메뉴 건너뛰기




Volumn 338, Issue 1, 2005, Pages 483-490

Ascorbate stimulates monooxygenase-dependent steroidogenesis in adrenal zona glomerulosa

Author keywords

Adrenal cortex; Aldosterone formation; Aldosterone synthase cytochrome P450aldo; Ascorbic acid; Outer mitochondrial membrane cytochrome b; Semidehydroascorbic acid reductase; Steroidogenesis

Indexed keywords

ALDOSTERONE; ASCORBIC ACID; CORTICOSTERONE; CYTOCHROME B; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; SODIUM; UNSPECIFIC MONOOXYGENASE;

EID: 27544442734     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.08.156     Document Type: Article
Times cited : (7)

References (39)
  • 1
    • 0016586659 scopus 로고
    • Distribution of ascorbic acid, metabolites and analogues in man and animals
    • D. Horning Distribution of ascorbic acid, metabolites and analogues in man and animals Ann. NY Acad. Sci. 258 1975 103 118
    • (1975) Ann. NY Acad. Sci. , vol.258 , pp. 103-118
    • Horning, D.1
  • 2
    • 0022273382 scopus 로고
    • Ascorbic acid in endocrine systems
    • M. Levine, and K. Morita Ascorbic acid in endocrine systems Vitam. Horm. 42 1985 1 64
    • (1985) Vitam. Horm. , vol.42 , pp. 1-64
    • Levine, M.1    Morita, K.2
  • 3
    • 0001218860 scopus 로고
    • Ascorbate is an outstanding antioxidant in human blood plasma
    • B. Frei, L. England, and B.N. Ames Ascorbate is an outstanding antioxidant in human blood plasma Proc. Natl. Acad. Sci. USA 86 1989 6377 6381
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 6377-6381
    • Frei, B.1    England, L.2    Ames, B.N.3
  • 4
    • 0022459326 scopus 로고
    • The biochemical functions of ascorbic acid
    • S. England, and S. Seifter The biochemical functions of ascorbic acid Ann. Rev. Nutr. 6 1986 365 406
    • (1986) Ann. Rev. Nutr. , vol.6 , pp. 365-406
    • England, S.1    Seifter, S.2
  • 5
    • 0018853467 scopus 로고
    • Semidehydroascorbate as a product of the enzymic conversion of dopamine to norepinephrine
    • E.J. Diliberto Jr., and P.L. Alle Semidehydroascorbate as a product of the enzymic conversion of dopamine to norepinephrine Mol. Pharmacol. 17 1980 421 426
    • (1980) Mol. Pharmacol. , vol.17 , pp. 421-426
    • Diliberto Jr., E.J.1    Alle, P.L.2
  • 6
    • 85015328573 scopus 로고    scopus 로고
    • Steroid monooxygenases as markers for studying functional zonation in the adrenal cortex
    • F. Mitani, and Y. Ishimura Steroid monooxygenases as markers for studying functional zonation in the adrenal cortex Int. Cong. Ser. 1233 2002 99 114
    • (2002) Int. Cong. Ser. , vol.1233 , pp. 99-114
    • Mitani, F.1    Ishimura, Y.2
  • 7
    • 0024308494 scopus 로고
    • Isolation of aldosterone synthase cytochrome P450 from zona glomerulosa mitochondria of rat adrenal cortex
    • T. Ogishima, F. Mitani, and Y. Ishimura Isolation of aldosterone synthase cytochrome P450 from zona glomerulosa mitochondria of rat adrenal cortex J. Biol. Chem. 264 1989 10935 10938
    • (1989) J. Biol. Chem. , vol.264 , pp. 10935-10938
    • Ogishima, T.1    Mitani, F.2    Ishimura, Y.3
  • 8
    • 27544474943 scopus 로고
    • The relation of cholesterol and ascorbic acid to the secretion of the adrenal cortex
    • C.N.H. Long The relation of cholesterol and ascorbic acid to the secretion of the adrenal cortex Rec. Prog. Horm. Res. 1 1947 99 122
    • (1947) Rec. Prog. Horm. Res. , vol.1 , pp. 99-122
    • Long, C.N.H.1
  • 9
    • 0023269294 scopus 로고
    • The function of NADH-semidehydroascorbate reductase and ascorbic acid in corticosteroid hydroxylation
    • R.D. Natarajan, and B.W. Harding The function of NADH- semidehydroascorbate reductase and ascorbic acid in corticosteroid hydroxylation Mol. Cell Endocrinol. 53 1987 75 86
    • (1987) Mol. Cell Endocrinol. , vol.53 , pp. 75-86
    • Natarajan, R.D.1    Harding, B.W.2
  • 10
    • 0025082901 scopus 로고
    • Ascorbate as a source of reducing equivalents for the synthesis of aldosterone
    • K. Yanagibashi, Y. Kobayashi, and P.H. Hall Ascorbate as a source of reducing equivalents for the synthesis of aldosterone Biochem. Biophys. Res. Commun. 170 1990 1256 1262
    • (1990) Biochem. Biophys. Res. Commun. , vol.170 , pp. 1256-1262
    • Yanagibashi, K.1    Kobayashi, Y.2    Hall, P.H.3
  • 11
    • 0028844664 scopus 로고
    • Ascorbate depletion prevents aldosterone stimulation by sodium deficiency in the guinea pig
    • A. Redmann, K. Mobius, H.H. Hiller, W. Oelkers, and V. Bahr Ascorbate depletion prevents aldosterone stimulation by sodium deficiency in the guinea pig Eur. J. Endocrinol. 133 1995 499 506
    • (1995) Eur. J. Endocrinol. , vol.133 , pp. 499-506
    • Redmann, A.1    Mobius, K.2    Hiller, H.H.3    Oelkers, W.4    Bahr, V.5
  • 12
    • 0020614389 scopus 로고
    • The role of lipid peroxidation and biological antioxidants in the function of the adrenal cortex. Part2
    • J. Hornsby, and J.F. Crivello The role of lipid peroxidation and biological antioxidants in the function of the adrenal cortex. Part2 Mol. Cell Endocrinol. 30 1983 123 147
    • (1983) Mol. Cell Endocrinol. , vol.30 , pp. 123-147
    • Hornsby, J.1    Crivello, J.F.2
  • 13
    • 84981877416 scopus 로고
    • Role of ascorbic acid in microsomal electron transport and the possible relationship to hydroxylation reactions
    • H. Staudinger, K. Krisch, and S. Leonhauser Role of ascorbic acid in microsomal electron transport and the possible relationship to hydroxylation reactions Ann. NY Acad. Sci. 92 1961 159 207
    • (1961) Ann. NY Acad. Sci. , vol.92 , pp. 159-207
    • Staudinger, H.1    Krisch, K.2    Leonhauser, S.3
  • 18
    • 0026802110 scopus 로고
    • A missense mutation of l-gulono-γ-lactone oxidase causes the inability of scurvy-prone osteogenic disorder rats to synthesize l-ascorbic acid
    • T. Kawai, M. Nishikimi, T. Ozawa, and K. Yagi A missense mutation of l-gulono-γ-lactone oxidase causes the inability of scurvy-prone osteogenic disorder rats to synthesize l-ascorbic acid J. Biol. Chem. 267 1992 21973 21976
    • (1992) J. Biol. Chem. , vol.267 , pp. 21973-21976
    • Kawai, T.1    Nishikimi, M.2    Ozawa, T.3    Yagi, K.4
  • 19
    • 0028356387 scopus 로고
    • A novel cell layer without corticosteroid-synthesizing enzymes in rat adrenal cortex: Histochemical detection and possible physiological role
    • F. Mitani, H. Suzuki, J. Hata, T. Ogishima, H. Shimada, and Y. Ishimura A novel cell layer without corticosteroid-synthesizing enzymes in rat adrenal cortex: histochemical detection and possible physiological role Endocrinology 135 1994 431 438
    • (1994) Endocrinology , vol.135 , pp. 431-438
    • Mitani, F.1    Suzuki, H.2    Hata, J.3    Ogishima, T.4    Shimada, H.5    Ishimura, Y.6
  • 20
    • 0033371226 scopus 로고    scopus 로고
    • Studies on cytogenesis in adult rat adrenal cortex: Circadian and zonal variations and their modulation by adrenocorticotropic hormone
    • H. Miyamoto, F. Mitani, K. Mukai, M. Suematsu, and Y. Ishimura Studies on cytogenesis in adult rat adrenal cortex: circadian and zonal variations and their modulation by adrenocorticotropic hormone J. Biochem (Tokyo) 126 1999 1175 1183
    • (1999) J. Biochem (Tokyo) , vol.126 , pp. 1175-1183
    • Miyamoto, H.1    Mitani, F.2    Mukai, K.3    Suematsu, M.4    Ishimura, Y.5
  • 21
    • 77957010110 scopus 로고
    • Isolation of liver or kidney mitochondria
    • D. Johnson, and H. Lardy Isolation of liver or kidney mitochondria Method Enzymol. 10 1967 94 101
    • (1967) Method Enzymol. , vol.10 , pp. 94-101
    • Johnson, D.1    Lardy, H.2
  • 22
    • 0015508174 scopus 로고
    • Improved purification of bovine adrenal iron-sulfur protein
    • K. Suhara, S. Takemori, and M. Katagiri Improved purification of bovine adrenal iron-sulfur protein Biochim. Biophys. Acta 263 1972 272 278
    • (1972) Biochim. Biophys. Acta , vol.263 , pp. 272-278
    • Suhara, K.1    Takemori, S.2    Katagiri, M.3
  • 23
    • 0015511154 scopus 로고
    • The purification and properties of NADPH-adrenodoxin reductase from bovine adrenocortical mitochondria
    • K. Suhara, Y. Ikeda, S. Takemori, and M. Katagiri The purification and properties of NADPH-adrenodoxin reductase from bovine adrenocortical mitochondria FEBS Lett. 28 1972 45 47
    • (1972) FEBS Lett. , vol.28 , pp. 45-47
    • Suhara, K.1    Ikeda, Y.2    Takemori, S.3    Katagiri, M.4
  • 25
    • 0018342988 scopus 로고
    • Immunohistochemical localization of adrenodoxin and adrenodoxin reductase in bovine adrenal cortex
    • F. Mitani, Y. Ishimura, S. Izumi, and K. Watanabe Immunohistochemical localization of adrenodoxin and adrenodoxin reductase in bovine adrenal cortex Acta Endocrinol. 90 1979 317 327
    • (1979) Acta Endocrinol. , vol.90 , pp. 317-327
    • Mitani, F.1    Ishimura, Y.2    Izumi, S.3    Watanabe, K.4
  • 26
    • 0001409906 scopus 로고    scopus 로고
    • A practical method for determination of vitamin C in plasma by high-performance liquid chromatography with an electrochemical detector
    • K. Kakizaki, M. Yoshimura, M. Nishimuta, and T. Esashi A practical method for determination of vitamin C in plasma by high-performance liquid chromatography with an electrochemical detector J. Jpn. Soc. Nutr. Food Sci. 52 1999 107 111
    • (1999) J. Jpn. Soc. Nutr. Food Sci. , vol.52 , pp. 107-111
    • Kakizaki, K.1    Yoshimura, M.2    Nishimuta, M.3    Esashi, T.4
  • 27
    • 0014742071 scopus 로고
    • 5 reductase solubilized by lysosomes from rat liver microsomes
    • 5 reductase solubilized by lysosomes from rat liver microsomes J. Biochem (Tokyo) 67 1970 267 276
    • (1970) J. Biochem (Tokyo) , vol.67 , pp. 267-276
    • Takesue, S.1    Omura, T.2
  • 28
    • 0022973182 scopus 로고
    • Subcellular distribution of OM cytochrome b-mediated NADH- semidehydroascorbate reductase activity in rat liver
    • H. Nishino, and A. Ito Subcellular distribution of OM cytochrome b-mediated NADH-semidehydroascorbate reductase activity in rat liver J. Biochem (Tokyo) 100 1986 1523 1531
    • (1986) J. Biochem (Tokyo) , vol.100 , pp. 1523-1531
    • Nishino, H.1    Ito, A.2
  • 29
    • 78651165715 scopus 로고
    • The carbon monoxide-binding pigment of liver microsomes. 1. Evidence for its hemoprotein nature
    • T. Omura, and R. Sato The carbon monoxide-binding pigment of liver microsomes. 1. Evidence for its hemoprotein nature J. Biol. Chem. 239 1964 2370 2378
    • (1964) J. Biol. Chem. , vol.239 , pp. 2370-2378
    • Omura, T.1    Sato, R.2
  • 32
    • 0016698235 scopus 로고
    • Enzymic studies on adrenocortical deoxycorticosterone 11β-hydroxylase system
    • F. Mitani, A. Ichiyama, A. Masuda, and I. Ogata Enzymic studies on adrenocortical deoxycorticosterone 11β-hydroxylase system J. Biol. Chem. 250 1975 8010 8015
    • (1975) J. Biol. Chem. , vol.250 , pp. 8010-8015
    • Mitani, F.1    Ichiyama, A.2    Masuda, A.3    Ogata, I.4
  • 33
    • 0032474436 scopus 로고    scopus 로고
    • 11β catalyzing successive reactions from deoxycorticosterone to aldosterone
    • 11β catalyzing successive reactions from deoxycorticosterone to aldosterone Biochemistry 37 1998 8097 8104
    • (1998) Biochemistry , vol.37 , pp. 8097-8104
    • Imai, T.1    Yamazaki, T.2    Kominami, S.3
  • 34
    • 0030450422 scopus 로고    scopus 로고
    • Effects of long term stimulation of ACTH and angiotensin II-secretions on the rat adrenal cortex
    • F. Mitani, H. Miyamoto, K. Mukai, and Y. Ishimura Effects of long term stimulation of ACTH and angiotensin II-secretions on the rat adrenal cortex Endocrine Res. 22 1996 421 431
    • (1996) Endocrine Res. , vol.22 , pp. 421-431
    • Mitani, F.1    Miyamoto, H.2    Mukai, K.3    Ishimura, Y.4
  • 35
    • 0023144702 scopus 로고
    • A sensitive method for quantitation of steroid hydroxylase activities of individual P-450 in tissue homogenates
    • K. Suhara, K. Fujii, T. Tani, and M. Katagiri A sensitive method for quantitation of steroid hydroxylase activities of individual P-450 in tissue homogenates J. Steroid Biochem. 26 1987 113 119
    • (1987) J. Steroid Biochem. , vol.26 , pp. 113-119
    • Suhara, K.1    Fujii, K.2    Tani, T.3    Katagiri, M.4
  • 36
    • 0029125737 scopus 로고
    • Alteration of the adrenal antioxidant defense system during aging in rats
    • S. Azhar, L. Cao, and E. Reaven Alteration of the adrenal antioxidant defense system during aging in rats J. Clin. Invest. 96 1995 1414 1424
    • (1995) J. Clin. Invest. , vol.96 , pp. 1414-1424
    • Azhar, S.1    Cao, L.2    Reaven, E.3
  • 38
    • 0019423519 scopus 로고
    • Mechanism of dopamine-β-hydroxylation. Semidehydroascorbate as the enzymic oxidation product of ascorbate
    • E.J. Diliberto, and A.L. Allen Mechanism of dopamine-β- hydroxylation. Semidehydroascorbate as the enzymic oxidation product of ascorbate J. Biol. Chem. 256 1981 3385 3393
    • (1981) J. Biol. Chem. , vol.256 , pp. 3385-3393
    • Diliberto, E.J.1    Allen, A.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.