyperplasia. Pediatr. Res. 34:698-700
    • (1993) Pediatr. Res. , vol.34 , pp. 698-700
    • Chang, Y.T.1    Kappy, M.S.2    Iwamoto, K.3    Wang, X.4    Pang, S.5
  • 17
    • 0029033431 scopus 로고
    • Absence of molecular defect in the type II 3β-hydroxysteroid dehydrogenase (3β-HSD) gene in premature pubarche children and hirsute female patients with moderately decreased adrenal 3β-HSD activity
    • Chang YT, Zhang L, Alkaddour HS, Mason JI, Lin K, et al. 1995. Absence of molecular defect in the type II 3β-hydroxysteroid dehydrogenase (3β-HSD) gene in premature pubarche children and hirsute female patients with moderately decreased adrenal 3β-HSD activity. Pediatr. Res. 37:820-24
    • (1995) Pediatr. Res. , vol.37 , pp. 820-824
    • Chang, Y.T.1    Zhang, L.2    Alkaddour, H.S.3    Mason, J.I.4    Lin, K.5
  • 18
    • 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 B, Picado-Leonard J, Haniu M, Bienkowski M, Hall PF, et al. 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: 407-11
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 407-411
    • Chung, B.1    Picado-Leonard, J.2    Haniu, M.3    Bienkowski, M.4    Hall, P.F.5
  • 19
    • 0027416241 scopus 로고
    • Linkage of 11β-hydroxylase mutations with altered steroid biosynthesis blood pressure in the Dahl rat
    • Cicila GT, Rapp JP, Wang J-M, St Lezin E, Ng SC, Kurtz TW. 1993. Linkage of 11β-hydroxylase mutations with altered steroid biosynthesis blood pressure in the Dahl rat. Nature Genet. 3:346-53
    • (1993) Nature Genet. , vol.3 , pp. 346-353
    • Cicila, G.T.1    Rapp, J.P.2    Wang, J.-M.3    St Lezin, E.4    Ng, S.C.5    Kurtz, T.W.6
  • 20
    • 0028104418 scopus 로고
    • The purification, cloning and expression of a novel luteinizing hormone-induced mitochondrial protein in MA-10 cells mouse Leydig tumor cells. Characterization of the steroidogenic acute regulatory protein (StAR)
    • Clark BJ, Wells J, King SR, Stocco DM. 1994. The purification, cloning and expression of a novel luteinizing hormone-induced mitochondrial protein in MA-10 cells mouse Leydig tumor cells. Characterization of the steroidogenic acute regulatory protein (StAR). J. Biol. Chem. 269:28314-22
    • (1994) J. Biol. Chem. , vol.269 , pp. 28314-28322
    • Clark, B.J.1    Wells, J.2    King, S.R.3    Stocco, D.M.4
  • 21
    • 0029055478 scopus 로고
    • Molecular variants in the P450c11AS gene as determinants of aldosterone synthase activity in the Dahl rat model of hypertension
    • Cover CM, Wang JM, St Letzin E, Kurtz TW, Mellon SH. 1995. Molecular variants in the P450c11AS gene as determinants of aldosterone synthase activity in the Dahl rat model of hypertension. J. Biol. Chem. 270:16555-60
    • (1995) J. Biol. Chem. , vol.270 , pp. 16555-16560
    • Cover, C.M.1    Wang, J.M.2    St Letzin, E.3    Kurtz, T.W.4    Mellon, S.H.5
  • 22
    • 0025999564 scopus 로고
    • The product of the CYP11B2 gene is required for aldosterone biosynthesis in the human adrenal cortex
    • Curnow KM, Tusie-Luna M, Pascoe L, Natarajan R, Gu J, et al. 1991. The product of the CYP11B2 gene is required for aldosterone biosynthesis in the human adrenal cortex. Mol. Endocrinol. 5:1513-22
    • (1991) Mol. Endocrinol. , vol.5 , pp. 1513-1522
    • Curnow, K.M.1    Tusie-Luna, M.2    Pascoe, L.3    Natarajan, R.4    Gu, J.5
  • 24
    • 0022383615 scopus 로고
    • 19-Nor-deoxycorticosteorne in rats bred for susceptibility and resistance to the hypertensive effects of salt
    • Dale SL, Holbrook MM, Melby JC. 1985. 19-Nor-deoxycorticosteorne in rats bred for susceptibility and resistance to the hypertensive effects of salt. Endocrinology 117:2424-27
    • (1985) Endocrinology , vol.117 , pp. 2424-2427
    • Dale, S.L.1    Holbrook, M.M.2    Melby, J.C.3
  • 25
    • 1842362472 scopus 로고
    • Analysis by immunocytochemistry and in situ hybridization of renin and its mRNA in kidney testis, adrenal and pituitary of the rat
    • Deschepper CF, Mellon SH, Cumin F, Baxter JD, Ganong WF. 1986. Analysis by immunocytochemistry and in situ hybridization of renin and its mRNA in kidney testis, adrenal and pituitary of the rat. Proc. Natl. Acad. Sci. USA 83: 7552-56
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 7552-7556
    • Deschepper, C.F.1    Mellon, S.H.2    Cumin, F.3    Baxter, J.D.4    Ganong, W.F.5
  • 26
    • 0023761690 scopus 로고
    • Localisation of 11β-hydroxysteroid dehydrogenase-tissue specific protector of the mineralocorticoid receptor
    • Edwards CR, Stewart PM, Burt D, Brett L, McIntyre MA, et al. 1988. Localisation of 11β-hydroxysteroid dehydrogenase-tissue specific protector of the mineralocorticoid receptor. Lancet 2: 986-89
    • (1988) Lancet , vol.2 , pp. 986-989
    • Edwards, C.R.1    Stewart, P.M.2    Burt, D.3    Brett, L.4    McIntyre, M.A.5
  • 27
    • 0022969531 scopus 로고
    • Activation of the rat kidney mineralocorticoid receptor
    • Eisen LP, Harmon JM. 1986. Activation of the rat kidney mineralocorticoid receptor. Endocrinology 119:1419-26
    • (1986) Endocrinology , vol.119 , pp. 1419-1426
    • Eisen, L.P.1    Harmon, J.M.2
  • 28
    • 0025996448 scopus 로고
    • Regulation of steroid hormone biosynthesis. Identification of precursors of a phosphoprotein targeted to the mitochondrion in stimulated rat adrenal cortex cells
    • Epstein LF, Orme-Johnson NR. 1991. Regulation of steroid hormone biosynthesis. Identification of precursors of a phosphoprotein targeted to the mitochondrion in stimulated rat adrenal cortex cells. J. Biol. Chem. 266:19739-45
    • (1991) J. Biol. Chem. , vol.266 , pp. 19739-19745
    • Epstein, L.F.1    Orme-Johnson, N.R.2
  • 29
    • 0023913120 scopus 로고
    • The steroid and thyroid hormone receptor superfamily
    • Evans RM. 1988. The steroid and thyroid hormone receptor superfamily. Science 240:889-95
    • (1988) Science , vol.240 , pp. 889-895
    • Evans, R.M.1
  • 30
    • 0028318144 scopus 로고
    • Point mutation Arg 440 to His in cytochrome P450c17 causes severe 17α-hydroxylase deficiency
    • Fardella CE, Hum DW, Homoki J, Miller WL. 1994. Point mutation Arg 440 to His in cytochrome P450c17 causes severe 17α-hydroxylase deficiency. J. Clin. Endocrinol. Metab. 79: 160-64
    • (1994) J. Clin. Endocrinol. Metab. , vol.79 , pp. 160-164
    • Fardella, C.E.1    Hum, D.W.2    Homoki, J.3    Miller, W.L.4
  • 31
    • 0030045134 scopus 로고    scopus 로고
    • Gene conversion in the CYP11B2 gene encoding aldosterone synthase (P450c11AS) is associated with, but does not cause, the syndrome of corticosterone methyl oxidase II deficiency
    • Fardella CE, Hum DW, Rodriguez H, Zhang G, Barry F, et al. 1996. Gene conversion in the CYP11B2 gene encoding aldosterone synthase (P450c11AS) is associated with, but does not cause, the syndrome of corticosterone methyl oxidase II deficiency. J. Clin. Endocrinol. Metab. 81:321-26
    • (1996) J. Clin. Endocrinol. Metab. , vol.81 , pp. 321-326
    • Fardella, C.E.1    Hum, D.W.2    Rodriguez, H.3    Zhang, G.4    Barry, F.5
  • 32
    • 0028907687 scopus 로고
    • Artificial mutations in P450c11AS (aldosterone synthase) can increase enzymatic activity: A model for low-renin hypertension?
    • Fardella CE, Rodriguez H, Hum DW, Mellon SH, Miller WL. 1995. Artificial mutations in P450c11AS (aldosterone synthase) can increase enzymatic activity: a model for low-renin hypertension? J. Clin. Endocrinol. Metab. 80:1040-43
    • (1995) J. Clin. Endocrinol. Metab. , vol.80 , pp. 1040-1043
    • Fardella, C.E.1    Rodriguez, H.2    Hum, D.W.3    Mellon, S.H.4    Miller, W.L.5
  • 34
    • 0000721214 scopus 로고
    • Protein synthesis and adrenocorticotropin responsiveness
    • Ferguson JJ. 1963. Protein synthesis and adrenocorticotropin responsiveness. J. Biol. Chem. 238:2754-59
    • (1963) J. Biol. Chem. , vol.238 , pp. 2754-2759
    • Ferguson, J.J.1
  • 35
    • 0002564483 scopus 로고
    • Lessons from experimental genetic hypertension
    • ed. JH Laragh, BM Brenner, New York: Raven. 2nd ed.
    • Ferrari P, Bianchi G. 1995. Lessons from experimental genetic hypertension. In Hypertension: Pathophysiology, Diagnosis and Management, ed. JH Laragh, BM Brenner, pp. 1261-79. New York: Raven. 2nd ed.
    • (1995) Hypertension: Pathophysiology, Diagnosis and Management , pp. 1261-1279
    • Ferrari, P.1    Bianchi, G.2
  • 36
    • 0028003682 scopus 로고
    • Corticosteroid receptors and the central nervous system
    • Funder JW. 1994. Corticosteroid receptors and the central nervous system. J. Steroid Biochem. Mol. Biol. 49:381-84
    • (1994) J. Steroid Biochem. Mol. Biol. , vol.49 , pp. 381-384
    • Funder, J.W.1
  • 37
    • 0018168024 scopus 로고
    • 19-Nor-deoxycorticosterone (19-nor-DOC): Mineralocorticoid receptor affinity higher than aldosterone, electrolyte activity lower
    • Funder JW, Mercer J, Ingram B, Feldman D, Wynne K, Adam WR. 1978. 19-Nor-deoxycorticosterone (19-nor-DOC): mineralocorticoid receptor affinity higher than aldosterone, electrolyte activity lower. Endocrinology 103: 1514-17
    • (1978) Endocrinology , vol.103 , pp. 1514-1517
    • Funder, J.W.1    Mercer, J.2    Ingram, B.3    Feldman, D.4    Wynne, K.5    Adam, W.R.6
  • 38
    • 0023743171 scopus 로고
    • Mineralocorticoid action: Target tissue specificity is enzyme, not receptor, mediated
    • Funder JW, Pearce PT, Smith R, Smith I. 1988. Mineralocorticoid action: Target tissue specificity is enzyme, not receptor, mediated. Science 242:583-85
    • (1988) Science , vol.242 , pp. 583-585
    • Funder, J.W.1    Pearce, P.T.2    Smith, R.3    Smith, I.4
  • 39
    • 0013783914 scopus 로고
    • Studies on the role of protein synthesis in the regulation of corticosterone production by ACTH in vivo
    • Garren LD, Ney RL, Davis WW. 1965. Studies on the role of protein synthesis in the regulation of corticosterone production by ACTH in vivo. Proc. Natl. Acad. Sci. USA 53:1443-50
    • (1965) Proc. Natl. Acad. Sci. USA , vol.53 , pp. 1443-1450
    • Garren, L.D.1    Ney, R.L.2    Davis, W.W.3
  • 40
    • 0028813929 scopus 로고
    • Amino acid substitution R384P in aldosterone synthase causes corticosterone methyloxidase type I deficiency
    • Geley S, Jöhrer K, Peter M, Denner K, Bernhardt R, et al. 1995. Amino acid substitution R384P in aldosterone synthase causes corticosterone methyloxidase type I deficiency. J. Clin. Endocrinol. Metab. 80:424-29
    • (1995) J. Clin. Endocrinol. Metab. , vol.80 , pp. 424-429
    • Geley, S.1    Jöhrer, K.2    Peter, M.3    Denner, K.4    Bernhardt, R.5
  • 41
    • 0018649747 scopus 로고
    • 19-Nor-deoxycorticosterone (19-nor-DOC): Mineralocorticoid isolated from the urine of rats with regenerating adrenals
    • Gomez-Sanchez CE, Holland OB, Murray BA, Lloyd HA, Milewich L. 1979. 19-Nor-deoxycorticosterone (19-nor-DOC): mineralocorticoid isolated from the urine of rats with regenerating adrenals. Endocrinology 105:708-11
    • (1979) Endocrinology , vol.105 , pp. 708-711
    • Gomez-Sanchez, C.E.1    Holland, O.B.2    Murray, B.A.3    Lloyd, H.A.4    Milewich, L.5
  • 42
    • 0027174837 scopus 로고
    • Evidence that primary aldosteronism may not be uncommon: 12% incidence among antihypertensive drug trial volunteers
    • Gordon RD, Zlesak MD, Tunny TJ, Stowasser M, Klemm SA. 1993. Evidence that primary aldosteronism may not be uncommon: 12% incidence among antihypertensive drug trial volunteers. Clin. Exp. Pharmacol. Physiol. 20:296-98
    • (1993) Clin. Exp. Pharmacol. Physiol. , vol.20 , pp. 296-298
    • Gordon, R.D.1    Zlesak, M.D.2    Tunny, T.J.3    Stowasser, M.4    Klemm, S.A.5
  • 44
    • 0021793996 scopus 로고
    • Unconjugated and conjugated 19-nor-deoxycorticosterone glucosidu-ronate. Elevated levels in essential hypertension
    • Griffing GT, Wilson TE, Melby JC. 1985. Unconjugated and conjugated 19-nor-deoxycorticosterone glucosidu-ronate. Elevated levels in essential hypertension. Hypertension 7(Suppl. 1): I12-17
    • (1985) Hypertension , vol.7 , Issue.1 SUPPL.
    • Griffing, G.T.1    Wilson, T.E.2    Melby, J.C.3
  • 45
    • 0025648068 scopus 로고
    • Alterations in aldosterone secretion and metabolism in low renin hypertension
    • Griffing GT, Wilson TE, Melby JC. 1990. Alterations in aldosterone secretion and metabolism in low renin hypertension. J. Clin. Endocrinol. Metab. 71:1454-60
    • (1990) J. Clin. Endocrinol. Metab. , vol.71 , pp. 1454-1460
    • Griffing, G.T.1    Wilson, T.E.2    Melby, J.C.3
  • 46
    • 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. 12:371-79
    • (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
  • 49
    • 0026547987 scopus 로고
    • Canadian Mennonites and individuals residing in the Friesland region of the Netherlands share the same molecular basis of 17α-hydroxylase deficiency
    • Imai T, Yanase T, Waterman MR, Simpson ER, Pratt JJ. 1992. Canadian Mennonites and individuals residing in the Friesland region of the Netherlands share the same molecular basis of 17α-hydroxylase deficiency. Hum. Genet. 89:95-96
    • (1992) Hum. Genet. , vol.89 , pp. 95-96
    • Imai, T.1    Yanase, T.2    Waterman, M.R.3    Simpson, E.R.4    Pratt, J.J.5
  • 50
    • 0025729737 scopus 로고
    • Inappropriate elevation of the aldosterone/plasma renin activity ratio in hypertensive patients with increases of 11-deoxycorticosterone and 18-hydroxy-11-deoxycorticosterone: A subtype of essential hypertension?
    • Komiya I, Yamada T, Aizawa T, Takasu N, Niwa A, et al. 1991. Inappropriate elevation of the aldosterone/plasma renin activity ratio in hypertensive patients with increases of 11-deoxycorticosterone and 18-hydroxy-11-deoxycorticosterone: a subtype of essential hypertension? Cardiology 78:99-110
    • (1991) Cardiology , vol.78 , pp. 99-110
    • Komiya, I.1    Yamada, T.2    Aizawa, T.3    Takasu, N.4    Niwa, A.5
  • 51
    • 9444241185 scopus 로고    scopus 로고
    • Deleted in proof
    • Deleted in proof.
  • 53
    • 0027230967 scopus 로고
    • Steroid 17α-hydroxylase and 17,20 lyase activities of P450c17: Contributions of serine and P450 reductase
    • Lin D, Black SM, Nagahama Y, Miller WL. 1993. Steroid 17α-hydroxylase and 17,20 lyase activities of P450c17: contributions of serine and P450 reductase. Endocrinology 132:2498-506
    • (1993) Endocrinology , vol.132 , pp. 2498-2506
    • Lin, D.1    Black, S.M.2    Nagahama, Y.3    Miller, W.L.4
  • 54
    • 0026348532 scopus 로고
    • Normal genes for the cholesterol side chain cleavage enzyme, P450scc, in congenital lipoid adrenal hyperplasia
    • Lin D, Gitelman SE, Saenger P, Miller WL. 1991. Normal genes for the cholesterol side chain cleavage enzyme, P450scc, in congenital lipoid adrenal hyperplasia. J. Clin. Invest. 88:1955-62
    • (1991) J. Clin. Invest. , vol.88 , pp. 1955-1962
    • Lin, D.1    Gitelman, S.E.2    Saenger, P.3    Miller, W.L.4
  • 55
    • 0028944669 scopus 로고
    • Role of steroidogenic acute regulatory protein in adrenal and gonadal sleroidogenesis
    • Lin D, Sugawara T, Strauss JF III, Clark BJ, Stocco DM, et al. 1995. Role of steroidogenic acute regulatory protein in adrenal and gonadal sleroidogenesis. Science 267:1828-31
    • (1995) Science , vol.267 , pp. 1828-1831
    • Lin, D.1    Sugawara, T.2    Strauss III, J.F.3    Clark, B.J.4    Stocco, D.M.5
  • 56
    • 0028220738 scopus 로고
    • Modeling and mutagenesis of the active site of human P450c17
    • Lin D, Zhang L, Chiao E, Miller WL. 1994. Modeling and mutagenesis of the active site of human P450c17. Mol. Endocrinol. 8:392-402
    • (1994) Mol. Endocrinol. , vol.8 , pp. 392-402
    • Lin, D.1    Zhang, L.2    Chiao, E.3    Miller, W.L.4
  • 58
    • 0025728267 scopus 로고
    • Zone-specific regulation of two distinct messenger RNAs for P450c11 (11/18-hydroxylase) in the adrenals of pregnant and non-pregnant rats
    • Malee MP, Mellon SH. 1991. Zone-specific regulation of two distinct messenger RNAs for P450c11 (11/18-hydroxylase) in the adrenals of pregnant and non-pregnant rats. Proc. Natl. Acad. Sci. USA 88:4731-35
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 4731-4735
    • Malee, M.P.1    Mellon, S.H.2
  • 59
    • 0027416423 scopus 로고
    • Dahl's salt-resistant normotensive rat has mutations in cytochrome P450(11β), but the salt-sensitive hypertensive rat does not
    • Matsukawa N, Nonaka Y, Higaki J, Nagano M, Mikami H, et al. 1993. Dahl's salt-resistant normotensive rat has mutations in cytochrome P450(11β), but the salt-sensitive hypertensive rat does not. J. Biol. Chem. 268:9117-21
    • (1993) J. Biol. Chem. , vol.268 , pp. 9117-9121
    • Matsukawa, N.1    Nonaka, Y.2    Higaki, J.3    Nagano, M.4    Mikami, H.5
  • 60
    • 0022995728 scopus 로고
    • Adrenal steroid receptors and actions in the nervous system
    • McEwen BS, de Kloet ER, Rostene W. 1986. Adrenal steroid receptors and actions in the nervous system. Physiol. Rev. 66:1121-88
    • (1986) Physiol. Rev. , vol.66 , pp. 1121-1188
    • McEwen, B.S.1    De Kloet, E.R.2    Rostene, W.3
  • 61
    • 0029041206 scopus 로고
    • Non-salt-losing male pseudohermaphroditism due to the novel homozygous N100S mutation in the type II 3β-hydroxysteroid dehydrogenase gene
    • Mebarki F, Sanchez R, Rheaume E, Laflamme N, Simard J, et al. 1995. Non-salt-losing male pseudohermaphroditism due to the novel homozygous N100S mutation in the type II 3β-hydroxysteroid dehydrogenase gene. J. Clin. Endocrinol. Metab. 80:2127-34
    • (1995) J. Clin. Endocrinol. Metab. , vol.80 , pp. 2127-2134
    • Mebarki, F.1    Sanchez, R.2    Rheaume, E.3    Laflamme, N.4    Simard, J.5
  • 62
    • 0028929022 scopus 로고
    • P450c11B3 mRNA, transcribed from a third P450c11 gene, is expressed in a tissue-specific, developmentally and hormonally regulated fashion in the rodent adrenal, and encodes a protein with both 11-hydroxylase and 18-hydroxylase activities
    • Mellon SH, Bair SR, Monis H. 1995. P450c11B3 mRNA, transcribed from a third P450c11 gene, is expressed in a tissue-specific, developmentally and hormonally regulated fashion in the rodent adrenal, and encodes a protein with both 11-hydroxylase and 18-hydroxylase activities. J. Biol. Chem. 270:1643-49
    • (1995) J. Biol. Chem. , vol.270 , pp. 1643-1649
    • Mellon, S.H.1    Bair, S.R.2    Monis, H.3
  • 63
    • 0024460383 scopus 로고
    • Extra-adrenal steroid 21-hydroxylation is not mediated by P450c21
    • Mellon SH, Miller WL. 1989. Extra-adrenal steroid 21-hydroxylation is not mediated by P450c21. J. Clin. Invest. 84:1497-502
    • (1989) J. Clin. Invest. , vol.84 , pp. 1497-1502
    • Mellon, S.H.1    Miller, W.L.2
  • 64
    • 0024064517 scopus 로고
    • Molecular biology of steroid hormone synthesis
    • Miller WL. 1988. Molecular biology of steroid hormone synthesis. Endocrin. Rev. 9:295-318
    • (1988) Endocrin. Rev. , vol.9 , pp. 295-318
    • Miller, W.L.1
  • 65
    • 0028154269 scopus 로고
    • Genetics, diagnosis, and management of 21-hydroxylase deficiency
    • Miller WL. 1994. Genetics, diagnosis, and management of 21-hydroxylase deficiency. J. Clin. Endocrinol. Metab. 78:241-46
    • (1994) J. Clin. Endocrinol. Metab. , vol.78 , pp. 241-246
    • Miller, W.L.1
  • 66
    • 0029583435 scopus 로고
    • Mitochondrial specificity of the early steps in steroidogenesis
    • Miller WL. 1995. Mitochondrial specificity of the early steps in steroidogenesis. J. Steroid Biochem. Mol. Biol. 55: 607-16
    • (1995) J. Steroid Biochem. Mol. Biol. , vol.55 , pp. 607-616
    • Miller, W.L.1
  • 67
    • 0000697658 scopus 로고
    • The adrenal cortex
    • P Felig, J Baxter, L Frohman, New York: McGraw Hill. 3rd ed.
    • Miller WL, Tyrrell JB. 1995. The adrenal cortex. In Endocrinology and Metabolism, P Felig, J Baxter, L Frohman, pp. 555-717. New York: McGraw Hill. 3rd ed.
    • (1995) Endocrinology and Metabolism , pp. 555-717
    • Miller, W.L.1    Tyrrell, J.B.2
  • 68
    • 0027218610 scopus 로고
    • Congenitally defective aldosterone biosynthesis in the humans: Inactivation of the P-450c18 gene (CYP11B2) due to nucleotide deletion in CMO I deficient patients
    • Mitsuuchi Y, Kawamoto T, Miyahara K, Ulick S, Morton D, et al. 1993. Congenitally defective aldosterone biosynthesis in the humans: inactivation of the P-450c18 gene (CYP11B2) due to nucleotide deletion in CMO I deficient patients. Biochem. Biophys. Res. Commun. 190:864-69
    • (1993) Biochem. Biophys. Res. Commun. , vol.190 , pp. 864-869
    • Mitsuuchi, Y.1    Kawamoto, T.2    Miyahara, K.3    Ulick, S.4    Morton, D.5
  • 69
    • 0026340803 scopus 로고
    • Corticosteroids, receptors, and the organ-specific functions of 11β-hydroxysteroid dehydrogenase
    • Monder C. 1991. Corticosteroids, receptors, and the organ-specific functions of 11β-hydroxysteroid dehydrogenase. FASEB J. 5:3047-54
    • (1991) FASEB J. , vol.5 , pp. 3047-3054
    • Monder, C.1
  • 70
    • 0025017957 scopus 로고
    • Human P450scc gene transcription is induced by cyclic AMP and repressed by 12-O-tetradecanolyphorbol-13-acetate and A23187 by independent cis-elements
    • Moore CCD, Brentano ST, Miller WL. 1990. Human P450scc gene transcription is induced by cyclic AMP and repressed by 12-O-tetradecanolyphorbol-13-acetate and A23187 by independent cis-elements. Mol. Cell Biol. 10:6013-23
    • (1990) Mol. Cell Biol. , vol.10 , pp. 6013-6023
    • Moore, C.C.D.1    Brentano, S.T.2    Miller, W.L.3
  • 71
    • 0027165109 scopus 로고
    • Structure and function of the model hepatic form of 11β-hydroxysteroid dehydrogenase in the squirrel monkey, an animal model of glucocorticoid resistance
    • Moore CCD, Mellon SH, Murai J, Siiteri PK, Miller WL. 1993. Structure and function of the model hepatic form of 11β-hydroxysteroid dehydrogenase in the squirrel monkey, an animal model of glucocorticoid resistance. Endocrinology 133:368-75
    • (1993) Endocrinology , vol.133 , pp. 368-375
    • Moore, C.C.D.1    Mellon, S.H.2    Murai, J.3    Siiteri, P.K.4    Miller, W.L.5
  • 72
    • 0025935967 scopus 로고
    • Clinical and molecular genetics of congenital adrenal hyperplasia due to 21-hydroxylase deficiency
    • Morel Y, Miller WL. 1991. Clinical and molecular genetics of congenital adrenal hyperplasia due to 21-hydroxylase deficiency. Adv. Hum. Genet. 20:1-68
    • (1991) Adv. Hum. Genet. , vol.20 , pp. 1-68
    • Morel, Y.1    Miller, W.L.2
  • 73
    • 0027401686 scopus 로고
    • Isolation and characterization of rat CYP11B genes involved in late steps of mineralo- and glucocorticoid syntheses
    • Mukai K, Imai M, Shimada H, Ishimura Y. 1993. Isolation and characterization of rat CYP11B genes involved in late steps of mineralo- and glucocorticoid syntheses. J. Biol. Chem. 268:9130-37
    • (1993) J. Biol. Chem. , vol.268 , pp. 9130-9137
    • Mukai, K.1    Imai, M.2    Shimada, H.3    Ishimura, Y.4
  • 74
    • 0029160972 scopus 로고
    • Human hypertension caused by mutations in the kidney isozyme of 11 beta-hydroxysteroid dehydrogenase
    • Mune T, Rogerson FM, Nikkila H, Agarwal AK, White PC. 1995. Human hypertension caused by mutations in the kidney isozyme of 11 beta-hydroxysteroid dehydrogenase. Nature Genet. 10: 394-99
    • (1995) Nature Genet. , vol.10 , pp. 394-399
    • Mune, T.1    Rogerson, F.M.2    Nikkila, H.3    Agarwal, A.K.4    White, P.C.5
  • 75
    • 0023918714 scopus 로고
    • On the membrane topology of vertebrate cytochrome P-450 proteins
    • Nelson DR, Strobel HW. 1988. On the membrane topology of vertebrate cytochrome P-450 proteins. J. Biol. Chem. 263:6038-50
    • (1988) J. Biol. Chem. , vol.263 , pp. 6038-6050
    • Nelson, D.R.1    Strobel, H.W.2
  • 76
    • 0026344299 scopus 로고
    • Functional expression of the cDNAs encoding rat 11β-hydroxylase (cytochrome P45011β) and aldosterone synthase (cytochrome P45011β, aldo)
    • Nonaka Y, Okamoto M. 1991. Functional expression of the cDNAs encoding rat 11β-hydroxylase (cytochrome P45011β) and aldosterone synthase (cytochrome P45011β, aldo). Eur. J. Biochem. 202:897-902
    • (1991) Eur. J. Biochem. , vol.202 , pp. 897-902
    • Nonaka, Y.1    Okamoto, M.2
  • 77
    • 0026748962 scopus 로고
    • Zone-specific expression of aldosterone synthase cytochrome P450 and cytochrome P450-11β in rat adrenal cortex: Histochemical basis for the functional zonation
    • Ogishima T, Suzuki H, Itala J, Mitani F, Ishimura Y. 1992. Zone-specific expression of aldosterone synthase cytochrome P450 and cytochrome P450-11β in rat adrenal cortex: histochemical basis for the functional zonation. Endocrinology 130:2971-77
    • (1992) Endocrinology , vol.130 , pp. 2971-2977
    • Ogishima, T.1    Suzuki, H.2    Itala, J.3    Mitani, F.4    Ishimura, Y.5
  • 78
    • 0027135717 scopus 로고
    • Regulation of Na-K-ATPase gene expression by aldosterone in vascular smooth muscle cells
    • Oguchi A, Ikeda U, Kanbe T, Tsuruya Y, Yamamoto K, et al. 1993. Regulation of Na-K-ATPase gene expression by aldosterone in vascular smooth muscle cells. Am. J Phvsiol. 265:H1167-72
    • (1993) Am. J Phvsiol. , vol.265
    • Oguchi, A.1    Ikeda, U.2    Kanbe, T.3    Tsuruya, Y.4    Yamamoto, K.5
  • 80
    • 0027447948 scopus 로고
    • Peripheral-type benzodiazepine/diazepam binding inhibitor receptor: Biological role in steroidogenic cell function
    • Papadopoulos V. 1993. Peripheral-type benzodiazepine/diazepam binding inhibitor receptor: biological role in steroidogenic cell function. Endocrin. Rev. 14:222-40
    • (1993) Endocrin. Rev. , vol.14 , pp. 222-240
    • Papadopoulos, V.1
  • 81
    • 0026771282 scopus 로고
    • Mutations in the human CYP11B2 (aldosterone synthase) gene causing corticosterone methyloxidase II deficiency
    • Pascoe L, Curnow K, Slutsker L, Rösler A, White PC. 1992. Mutations in the human CYP11B2 (aldosterone synthase) gene causing corticosterone methyloxidase II deficiency. Proc. Natl. Acad. Sci. USA 89:4996-5000
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4996-5000
    • Pascoe, L.1    Curnow, K.2    Slutsker, L.3    Rösler, A.4    White, P.C.5
  • 82
    • 0023761877 scopus 로고
    • Homologous sequences in steroidogenic enzymes, steroid receptors and a steroid binding protein suggest a consensus steroid-binding sequence
    • Picado-Leonard J, Miller WL. 1988. Homologous sequences in steroidogenic enzymes, steroid receptors and a steroid binding protein suggest a consensus steroid-binding sequence. Mol. Endocrinol. 2:1145-50
    • (1988) Mol. Endocrinol. , vol.2 , pp. 1145-1150
    • Picado-Leonard, J.1    Miller, W.L.2
  • 85
    • 0024411065 scopus 로고
    • Mineralocorticoid receptor of the chick intestine: Oligomeric structure and transformation
    • Rafestin-Oblin ME, Coletter B, Radanyi C, Lombès M, Baulieu EE. 1989. Mineralocorticoid receptor of the chick intestine: oligomeric structure and transformation. J. Biol. Chem. 264: 9304-9
    • (1989) J. Biol. Chem. , vol.264 , pp. 9304-9309
    • Rafestin-Oblin, M.E.1    Coletter, B.2    Radanyi, C.3    Lombès, M.4    Baulieu, E.E.5
  • 86
    • 0020435968 scopus 로고
    • Dahl salt-susceptible and salt-resistant rats. A review
    • Rapp JP. 1982. Dahl salt-susceptible and salt-resistant rats. A review. Hypertension 4:753-63
    • (1982) Hypertension , vol.4 , pp. 753-763
    • Rapp, J.P.1
  • 87
    • 0003082114 scopus 로고
    • Genetics of experimental hypertension
    • ed. J Genest, O Kuchel, P Hamet, M Cantin, New York: McGraw-Hill. 2nd ed.
    • Rapp JP. 1983. Genetics of experimental hypertension. In Hypertension, Pathophysiology and Treatment, ed. J Genest, O Kuchel, P Hamet, M Cantin, pp. 582-98. New York: McGraw-Hill. 2nd ed.
    • (1983) Hypertension, Pathophysiology and Treatment , pp. 582-598
    • Rapp, J.P.1
  • 88
    • 0021858418 scopus 로고
    • Development and characteristics of inbred strains of Dahl salt-sensitive and salt-resistant rats
    • Rapp JP, Dene H. 1985. Development and characteristics of inbred strains of Dahl salt-sensitive and salt-resistant rats. Hypertension 7:340-49
    • (1985) Hypertension , vol.7 , pp. 340-349
    • Rapp, J.P.1    Dene, H.2
  • 90
    • 0025337581 scopus 로고
    • The non-DNA-binding heterooligomeric form of mammalian steroid hormone receptors contain a hsp 90-bound 59 kilodalton protein
    • Renoir J, Radanyi C, Faber LE, Baulieu EE. 1990. The non-DNA-binding heterooligomeric form of mammalian steroid hormone receptors contain a hsp 90-bound 59 kilodalton protein. J. Biol. Chem. 265:10740-45
    • (1990) J. Biol. Chem. , vol.265 , pp. 10740-10745
    • Renoir, J.1    Radanyi, C.2    Faber, L.E.3    Baulieu, E.E.4
  • 92
    • 0028920247 scopus 로고
    • Identification and characterization of the G15D mutation found in a male patient with 3β-hydroxysteroid dehydrogenase (3β-HSD) deficiency: Alteration of the putative NAD-binding domain of type II 3β-HSD
    • Rhéaume E, Sanchez R, Mébarki F, Gagnon E, Carel J-C, et al. 1995. Identification and characterization of the G15D mutation found in a male patient with 3β-hydroxysteroid dehydrogenase (3β-HSD) deficiency: alteration of the putative NAD-binding domain of type II 3β-HSD. Biochemistry 34:2893-900
    • (1995) Biochemistry , vol.34 , pp. 2893-2900
    • Rhéaume, E.1    Sanchez, R.2    Mébarki, F.3    Gagnon, E.4    Carel, J.-C.5
  • 93
    • 0027971610 scopus 로고
    • Molecular basis of congenital adrenal hyperplasia in two siblings with classical nonsalt-losing 3β-hydroxysteroid dehydrogenase deficiency
    • Rhéaume E, Sanchez R, Simard J, Change YT, Wang J, et al. 1994. Molecular basis of congenital adrenal hyperplasia in two siblings with classical nonsalt-losing 3β-hydroxysteroid dehydrogenase deficiency. J. Clin. Endocrinol. Metab. 79:1012-18
    • (1994) J. Clin. Endocrinol. Metab. , vol.79 , pp. 1012-1018
    • Rhéaume, E.1    Sanchez, R.2    Simard, J.3    Change, Y.T.4    Wang, J.5
  • 94
    • 0025164709 scopus 로고
    • A case of male pseudohermaph-roditism due to 17α-hydroxylse deficiency and hormonal profiles in the nuclear family
    • Rohmer V, Barbot N, Bertrand P, Hanoul K, Bigorgne JC, Forest MG. 1990. A case of male pseudohermaph-roditism due to 17α-hydroxylse deficiency and hormonal profiles in the nuclear family. J. Clin. Endocrinol. Metab. 71:523-29
    • (1990) J. Clin. Endocrinol. Metab. , vol.71 , pp. 523-529
    • Rohmer, V.1    Barbot, N.2    Bertrand, P.3    Hanoul, K.4    Bigorgne, J.C.5    Forest, M.G.6
  • 95
    • 0023684483 scopus 로고
    • The hypertensinogenic activity of 18-hydroxy-19-norcorticosterone in the adrenalectomized rat
    • Rosenthal T, Shani M, Peleg E, Harnik M. 1988. The hypertensinogenic activity of 18-hydroxy-19-norcorticosterone in the adrenalectomized rat. Am. J. Hypertens. 1:49S-52S
    • (1988) Am. J. Hypertens. , vol.1
    • Rosenthal, T.1    Shani, M.2    Peleg, E.3    Harnik, M.4
  • 96
    • 0021223924 scopus 로고
    • The natural history of salt-wasting disorders of adrenal and renal origin
    • Rösler A. 1984. The natural history of salt-wasting disorders of adrenal and renal origin. J. Clin. Endocrinol. Metab. 59:689-700
    • (1984) J. Clin. Endocrinol. Metab. , vol.59 , pp. 689-700
    • Rösler, A.1
  • 97
    • 0026591712 scopus 로고
    • High frequency of congenital adrenal hyperplasia (classic 11-beta-hydroxylase deficiency) among Jews from Morocco
    • Rösler A, Leiberman E, Cohen T. 1992. High frequency of congenital adrenal hyperplasia (classic 11-beta-hydroxylase deficiency) among Jews from Morocco. Am. J. Med. Genet. 42:827-34
    • (1992) Am. J. Med. Genet. , vol.42 , pp. 827-834
    • Rösler, A.1    Leiberman, E.2    Cohen, T.3
  • 98
    • 0027527215 scopus 로고
    • Pharmacological and functional characterization of human mineralocorticoid and glucccorticoid receptor ligands
    • Rupprecht R, Reul JMHM, van Steensel B, Spengler D, Söder M, et al. 1993. Pharmacological and functional characterization of human mineralocorticoid and glucccorticoid receptor ligands. Eur. J. Pharm. 247:145-54
    • (1993) Eur. J. Pharm. , vol.247 , pp. 145-154
    • Rupprecht, R.1    Reul, J.M.H.M.2    Van Steensel, B.3    Spengler, D.4    Söder, M.5
  • 99
    • 0015535991 scopus 로고
    • Significant associations of adrenal cortical abnormalities with 'essential' hypertension
    • Russel RP, Masi AT. 1973. Significant associations of adrenal cortical abnormalities with 'essential' hypertension. Am. J. Med. 54:44-51
    • (1973) Am. J. Med. , vol.54 , pp. 44-51
    • Russel, R.P.1    Masi, A.T.2
  • 100
    • 0027162955 scopus 로고
    • A new isoform of 11β-hydroxysteroid dehydrogenase in aldosterone target cells
    • Rusvai E, Náray-Fejes-Tóth A. 1993. A new isoform of 11β-hydroxysteroid dehydrogenase in aldosterone target cells. J. Biol. Chem. 268:10717-20
    • (1993) J. Biol. Chem. , vol.268 , pp. 10717-10720
    • Rusvai, E.1    Náray-Fejes-Tóth, A.2
  • 101
    • 0025290187 scopus 로고
    • The 56-59 kilodalton protein identified in untransformed steroid receptor complexes is a unique protein that exists in cytosol in a complex with both the 70- and 90-kilodalton beat shock protein
    • Sanchez E, Faber L, Henzel M, Proatt W. 1990. The 56-59 kilodalton protein identified in untransformed steroid receptor complexes is a unique protein that exists in cytosol in a complex with both the 70- and 90-kilodalton beat shock protein. Biochemistry 29:5145-52
    • (1990) Biochemistry , vol.29 , pp. 5145-5152
    • Sanchez, E.1    Faber, L.2    Henzel, M.3    Proatt, W.4
  • 102
    • 0028069041 scopus 로고
    • Functional characterization of the novel L108W and P186L mutations detected in the type II 3 β-hydroxysteroid dehydrogenase gene of a male pseudohermaphrodite with congenital adrenal hyperplasia
    • Sanchez R, Mebarki F, Rheaume E, Laflamme N, Forest MG, et al. 1994. Functional characterization of the novel L108W and P186L mutations detected in the type II 3 β-hydroxysteroid dehydrogenase gene of a male pseudohermaphrodite with congenital adrenal hyperplasia. Hum. Mol. Genet. 3:1639-45
    • (1994) Hum. Mol. Genet. , vol.3 , pp. 1639-1645
    • Sanchez, R.1    Mebarki, F.2    Rheaume, E.3    Laflamme, N.4    Forest, M.G.5
  • 103
    • 0028328226 scopus 로고
    • Detection and functional characterization of the novel missense mutation Y254D in type II 3β-hydroxysteroid dehydrogenase (3βHSD) gene of a female patient with nonsalt-losing 3βHSD deficiency
    • Sanchez R, Rheaume E, Laflamme N, Rosenfield RL, Labrie F, Simard J. 1994. Detection and functional characterization of the novel missense mutation Y254D in type II 3β-hydroxysteroid dehydrogenase (3βHSD) gene of a female patient with nonsalt-losing 3βHSD deficiency. J. Clin. Endocrinol. Metab. 78:561-67
    • (1994) J. Clin. Endocrinol. Metab. , vol.78 , pp. 561-567
    • Sanchez, R.1    Rheaume, E.2    Laflamme, N.3    Rosenfield, R.L.4    Labrie, F.5    Simard, J.6
  • 104
    • 0028036187 scopus 로고
    • Role of adrenal renin in the regulation of adrenal steroidogenesis by ACTH
    • Sander M, Ganten D, Mellon SH. 1994. Role of adrenal renin in the regulation of adrenal steroidogenesis by ACTH. Proc. Natl. Acad. Sci. USA 91:148-52
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 148-152
    • Sander, M.1    Ganten, D.2    Mellon, S.H.3
  • 105
    • 0022993934 scopus 로고
    • Characterization of the rat colonic aldosterone receptor and its activation process
    • Schulman G, Miller-Diener A, Litwach G, Bastl CP. 1986. Characterization of the rat colonic aldosterone receptor and its activation process. J. Biol. Chem. 261:12102-8
    • (1986) J. Biol. Chem. , vol.261 , pp. 12102-12108
    • Schulman, G.1    Miller-Diener, A.2    Litwach, G.3    Bastl, C.P.4
  • 106
    • 0028123293 scopus 로고
    • Congenital adrenal hyperplasia caused by a novel homozygous frameshift mutation 273DAA in type II 3β-hydroxysteroid dehydrogenase gene (HSD3B2) in three male patients of Afghan/Pakistani origin
    • Simard J, Rhéaume E, Leblanc J-F, Wallis SC, Joplin GF, et al. 1994. Congenital adrenal hyperplasia caused by a novel homozygous frameshift mutation 273DAA in type II 3β-hydroxysteroid dehydrogenase gene (HSD3B2) in three male patients of Afghan/Pakistani origin. Hum. Mol. Genet. 3:327-30
    • (1994) Hum. Mol. Genet. , vol.3 , pp. 327-330
    • Simard, J.1    Rhéaume, E.2    Leblanc, J.-F.3    Wallis, S.C.4    Joplin, G.F.5
  • 107
    • 0027322946 scopus 로고
    • Molecular basis of congenital adrenal hyperplasia due to 3β-hydroxysteroid dehydrogenase deficiency
    • Simard J, Rheaume E, Sanchez R, Laflamme N, de Launoit Y, et al. 1993. Molecular basis of congenital adrenal hyperplasia due to 3β-hydroxysteroid dehydrogenase deficiency. Mol. Endocrinol. 7:716-28
    • (1993) Mol. Endocrinol. , vol.7 , pp. 716-728
    • Simard, J.1    Rheaume, E.2    Sanchez, R.3    Laflamme, N.4    De Launoit, Y.5
  • 108
    • 0025233648 scopus 로고
    • Purification of unactivated progesterone receptor and identification of novel receptor-associated proteins
    • Smith J, Faber L, Toft D. 1990. Purification of unactivated progesterone receptor and identification of novel receptor-associated proteins. J. Biol. Chem. 265:3996-4003
    • (1990) J. Biol. Chem. , vol.265 , pp. 3996-4003
    • Smith, J.1    Faber, L.2    Toft, D.3
  • 109
    • 0026074413 scopus 로고
    • Aldosterone synthesis in patients with salt-wasting congenital adrenal hyperplasia (21-hydroxylase deficiency) and complete absence of adrenal 21-hydroxylase (P450c21)
    • Speiser PW, Agdere L, Veshiba H, White PC, New MI. 1991. Aldosterone synthesis in patients with salt-wasting congenital adrenal hyperplasia (21-hydroxylase deficiency) and complete absence of adrenal 21-hydroxylase (P450c21). N. Engl. J. Med. 3221:145-49
    • (1991) N. Engl. J. Med. , vol.3221 , pp. 145-149
    • Speiser, P.W.1    Agdere, L.2    Veshiba, H.3    White, P.C.4    New, M.I.5
  • 110
    • 0023760499 scopus 로고
    • Syndrome of apparent mineralocorticoid excess. A defect in the cortisol-cortisone shuttle
    • Stewart PM, Corrie JET, Shackleton CHL, Edward CRW. 1988. Syndrome of apparent mineralocorticoid excess. A defect in the cortisol-cortisone shuttle. J. Clin. Invest. 82:340-49
    • (1988) J. Clin. Invest. , vol.82 , pp. 340-349
    • Stewart, P.M.1    Corrie, J.E.T.2    Shackleton, C.H.L.3    Edward, C.R.W.4
  • 111
    • 0025176537 scopus 로고
    • Mineralocorticoid activity of carbenoxolone: Contrasting effects of carbenoxolone and liquorice on 11β-hydroxysteroid dehydrogenase activity in man
    • Stewart PM, Wallace AM, Atherden SM, Shearing CH, Edwards CRW. 1990. Mineralocorticoid activity of carbenoxolone: contrasting effects of carbenoxolone and liquorice on 11β-hydroxysteroid dehydrogenase activity in man. Clin. Sci. 78:49-54
    • (1990) Clin. Sci. , vol.78 , pp. 49-54
    • Stewart, P.M.1    Wallace, A.M.2    Atherden, S.M.3    Shearing, C.H.4    Edwards, C.R.W.5
  • 112
    • 0025941096 scopus 로고
    • The 30 kDa mitochondrial protein induced by hormone stimulation in MA-10 mouse Leydig tumor cells are processed from larger precursors
    • Stocco DM, Sodeman TC. 1991. The 30 kDa mitochondrial protein induced by hormone stimulation in MA-10 mouse Leydig tumor cells are processed from larger precursors. J. Biol. Chem. 266:19731-38
    • (1991) J. Biol. Chem. , vol.266 , pp. 19731-19738
    • Stocco, D.M.1    Sodeman, T.C.2
  • 113
    • 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 JF III, Lin D, et al. 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 92:4778-82
    • (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
  • 114
    • 0028819993 scopus 로고
    • The structure of the human steroidogenic acute regulatory (StAR) protein gene: StAR stimulates mitochondrial cholesterol 27-hydroxylase activity
    • Sugawara T, Lin D, Holt JA, Martin KO, Javitt NB, et al. 1995. The structure of the human steroidogenic acute regulatory (StAR) protein gene: StAR stimulates mitochondrial cholesterol 27-hydroxylase activity. Biochemistry 34: 12506-12
    • (1995) Biochemistry , vol.34 , pp. 12506-12512
    • Sugawara, T.1    Lin, D.2    Holt, J.A.3    Martin, K.O.4    Javitt, N.B.5
  • 115
    • 0028923222 scopus 로고
    • Significance of 19-nor aldosterone, a new mineralocorticoid, in clinical and experimental hypertension
    • Takeda Y, Miyamori I, Takeda R. 1995. Significance of 19-nor aldosterone, a new mineralocorticoid, in clinical and experimental hypertension. Steroids 60: 137-42
    • (1995) Steroids , vol.60 , pp. 137-142
    • Takeda, Y.1    Miyamori, I.2    Takeda, R.3
  • 116
    • 0026095840 scopus 로고
    • The human gene for 11β-hydroxysteroid dehydrogenase. Structure, tissue distribution, and chromosomal localization
    • Tannin GM, Agarwal AK, Monder C, New MI, White PC. 1991. The human gene for 11β-hydroxysteroid dehydrogenase. Structure, tissue distribution, and chromosomal localization. J. Biol. Chem. 266:16653-58
    • (1991) J. Biol. Chem. , vol.266 , pp. 16653-16658
    • Tannin, G.M.1    Agarwal, A.K.2    Monder, C.3    New, M.I.4    White, P.C.5
  • 117
    • 0028973522 scopus 로고
    • T→A transversion 11 bp from a splice acceptor site in the gene for steroidogenic acute regulatory protein causes congenital lipoid adrenal hyperplasia
    • Tee MK, Lin D, Sugawara T, Holt JA, Guiguen Y, et al. 1995. T→A transversion 11 bp from a splice acceptor site in the gene for steroidogenic acute regulatory protein causes congenital lipoid adrenal hyperplasia. Hum. Mol. Genet. 4:2299-305
    • (1995) Hum. Mol. Genet. , vol.4 , pp. 2299-2305
    • Tee, M.K.1    Lin, D.2    Sugawara, T.3    Holt, J.A.4    Guiguen, Y.5
  • 119
    • 0026651143 scopus 로고
    • Dietary potassium supplementation and sodium restriction stimulate aldosterone synthase but not 11β-hydroxylase P450 messenger ribonucleic acid accumulation in rat adrenals and require angiotensin II production
    • Tremblay A, Parker KL, Lehoux JG. 1992. Dietary potassium supplementation and sodium restriction stimulate aldosterone synthase but not 11β-hydroxylase P450 messenger ribonucleic acid accumulation in rat adrenals and require angiotensin II production. Endocrinology 130:3152-58
    • (1992) Endocrinology , vol.130 , pp. 3152-3158
    • Tremblay, A.1    Parker, K.L.2    Lehoux, J.G.3
  • 120
    • 0026703632 scopus 로고
    • The biochemical phenotypes of two inborn errors in the biosynthesis of aldosterone
    • Ulick S, Wang JZ, Morton H. 1992. The biochemical phenotypes of two inborn errors in the biosynthesis of aldosterone. J. Clin. Endocrinol. Metab. 74: 1415-20
    • (1992) J. Clin. Endocrinol. Metab. , vol.74 , pp. 1415-1420
    • Ulick, S.1    Wang, J.Z.2    Morton, H.3
  • 121
    • 0025821905 scopus 로고
    • A hybrid cell mapping panel for regional localization of probes to human chromosome 8
    • Wagner MJ, Ge Y, Siciliano M, Wells DE. 1991. A hybrid cell mapping panel for regional localization of probes to human chromosome 8. Genomics 10: 114-25
    • (1991) Genomics , vol.10 , pp. 114-125
    • Wagner, M.J.1    Ge, Y.2    Siciliano, M.3    Wells, D.E.4
  • 122
    • 0028167769 scopus 로고
    • Disorders of steroid 11β-hydroxylase isozymes
    • White PC, Curnow KM, Pascoe L. 1994. Disorders of steroid 11β-hydroxylase isozymes. Endocrin. Rev. 15: 421-38
    • (1994) Endocrin. Rev. , vol.15 , pp. 421-438
    • White, P.C.1    Curnow, K.M.2    Pascoe, L.3
  • 123
    • 0025847381 scopus 로고
    • A mutation in CYP11B1 (Arg 448→His) associated with steroid 11β-hydroxylase deficiency in Jews of Moroccan origin
    • White PC, Dupont J, New MI, Lieberman E, Hochberg Z, Rösler A. 1991. A mutation in CYP11B1 (Arg 448→His) associated with steroid 11β-hydroxylase deficiency in Jews of Moroccan origin. J. Clin. Invest. 87:1664-67
    • (1991) J. Clin. Invest. , vol.87 , pp. 1664-1667
    • White, P.C.1    Dupont, J.2    New, M.I.3    Lieberman, E.4    Hochberg, Z.5    Rösler, A.6
  • 124
    • 0025953758 scopus 로고
    • Dysregulation of aldosterone secretion and its relationship to the pathogenesis of essential hypertension
    • Williams G, Moore T, Hollenberg N. 1991. Dysregulation of aldosterone secretion and its relationship to the pathogenesis of essential hypertension. Endocrinol. Metab. Clin. North. Am. 20: 423
    • (1991) Endocrinol. Metab. Clin. North. Am. , vol.20 , pp. 423
    • Williams, G.1    Moore, T.2    Hollenberg, N.3
  • 126
    • 0023929088 scopus 로고
    • Heterozygotes for 17α-hydroxylase deficiency can be detected with a short ACTH test
    • Wit JM, Van Roermund HPC, Oostdijk W. 1988. Heterozygotes for 17α-hydroxylase deficiency can be detected with a short ACTH test. Clin. Endocrinol. 28:657-64
    • (1988) Clin. Endocrinol. , vol.28 , pp. 657-664
    • Wit, J.M.1    Van Roermund, H.P.C.2    Oostdijk, W.3
  • 127
    • 0026081588 scopus 로고
    • 17α-Hydroxylase/17,20 lyase deficiency: From clinical investigation to molecular definition
    • Yanase T, Simpson ER, Waterman MR. 1991. 17α-Hydroxylase/17,20 lyase deficiency: from clinical investigation to molecular definition. Endocrin. Rev. 12: 91-108
    • (1991) Endocrin. Rev. , vol.12 , pp. 91-108
    • Yanase, T.1    Simpson, E.R.2    Waterman, M.R.3
  • 128
    • 0026756522 scopus 로고
    • Molecular basis of apparent isolated 17,20-lyase deficiency: Compound heterozygous mutations in the C-terminal region (Arg(496)→Cys, Gln(461)→Stop) actually cause combined 17α-hydroxylase/17,20-lyase deficiency
    • Yanase T, Waterman MR, Zachmann M, Winter JSD, Simpson ER, Kagimoto M. 1992. Molecular basis of apparent isolated 17,20-lyase deficiency: compound heterozygous mutations in the C-terminal region (Arg(496)→Cys, Gln(461)→Stop) actually cause combined 17α-hydroxylase/17,20-lyase deficiency. Biochim. Biophys. Acta 1139: 275-79
    • (1992) Biochim. Biophys. Acta , vol.1139 , pp. 275-279
    • Yanase, T.1    Waterman, M.R.2    Zachmann, M.3    Winter, J.S.D.4    Simpson, E.R.5    Kagimoto, M.6
  • 129
    • 0028607480 scopus 로고
    • No evidence of mutations in the genes for type I and type II 3β-hydroxysteroid dehydrogenase (3βHSD) in nonclassical 3βHSD deficiency
    • Zerah M, Rhéaume E, Mani P, Schram P, Simard J, et al. 1994. No evidence of mutations in the genes for type I and type II 3β-hydroxysteroid dehydrogenase (3βHSD) in nonclassical 3βHSD deficiency. J. Clin. Endocrinol. Metab. 79:1811-17
    • (1994) J. Clin. Endocrinol. Metab. , vol.79 , pp. 1811-1817
    • Zerah, M.1    Rhéaume, E.2    Mani, P.3    Schram, P.4    Simard, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.