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Volumn 11, Issue 4, 1997, Pages 206-216

Enzymology of human cytosolic sulfotransferases

Author keywords

drug metabolism; human; steroid; sulfation; xenobiotics

Indexed keywords

ARYL SULFOTRANSFERASE; ESTROGEN; HYDROXYSTEROID; PRASTERONE; SULFOTRANSFERASE;

EID: 0030996250     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fasebj.11.4.9068609     Document Type: Review
Times cited : (538)

References (106)
  • 3
    • 0002422333 scopus 로고
    • (Bridges, J. W., and Chasseaud, L. F., eds) Taylor & Francis, London
    • Mulder, G. J. In Progress in Drug Metabolism (Bridges, J. W., and Chasseaud, L. F., eds) Vol. 8, pp. 35-100, Taylor & Francis, London (1984)
    • (1984) Progress in Drug Metabolism , vol.8 , pp. 35-100
    • Mulder, G.J.1
  • 6
  • 7
    • 0023942718 scopus 로고
    • Mechanism of action of minoxidil sulfate-induced vasodilatation: A role for increased K+ permeability
    • Meisheri, K. D., Cipkus, L. A., and Taylor, C. J. (1988) Mechanism of action of minoxidil sulfate-induced vasodilatation: A role for increased K+ permeability. J. Pharm. Exp. Ther. 245, 751-760
    • (1988) J. Pharm. Exp. Ther. , vol.245 , pp. 751-760
    • Meisheri, K.D.1    Cipkus, L.A.2    Taylor, C.J.3
  • 8
    • 0001547782 scopus 로고
    • Identification of enzymatically active sulfate as adenosine-3′-phosphate-5′-pbosphosulfate
    • Robbins, P. W., and Lippman, F. (1956) Identification of enzymatically active sulfate as adenosine-3′-phosphate-5′-pbosphosulfate. J. Am. Chem. Soc. 78, 2652-2654
    • (1956) J. Am. Chem. Soc. , vol.78 , pp. 2652-2654
    • Robbins, P.W.1    Lippman, F.2
  • 9
    • 0002576257 scopus 로고
    • Kinetics of conjugation reactions in eliminating organs
    • (Mulder G. J., ed) Taylor & Francis, London
    • Pang, K. S. (1990) Kinetics of conjugation reactions in eliminating organs. In Conjugation Reactions in Drug Metabolism (Mulder G. J., ed) pp. 5-39. Taylor & Francis, London
    • (1990) Conjugation Reactions in Drug Metabolism , pp. 5-39
    • Pang, K.S.1
  • 10
    • 0020632276 scopus 로고
    • Serum concentration and renal excretion by normal adults of inorganic sulfate after acetaminophen, ascorbic acid, and sodium sulfate
    • Morris, M. E., and Levy, G. (1983) Serum concentration and renal excretion by normal adults of inorganic sulfate after acetaminophen, ascorbic acid, and sodium sulfate. Clin. Pharm. Ther. 33, 529-535
    • (1983) Clin. Pharm. Ther. , vol.33 , pp. 529-535
    • Morris, M.E.1    Levy, G.2
  • 12
    • 0023851252 scopus 로고
    • Tyrosine sulfation and the secretory pathway
    • Huttner, W. B. (1988) Tyrosine sulfation and the secretory pathway. Annu. Rev. Physiol. 50, 363-376
    • (1988) Annu. Rev. Physiol. , vol.50 , pp. 363-376
    • Huttner, W.B.1
  • 13
    • 0023582046 scopus 로고
    • Tyrosine sulfation is a trans-Golgi specific modification
    • Baeuerle, P. A., and Huttner, W. B. (1987) Tyrosine sulfation is a trans-Golgi specific modification. J. Cell Biol. 105, 2655-2664
    • (1987) J. Cell Biol. , vol.105 , pp. 2655-2664
    • Baeuerle, P.A.1    Huttner, W.B.2
  • 14
    • 0000497607 scopus 로고
    • Sulfoconjugation: Role in neurotransmitter and secretory protein activity
    • Roth, J. A. (1986) Sulfoconjugation: role in neurotransmitter and secretory protein activity. Trends Pharmacol. Sci. 1, 404-407
    • (1986) Trends Pharmacol. Sci. , vol.1 , pp. 404-407
    • Roth, J.A.1
  • 16
    • 0014105002 scopus 로고
    • The metabolic clearance rates of dehydroepiandrosterone, testosterone and their sulphate esters in man, rat and rabbit
    • Wang, D. Y., Bulbrook, R. D., Sneddon, A., and Hamilton, T. (1967) The metabolic clearance rates of dehydroepiandrosterone, testosterone and their sulphate esters in man, rat and rabbit. J. Endocrinol. 38, 307-318
    • (1967) J. Endocrinol. , vol.38 , pp. 307-318
    • Wang, D.Y.1    Bulbrook, R.D.2    Sneddon, A.3    Hamilton, T.4
  • 17
    • 0016654243 scopus 로고
    • Dehydroepiandrosterone and dehydroepiandrosterone sulfate dynamics in obesity
    • Feher, T., and Halmy, L. (1975) Dehydroepiandrosterone and dehydroepiandrosterone sulfate dynamics in obesity. Can. J. Biochem. 53, 215-222
    • (1975) Can. J. Biochem. , vol.53 , pp. 215-222
    • Feher, T.1    Halmy, L.2
  • 18
    • 0019935052 scopus 로고
    • Asymmetric release of estrone and estradiol derived from labeled precursors in perfused human placentas
    • Gurpide, E., Marks, C., de Ziegler, D., Berk, P., and Brandes, J. (1982) Asymmetric release of estrone and estradiol derived from labeled precursors in perfused human placentas. Amer. J. Obstet. Gynecol. 144, 551-554
    • (1982) Amer. J. Obstet. Gynecol. , vol.144 , pp. 551-554
    • Gurpide, E.1    Marks, C.2    De Ziegler, D.3    Berk, P.4    Brandes, J.5
  • 19
    • 0021181906 scopus 로고
    • Age changes and sex differences in serum dehydroepiandrosterone sulfate concentrations throughout adulthood
    • Oentreich, N., Brind, J. L., Rizer, R. L., and Vogelman, J. H. (1984) Age changes and sex differences in serum dehydroepiandrosterone sulfate concentrations throughout adulthood. J. Cin. Endocr. & Metab. 59, 551-555
    • (1984) J. Cin. Endocr. & Metab. , vol.59 , pp. 551-555
    • Oentreich, N.1    Brind, J.L.2    Rizer, R.L.3    Vogelman, J.H.4
  • 20
    • 0029549896 scopus 로고
    • Biosynthesis of DHEAS by the human adrenal cortex and its age-related decline
    • Hornsby, P. J. (1995) Biosynthesis of DHEAS by the human adrenal cortex and its age-related decline. Ann. N.Y. Acad. Sci. 774, 29-46
    • (1995) Ann. N.Y. Acad. Sci. , vol.774 , pp. 29-46
    • Hornsby, P.J.1
  • 21
    • 0029554030 scopus 로고
    • Metabolism of dehydroepiandrosterone
    • Longcope, C. (1995) Metabolism of dehydroepiandrosterone. Ann. N.Y. Acad. Sci. 774, 143-148
    • (1995) Ann. N.Y. Acad. Sci. , vol.774 , pp. 143-148
    • Longcope, C.1
  • 22
    • 0025046185 scopus 로고
    • The effects of oral dehydroepiandrosterone on endocrine-metabolic parameters in postmenopausal women
    • Mortola, J. F., and Yen, S. S. C. (1990) The effects of oral dehydroepiandrosterone on endocrine-metabolic parameters in postmenopausal women. J. Clin. Endocr. & Metab. 71, 696-704
    • (1990) J. Clin. Endocr. & Metab. , vol.71 , pp. 696-704
    • Mortola, J.F.1    Yen, S.S.C.2
  • 23
    • 0024225368 scopus 로고
    • Dehydroepiandrosterone and structural analogs; a new class of cancer chemopreventive agents
    • Academic Press, New York
    • Schwartz, A. G., Witcomb, J. M., Nyce, J. W., Lewbart, M. L., and Pashko, L. L. (1988) Dehydroepiandrosterone and structural analogs; a new class of cancer chemopreventive agents. In Advances in Cancer Research, pp. 391-424, Academic Press, New York
    • (1988) Advances in Cancer Research , pp. 391-424
    • Schwartz, A.G.1    Witcomb, J.M.2    Nyce, J.W.3    Lewbart, M.L.4    Pashko, L.L.5
  • 24
    • 0022921501 scopus 로고
    • Prospective study of dehydroepiandrosterone sulfate, mortality, and cardiovascular disease
    • Barrett-Conner, E., Khaw, K. T., and Yen, S. S. C. A (1986) prospective study of dehydroepiandrosterone sulfate, mortality, and cardiovascular disease. New Engl. J. Med. 315, 1519-1524
    • (1986) New Engl. J. Med. , vol.315 , pp. 1519-1524
    • Barrett-Conner, E.1    Khaw, K.T.2    Yen, S.S.C.A.3
  • 25
    • 0029552972 scopus 로고
    • Neuronal actions of debydroepiandrosterone: Possible roles in brain development, aging, memory, and affect
    • Majewska, M. D. (1995) Neuronal actions of debydroepiandrosterone: Possible roles in brain development, aging, memory, and affect. Ann. N.Y. Acad. Sci. 774, 111-120
    • (1995) Ann. N.Y. Acad. Sci. , vol.774 , pp. 111-120
    • Majewska, M.D.1
  • 27
    • 0024401919 scopus 로고
    • Purification and characterization of human liver dehydroepiandrosterone sulfotransferase
    • Falany, C. N., Vazquez, M. E., and Kalb, J. M. (1989) Purification and characterization of human liver dehydroepiandrosterone sulfotransferase. Arch. Biochem. Biophys. 260, 641-646
    • (1989) Arch. Biochem. Biophys. , vol.260 , pp. 641-646
    • Falany, C.N.1    Vazquez, M.E.2    Kalb, J.M.3
  • 28
    • 0027051110 scopus 로고
    • Immunological characterization of dehydroepiandrosterone sulfotransferase from human liver and adrenals
    • Comer, K. A., and Falany, C. N. (1992) Immunological characterization of dehydroepiandrosterone sulfotransferase from human liver and adrenals. Mol. Pharmacol. 41, 645-651
    • (1992) Mol. Pharmacol. , vol.41 , pp. 645-651
    • Comer, K.A.1    Falany, C.N.2
  • 29
    • 0018345601 scopus 로고
    • Enzymatic synthesis of steroid sulphates. XII. Isolation of dehydroepiandrosterone sulphotransferase front human adrenals by affinity chromatography
    • Adams, J. B., and McDonald, D. (1979) Enzymatic synthesis of steroid sulphates. XII. Isolation of dehydroepiandrosterone sulphotransferase front human adrenals by affinity chromatography. Biochim. Biophys. Acta 567, 114-153
    • (1979) Biochim. Biophys. Acta , vol.567 , pp. 114-153
    • Adams, J.B.1    McDonald, D.2
  • 30
    • 0026739431 scopus 로고
    • Molecular cloning of the alcohol/hydroxysteroid form (hSTa) of sulfotransferase from human liver
    • Kong, A.-N. T., Yang, L., Ma, M., Tao, D., and Bjornsson, T. D. (1992) Molecular cloning of the alcohol/hydroxysteroid form (hSTa) of sulfotransferase from human liver. Biochem. Biophys. Res. Commun. 187, 448-454
    • (1992) Biochem. Biophys. Res. Commun. , vol.187 , pp. 448-454
    • Kong, A.-N.T.1    Yang, L.2    Ma, M.3    Tao, D.4    Bjornsson, T.D.5
  • 31
    • 0027475375 scopus 로고
    • Cloning and expression of human liver dehydroepiandrosterone sulfotransferase
    • Comer, K. A., Falany, J. L., and Falany, C. M. (1993) Cloning and expression of human liver dehydroepiandrosterone sulfotransferase. Biochem. J. 289, 233-240
    • (1993) Biochem. J. , vol.289 , pp. 233-240
    • Comer, K.A.1    Falany, J.L.2    Falany, C.M.3
  • 32
    • 0029051063 scopus 로고
    • Human fetal adrenal hydroxysteroid sulphotransferase: cDNA cloning, stable expression in V79 cells and functional characterization of the expressed enzyme
    • Forbes, K. J., Hagen, M., Glatt, H., Hume, R., and Coughtrie, M. W. H. (1995) Human fetal adrenal hydroxysteroid sulphotransferase: cDNA cloning, stable expression in V79 cells and functional characterization of the expressed enzyme. Mol. Cell. Endocrinol. 112, 53-60
    • (1995) Mol. Cell. Endocrinol. , vol.112 , pp. 53-60
    • Forbes, K.J.1    Hagen, M.2    Glatt, H.3    Hume, R.4    Coughtrie, M.W.H.5
  • 34
    • 0028969206 scopus 로고
    • Dehydroepiandrosterone sulfotransferase gene (STD): Localization to human chromosome 19q13.3
    • Otterness, D., Mohrenweiser, H. W., Brandiff, B. F., and Weinshilboum, R. M. (1995) Dehydroepiandrosterone sulfotransferase gene (STD): Localization to human chromosome 19q13.3. Cytogenet. Cell Genet. 70, 15-52
    • (1995) Cytogenet. Cell Genet. , vol.70 , pp. 15-52
    • Otterness, D.1    Mohrenweiser, H.W.2    Brandiff, B.F.3    Weinshilboum, R.M.4
  • 35
    • 0028172839 scopus 로고
    • Biochemistry and molecular biology of drug-metabolizing sulfotransferases
    • Matsui, M., and Homma, H. (1994) Biochemistry and molecular biology of drug-metabolizing sulfotransferases. Int. J. Biochem. 26, 1237-1247
    • (1994) Int. J. Biochem. , vol.26 , pp. 1237-1247
    • Matsui, M.1    Homma, H.2
  • 36
    • 0024580798 scopus 로고
    • Bile acid sulfotransferase I from rat liver sulfates bile acids and 3-hydroxy steroids: Purification, N-terminal amino acid sequence, and kinetic properties
    • Barnes, S., Buchina, E. S., King, R. J., McBurnett, T., and Taylor, K. B. (1989) Bile acid sulfotransferase I from rat liver sulfates bile acids and 3-hydroxy steroids: purification, N-terminal amino acid sequence, and kinetic properties. J. Lipid Res. 30, 529-540
    • (1989) J. Lipid Res. , vol.30 , pp. 529-540
    • Barnes, S.1    Buchina, E.S.2    King, R.J.3    McBurnett, T.4    Taylor, K.B.5
  • 37
    • 0028322264 scopus 로고
    • Studies on rat hydroxysteroid sulfotransferase -immunochemistry, development and pI varients
    • Homma, H., Nakagome, I., Kamakura, M., Hirota, M., Takahashi, M., and Matsui, M. (1994) Studies on rat hydroxysteroid sulfotransferase -immunochemistry, development and pI varients. Chem.-Bio. Interact. 92, 15-24
    • (1994) Chem.-Bio. Interact. , vol.92 , pp. 15-24
    • Homma, H.1    Nakagome, I.2    Kamakura, M.3    Hirota, M.4    Takahashi, M.5    Matsui, M.6
  • 38
    • 0027027396 scopus 로고
    • Bioactivation of 7-hydroxymethyl-12-methylbenz(a)anthracene by rat liver bile acid sulfotransferase I
    • Falany, C. N., Wheeler, J., Coward, L., Keehan, D., Falany, J. L., and Barnes, S. (1992) Bioactivation of 7-hydroxymethyl-12-methylbenz(a)anthracene by rat liver bile acid sulfotransferase I. J. Biochem. Toxicol. 7, 241-248
    • (1992) J. Biochem. Toxicol. , vol.7 , pp. 241-248
    • Falany, C.N.1    Wheeler, J.2    Coward, L.3    Keehan, D.4    Falany, J.L.5    Barnes, S.6
  • 39
    • 0025851901 scopus 로고
    • Age and gender-related gene expression of hydroxysteroid sulfotransferase-a in rat liver
    • Runge-Morris, M., and Wilusz, J. (1991) Age and gender-related gene expression of hydroxysteroid sulfotransferase-a in rat liver. Biochem. Biophys. Res. Commun. 175, 1051-1056
    • (1991) Biochem. Biophys. Res. Commun. , vol.175 , pp. 1051-1056
    • Runge-Morris, M.1    Wilusz, J.2
  • 40
    • 0023912623 scopus 로고
    • Dual regulation of 3β-hydroxysteroid dehydrogenase, 17X-hydroxylase, and dehydroepiandrosterone sulfotransferase by adenosine 3′,5′-monophosphate and activators of protein kinase C in cultured human adrenocortical cells
    • McAllister, J. M., and Hornsby, P. J. (1988) Dual regulation of 3β-hydroxysteroid dehydrogenase, 17X-hydroxylase, and dehydroepiandrosterone sulfotransferase by adenosine 3′,5′-monophosphate and activators of protein kinase C in cultured human adrenocortical cells. Endocrinology 122, 2012-2018
    • (1988) Endocrinology , vol.122 , pp. 2012-2018
    • McAllister, J.M.1    Hornsby, P.J.2
  • 41
    • 0028037804 scopus 로고
    • Bile salt sulfotransferase activity in the liver of cholestatic infants
    • Obinata, K., Nemeth, A., Ellin, A., and Strandvik, B. (1994) Bile salt sulfotransferase activity in the liver of cholestatic infants. Scand. J. Clin. Lab. Invest. 54, 285-290
    • (1994) Scand. J. Clin. Lab. Invest. , vol.54 , pp. 285-290
    • Obinata, K.1    Nemeth, A.2    Ellin, A.3    Strandvik, B.4
  • 42
    • 0027520742 scopus 로고
    • Cholesterol sulfation in human liver: Catalysis by dehydropeiandrosterone sulfotransferase
    • Aksoy, I. A., Otterness, D. M., and Weinshilboum, R. M. (1993) Cholesterol sulfation in human liver: catalysis by dehydropeiandrosterone sulfotransferase. Drug Metab. Dispos. 21, 268-276
    • (1993) Drug Metab. Dispos. , vol.21 , pp. 268-276
    • Aksoy, I.A.1    Otterness, D.M.2    Weinshilboum, R.M.3
  • 43
    • 0021077285 scopus 로고
    • Sulfurylation of deoxycorticosterone in human fetal tissues
    • Casey, M. L., and MacDonald, P. C. (1983) Sulfurylation of deoxycorticosterone in human fetal tissues. J. steroid Biochem. 19, 1403-1406
    • (1983) J. Steroid Biochem. , vol.19 , pp. 1403-1406
    • Casey, M.L.1    MacDonald, P.C.2
  • 44
    • 1842306849 scopus 로고
    • Sulphation of bile acids
    • (Bianchi, L., Gerok, W., and Stichinger, K., eds) Universily Park Press, Baltimore, Md
    • Stiehl, A., Czygan, P., Frohling, W., Liersch, M., and Kommerell, B. (1977) Sulphation of bile acids. In Liver and Bile (Bianchi, L., Gerok, W., and Stichinger, K., eds) pp. 129-138. Universily Park Press, Baltimore, Md.
    • (1977) Liver and Bile , pp. 129-138
    • Stiehl, A.1    Czygan, P.2    Frohling, W.3    Liersch, M.4    Kommerell, B.5
  • 46
    • 1842263379 scopus 로고
    • Metabolism of bile acids
    • (McIntyre, N., Benhamon, J. P., Bircher, J., Rizzeito, M., and Rhodes, J., eds) Oxford University Press, Oxford, U.K.
    • Barnes, S. (1991) Metabolism of bile acids. In Oxford Textbook of Clinical Hepatology (McIntyre, N., Benhamon, J. P., Bircher, J., Rizzeito, M., and Rhodes, J., eds) pp. 115-129, Oxford University Press, Oxford, U.K.
    • (1991) Oxford Textbook of Clinical Hepatology , pp. 115-129
    • Barnes, S.1
  • 47
    • 0021828106 scopus 로고
    • Purification and characterization of a dopamine-sulfating form of phenol sulfotransferase from human brain
    • Whittemore, R. M., Pearce, L. B., and Roth, J. A. (1985) Purification and characterization of a dopamine-sulfating form of phenol sulfotransferase from human brain. Biochemistry 24, 2477-2482
    • (1985) Biochemistry , vol.24 , pp. 2477-2482
    • Whittemore, R.M.1    Pearce, L.B.2    Roth, J.A.3
  • 48
    • 0024340713 scopus 로고
    • Immunological characterization of human phenol sulfotransferase
    • Heroux, J. A., Falany, C. N., and Roth, J. A. (1989) Immunological characterization of human phenol sulfotransferase. Mol. Pharmacol. 36, 29-33
    • (1989) Mol. Pharmacol. , vol.36 , pp. 29-33
    • Heroux, J.A.1    Falany, C.N.2    Roth, J.A.3
  • 49
    • 0027433251 scopus 로고
    • Human liver dehydroepiandrosterone sulfotransferase: Nature and extent of individual variation
    • Aksoy, I. A., Sochorova, V., and Weinshilboum, R. M. (1993) Human liver dehydroepiandrosterone sulfotransferase: nature and extent of individual variation. Clin. Pharmacol. & Ther. 54, 498-506
    • (1993) Clin. Pharmacol. & Ther. , vol.54 , pp. 498-506
    • Aksoy, I.A.1    Sochorova, V.2    Weinshilboum, R.M.3
  • 50
    • 0028078591 scopus 로고
    • Dehydroepiandrosterone sulfotransferase in the developing human fetus: Quantitative biochemical and immunological characterisation of the hepatic, renal and adrenal enzymes
    • Barker, E. V., Hume, R., Hallas, A., and Coughtrie, M. W. H. (1994) Dehydroepiandrosterone sulfotransferase in the developing human fetus: quantitative biochemical and immunological characterisation of the hepatic, renal and adrenal enzymes. Endocrinology 134, 982-989
    • (1994) Endocrinology , vol.134 , pp. 982-989
    • Barker, E.V.1    Hume, R.2    Hallas, A.3    Coughtrie, M.W.H.4
  • 51
    • 0027958438 scopus 로고
    • Immunohistochemical localization of dehydroepiandrosterone sulfotransferase in human fetal tissues
    • Parker, C. R., Falany, C. N., Stockard, C. R., Stankovic, A. K., and Grizzle, W. E. (1993) Immunohistochemical localization of dehydroepiandrosterone sulfotransferase in human fetal tissues. J. Clin. Endocr. & Metab. 78, 234-236
    • (1993) J. Clin. Endocr. & Metab. , vol.78 , pp. 234-236
    • Parker, C.R.1    Falany, C.N.2    Stockard, C.R.3    Stankovic, A.K.4    Grizzle, W.E.5
  • 52
    • 0020661270 scopus 로고
    • Dehydroepiandrosterone sulfotransferase localization in human adrenal glands: A light and electron microscopic study
    • Kennerson, A. R., McDonald, D. A., and Adams, J. B. (1983) Dehydroepiandrosterone sulfotransferase localization in human adrenal glands: a light and electron microscopic study. J. Clin. Endocr. & Metab. 56, 786-790
    • (1983) J. Clin. Endocr. & Metab. , vol.56 , pp. 786-790
    • Kennerson, A.R.1    McDonald, D.A.2    Adams, J.B.3
  • 53
    • 0029549968 scopus 로고
    • Human dehydroepiandrosterone sulfotransferase: Purification, molecular cloning, and characterization
    • Falany, C. N., Comer, K. A., Dooley, T. P., and Glatt, H. (1995) Human dehydroepiandrosterone sulfotransferase: purification, molecular cloning, and characterization. Ann. N.Y. Acad. Sci. 774, 59-72
    • (1995) Ann. N.Y. Acad. Sci. , vol.774 , pp. 59-72
    • Falany, C.N.1    Comer, K.A.2    Dooley, T.P.3    Glatt, H.4
  • 54
    • 0002590138 scopus 로고
    • The Adrenal Cortex
    • (Felig, P., Baxter, J. D., Broadus, A. E., and Frohman, L. A., eds) McGraw-Hill, New York
    • Baxter, J. D., and Tyrrell, J. B. (1987) The Adrenal Cortex. In Endocrinology and Metabolism (Felig, P., Baxter, J. D., Broadus, A. E., and Frohman, L. A., eds) pp. 511-632, McGraw-Hill, New York
    • (1987) Endocrinology and Metabolism , pp. 511-632
    • Baxter, J.D.1    Tyrrell, J.B.2
  • 55
    • 0001861949 scopus 로고
    • Endocrine implications of endometrial estrogen sulfurylation
    • (Jasonni, V., M., et al., eds) Raven Press, New York
    • Brooks, S. C., Christensen, C., Meyers, S., Corombos, J., and Pack, B. A. (1983) Endocrine implications of endometrial estrogen sulfurylation. In Steroids and Endometrial Cancer (Jasonni, V., M., et al., eds) pp. 145-155, Raven Press, New York
    • (1983) Steroids and Endometrial Cancer , pp. 145-155
    • Brooks, S.C.1    Christensen, C.2    Meyers, S.3    Corombos, J.4    Pack, B.A.5
  • 56
    • 0026515042 scopus 로고
    • Regulation of steroid hormone action in target cells by specific hormone-inactivating enzymes
    • Roy, A. K. (1992) Regulation of steroid hormone action in target cells by specific hormone-inactivating enzymes. Proc. Soc. Exp. Biol. Med. 199, 265-272
    • (1992) Proc. Soc. Exp. Biol. Med. , vol.199 , pp. 265-272
    • Roy, A.K.1
  • 58
    • 0029053067 scopus 로고
    • Bacterial expression and characterization of a cDNA for human liver estrogen sulfotransferase
    • Falany, C. N., Krasnykh, V., and Falany, J. L. (1995) Bacterial expression and characterization of a cDNA for human liver estrogen sulfotransferase. J. Steroid Biochem. Mol. Biol. 52, 529-539
    • (1995) J. Steroid Biochem. Mol. Biol. , vol.52 , pp. 529-539
    • Falany, C.N.1    Krasnykh, V.2    Falany, J.L.3
  • 59
    • 0010556002 scopus 로고
    • Human liver estrogen sulfotransferase (EST): Polymerase chain reaction (PCR) cloning of cDNA
    • Aksoy, I. A., Wood, T. C., and Weinshilboum, R. M. (1993) Human liver estrogen sulfotransferase (EST): polymerase chain reaction (PCR) cloning of cDNA. Biochem. Biophys. Res. Commun. 4, 181
    • (1993) Biochem. Biophys. Res. Commun. , vol.4 , pp. 181
    • Aksoy, I.A.1    Wood, T.C.2    Weinshilboum, R.M.3
  • 60
    • 0021020861 scopus 로고
    • Estrogen sulfatase and estrogen sulfotransferase in human primary mammary carcinoma
    • Tseng, L., Mazella, J., Lee, L. U., and Stone, M. L. (1983) Estrogen sulfatase and estrogen sulfotransferase in human primary mammary carcinoma. J. Steroid Biochem. 19, 1413-1417
    • (1983) J. Steroid Biochem. , vol.19 , pp. 1413-1417
    • Tseng, L.1    Mazella, J.2    Lee, L.U.3    Stone, M.L.4
  • 61
    • 0021217855 scopus 로고
    • Characterization of cytosolic estrogen sulfotransferase from RL95-2 endometrial cancer cells
    • 1984
    • Grosso, D. S., and Way, D. L. (1984) Characterization of cytosolic estrogen sulfotransferase from RL95-2 endometrial cancer cells. J. Clin. Endocr. & Metab. 59, 829-833 (1984)
    • (1984) J. Clin. Endocr. & Metab. , vol.59 , pp. 829-833
    • Grosso, D.S.1    Way, D.L.2
  • 62
    • 0029098573 scopus 로고
    • Human estrogen sulfotransferase gene (STE): Cloning, structure and chromosomal localization
    • Her, C., Aksoy, I. A., and Weinshilboum, R. M. (1995) Human estrogen sulfotransferase gene (STE): Cloning, structure and chromosomal localization. Genomics 29, 16-23
    • (1995) Genomics , vol.29 , pp. 16-23
    • Her, C.1    Aksoy, I.A.2    Weinshilboum, R.M.3
  • 63
    • 0029916538 scopus 로고    scopus 로고
    • Expression of cytosolic sulfotransferases in normal mammary epithelial cells and breast cancer cell lines
    • Falany, J. L., and Falany, C. N. (1996) Expression of cytosolic sulfotransferases in normal mammary epithelial cells and breast cancer cell lines. Cancer Res. 56. 1551-1555
    • (1996) Cancer Res. , vol.56 , pp. 1551-1555
    • Falany, J.L.1    Falany, C.N.2
  • 64
    • 0020414704 scopus 로고
    • Induction of estrogen sulfotransferase in the human endometrium by progesterone in organ culture
    • Clarke, C. L., Adams, J. B., and Wren, B. G. (1982) Induction of estrogen sulfotransferase in the human endometrium by progesterone in organ culture. J. Clin. Endocrin. Metab. 55, 70-75
    • (1982) J. Clin. Endocrin. Metab. , vol.55 , pp. 70-75
    • Clarke, C.L.1    Adams, J.B.2    Wren, B.G.3
  • 65
    • 0018772667 scopus 로고
    • The cyclic relationship of estrogen sulfurylation to the nuclear receptor level in human endometrial curettings
    • Pack, B. A., Tovar, R., Booth, E., and Brooks, S. C. (1979) The cyclic relationship of estrogen sulfurylation to the nuclear receptor level in human endometrial curettings. J. Clin. Endocr. & Metab. 48, 420424
    • (1979) J. Clin. Endocr. & Metab. , vol.48 , pp. 420424
    • Pack, B.A.1    Tovar, R.2    Booth, E.3    Brooks, S.C.4
  • 66
    • 0018744903 scopus 로고
    • Estradiol metabolism in isolated human endometrial epithelial glands and stromal cells
    • Liu, H.-C., and Tseng, L. (1979) Estradiol metabolism in isolated human endometrial epithelial glands and stromal cells. Endocrinology 104, 1674-1694
    • (1979) Endocrinology , vol.104 , pp. 1674-1694
    • Liu, H.-C.1    Tseng, L.2
  • 67
    • 0029976195 scopus 로고    scopus 로고
    • Regulation of estrogen sulfotransferase in human endometrial adenocarcinoma cells by progesterone
    • Falany, J. L., and Falany, C. N. (1996) Regulation of estrogen sulfotransferase in human endometrial adenocarcinoma cells by progesterone. Endocrinology 137, 1395-1401
    • (1996) Endocrinology , vol.137 , pp. 1395-1401
    • Falany, J.L.1    Falany, C.N.2
  • 68
    • 0018351146 scopus 로고
    • Localization and characterization of phenol sulfotransferase in human platelets
    • Hart, R. F., Renskers, K. J., Nelson, E. B., and Roth, J. A. (1979) Localization and characterization of phenol sulfotransferase in human platelets. Life Sci. 24, 125-130
    • (1979) Life Sci. , vol.24 , pp. 125-130
    • Hart, R.F.1    Renskers, K.J.2    Nelson, E.B.3    Roth, J.A.4
  • 69
    • 0022459257 scopus 로고
    • Phenol Sulfotransferase in Humans: Properties, regulation, and function
    • Weinshilboum, R. M. (1986) Phenol Sulfotransferase in Humans: properties, regulation, and function. Federation Proc. 45, 2223-2228
    • (1986) Federation Proc. , vol.45 , pp. 2223-2228
    • Weinshilboum, R.M.1
  • 70
    • 0028245602 scopus 로고
    • Identification of a new adult human liver sulfotransferase with specificity for endogenous and xenobiotic estrogens
    • Forbes-Bamforth, K. J., and Coughtrie, M. W. H. (1994) Identification of a new adult human liver sulfotransferase with specificity for endogenous and xenobiotic estrogens. Biochem. Biophys. Res. Commun. 198, 707-711
    • (1994) Biochem. Biophys. Res. Commun. , vol.198 , pp. 707-711
    • Forbes-Bamforth, K.J.1    Coughtrie, M.W.H.2
  • 71
    • 0028112007 scopus 로고
    • Functional characterization of two human sulphotransferase cDNAs that encode monoamine- and phenol-sulphating forms of phenol sulphotransferase: Substrate kinetics, thermal-stability and inhibitor-sensitivity studies
    • Veronese, M. E., Burgess, W., Zhu, X., and McManus, M. E. (1994) Functional characterization of two human sulphotransferase cDNAs that encode monoamine- and phenol-sulphating forms of phenol sulphotransferase: substrate kinetics, thermal-stability and inhibitor-sensitivity studies. Biochem. J. 302, 497-502
    • (1994) Biochem. J. , vol.302 , pp. 497-502
    • Veronese, M.E.1    Burgess, W.2    Zhu, X.3    McManus, M.E.4
  • 72
    • 0029013183 scopus 로고
    • Primary structures and properties of two related forms of aryl sulfotransferase in human liver
    • Ozawa, S. H., Nagata, K., Shimada, M., Ueda, M., Tsuzuki, T., Yamazoe, Y., and Kata, R. (1995) Primary structures and properties of two related forms of aryl sulfotransferase in human liver. Pharmacogenetics 5, S135-S140
    • (1995) Pharmacogenetics , vol.5
    • Ozawa, S.H.1    Nagata, K.2    Shimada, M.3    Ueda, M.4    Tsuzuki, T.5    Yamazoe, Y.6    Kata, R.7
  • 73
    • 0028848909 scopus 로고
    • Homodimeric and heterodimeric aryl sulfotransferases catalyze the sulfuric acid esterification of N-hydroxy-2-acetylaminofluorene
    • Kiehlbauch, C. C., Lam, Y. F., and Ringer, D. P. (1995) Homodimeric and heterodimeric aryl sulfotransferases catalyze the sulfuric acid esterification of N-hydroxy-2-acetylaminofluorene. J. Biol. Chem. 270, 18941-18947
    • (1995) J. Biol. Chem. , vol.270 , pp. 18941-18947
    • Kiehlbauch, C.C.1    Lam, Y.F.2    Ringer, D.P.3
  • 74
    • 0023812901 scopus 로고
    • Physical characterization of a monoamine-sulfating form of phenol sulfotransferase from human platelets
    • Heroux, J. A., and Roth, J. A. (1988) Physical characterization of a monoamine-sulfating form of phenol sulfotransferase from human platelets. Mol. Pharmacol. 34, 29-33
    • (1988) Mol. Pharmacol. , vol.34 , pp. 29-33
    • Heroux, J.A.1    Roth, J.A.2
  • 75
    • 0025230526 scopus 로고
    • Purification and characterization of human liver phenol-sulfating phenol sulfotransferase
    • Falany, C. N., Vazquez, M. E., Heroux, J. A., and Roth, J. A. (1990) Purification and characterization of human liver phenol-sulfating phenol sulfotransferase. Arch. Biochem. Biophys. 278, 312-318
    • (1990) Arch. Biochem. Biophys. , vol.278 , pp. 312-318
    • Falany, C.N.1    Vazquez, M.E.2    Heroux, J.A.3    Roth, J.A.4
  • 76
    • 0028334382 scopus 로고
    • Human liver thermolabile phenol sulfotransferase: cDNA cloning, expression and characterization
    • Wood, T. C., Aksoy, I. A., Aksoy, S., and Weinshilboum, R. M. (1994) Human liver thermolabile phenol sulfotransferase: cDNA cloning, expression and characterization. Biochem. Biopys. Res. Commun. 198, 1119-1127
    • (1994) Biochem. Biopys. Res. Commun. , vol.198 , pp. 1119-1127
    • Wood, T.C.1    Aksoy, I.A.2    Aksoy, S.3    Weinshilboum, R.M.4
  • 77
    • 0029093466 scopus 로고
    • Bacterial expression and kinetic characterization of the human monoamine-sulfating form of phenol sulfotransferase
    • Ganguly, T. G., Krasnykh, V., and Falany, C. N. (1995) Bacterial expression and kinetic characterization of the human monoamine-sulfating form of phenol sulfotransferase. Drug Metab. Dispos. 23, 945-950
    • (1995) Drug Metab. Dispos. , vol.23 , pp. 945-950
    • Ganguly, T.G.1    Krasnykh, V.2    Falany, C.N.3
  • 78
    • 0028981772 scopus 로고
    • Activation of benzylic alcohols to mutagens by rat and human sulfotransferases expressed in E. coli
    • Glatt, H., Pauly, K., Czich, A., Falany, J. L., and Falany, C. N. (1995) Activation of benzylic alcohols to mutagens by rat and human sulfotransferases expressed in E. coli. Eur. J. Pharmacol. 293, 173-181
    • (1995) Eur. J. Pharmacol. , vol.293 , pp. 173-181
    • Glatt, H.1    Pauly, K.2    Czich, A.3    Falany, J.L.4    Falany, C.N.5
  • 81
    • 0023943785 scopus 로고
    • Triiodothyronine: A substrate for the thermostable and thermolabile forms of human phenol sulfotransferase
    • Young, W. F., Gorman, C. A., and Weinshilboum, R. M. (1988) Triiodothyronine: a substrate for the thermostable and thermolabile forms of human phenol sulfotransferase. Endocrinology 122, 1816-1824
    • (1988) Endocrinology , vol.122 , pp. 1816-1824
    • Young, W.F.1    Gorman, C.A.2    Weinshilboum, R.M.3
  • 83
    • 0025193236 scopus 로고
    • Sulfation of minoxidil by human liver phenol sulfotransferase
    • Falany, C. N., and Kerl, E. A. (1990) Sulfation of minoxidil by human liver phenol sulfotransferase. Biochem. Pharmacol. 40, 1027-1032
    • (1990) Biochem. Pharmacol. , vol.40 , pp. 1027-1032
    • Falany, C.N.1    Kerl, E.A.2
  • 84
    • 0026520917 scopus 로고
    • Stereoselective sulfate conjugation of 4-hydroxypropranolol and terbutaline by human liver sulfotransferases
    • Walle, T., and Walle, U. K. (1992) Stereoselective sulfate conjugation of 4-hydroxypropranolol and terbutaline by human liver sulfotransferases. Drug Metab. Dispos. 20, 333-336
    • (1992) Drug Metab. Dispos. , vol.20 , pp. 333-336
    • Walle, T.1    Walle, U.K.2
  • 87
    • 0029027552 scopus 로고
    • Characterization of recombinant human liver thermolabile phenol sulfotransferase with minoxidil as the substrate
    • Kudlecek, P. E., Clemens, D. L., and Anderson, R. J. (1995) Characterization of recombinant human liver thermolabile phenol sulfotransferase with minoxidil as the substrate. Biochem. Biophys. Res. Commun. 210, 363-369
    • (1995) Biochem. Biophys. Res. Commun. , vol.210 , pp. 363-369
    • Kudlecek, P.E.1    Clemens, D.L.2    Anderson, R.J.3
  • 89
    • 0030021617 scopus 로고    scopus 로고
    • Role of sulfate in thyroid hormone sulfation
    • Visser, T. J. Role of sulfate in thyroid hormone sulfation. Eur. J. Endocrinol. 134, 12-14 (1996)
    • (1996) Eur. J. Endocrinol. , vol.134 , pp. 12-14
    • Visser, T.J.1
  • 90
    • 0020579139 scopus 로고
    • Thermolabile and thermostable human platelet phenol sulfotransferase: Substrate specificity and physical separation
    • Reiter, C., Mwaluko, G., Dunnette, J., Van Loon, J., and Weinshilboum, R. (1983) Thermolabile and thermostable human platelet phenol sulfotransferase: Substrate specificity and physical separation. Naunyn-Schmied. Arch. Pharmacol. 324, 140-147
    • (1983) Naunyn-Schmied. Arch. Pharmacol. , vol.324 , pp. 140-147
    • Reiter, C.1    Mwaluko, G.2    Dunnette, J.3    Van Loon, J.4    Weinshilboum, R.5
  • 91
    • 0025129340 scopus 로고
    • Sulfotransferase pharmacogenetics
    • Weinshilboum, R. (1990) Sulfotransferase pharmacogenetics. Pharmacol. & Ther. 45, 93-107
    • (1990) Pharmacol. & Ther. , vol.45 , pp. 93-107
    • Weinshilboum, R.1
  • 92
    • 0023735827 scopus 로고
    • Phenol sulfotransferase inheritance
    • Weinshilboum, R. (1988) Phenol sulfotransferase inheritance. Cell. Mol. Neurol. 8, 27-34
    • (1988) Cell. Mol. Neurol. , vol.8 , pp. 27-34
    • Weinshilboum, R.1
  • 93
    • 0020430630 scopus 로고
    • Genetic study of platelet phenol sulfotransferase activity in normal and schizophrenic twins
    • Reveley, A. M., Carter, S. M. B., Revely, M. A., and Sandler, M. A. (1982/1983) genetic study of platelet phenol sulfotransferase activity in normal and schizophrenic twins. J. Psychiatr. Res. 17, 303-307
    • (1982) J. Psychiatr. Res. , vol.17 , pp. 303-307
    • Reveley, A.M.1    Carter, S.M.B.2    Revely, M.A.3    Sandler, M.A.4
  • 94
    • 0023272095 scopus 로고
    • Human liver phenol sulfotransferase: Assay conditions, biochemical properties and partial purification of isozymes of the thermostable form
    • Campbell, N. R. C., Van Loon, J. A., and Weinshilboum, R. M. (1987) Human liver phenol sulfotransferase: Assay conditions, biochemical properties and partial purification of isozymes of the thermostable form. Biochem. Pharmacol. 36, 1435-1446
    • (1987) Biochem. Pharmacol. , vol.36 , pp. 1435-1446
    • Campbell, N.R.C.1    Van Loon, J.A.2    Weinshilboum, R.M.3
  • 96
    • 0028898346 scopus 로고
    • Human platelet phenolsulfotransferases: cDNA cloning, stable expression in V79 cells and identification of a novel allelic varient of the phenol-sulfating form
    • Jones, A. L., Hagen, M., Coughtrie, M. W. H., Roberts, R. C., and Glatt, H. (1995) Human platelet phenolsulfotransferases: cDNA cloning, stable expression in V79 cells and identification of a novel allelic varient of the phenol-sulfating form. Biochem. Biophys. Res. Commun. 208, 855-862
    • (1995) Biochem. Biophys. Res. Commun. , vol.208 , pp. 855-862
    • Jones, A.L.1    Hagen, M.2    Coughtrie, M.W.H.3    Roberts, R.C.4    Glatt, H.5
  • 97
    • 0024330810 scopus 로고
    • Sulfation pharmacogenetics: Correlation of human platelet and small intestinal phenol sulfotransferase
    • Sundaram, R. S., Van Loon, J. A., Tucker, R., and Weinshilboum, R. M. (1989) Sulfation pharmacogenetics: correlation of human platelet and small intestinal phenol sulfotransferase. Clin. Pharmacol. & Ther. 46, 501-509
    • (1989) Clin. Pharmacol. & Ther. , vol.46 , pp. 501-509
    • Sundaram, R.S.1    Van Loon, J.A.2    Tucker, R.3    Weinshilboum, R.M.4
  • 98
    • 0021960624 scopus 로고
    • Human phenol sulfotransferase: Correlation of brain and platelet activities
    • Young, W. F., Jr., Laws, E. R., Sharbrough, F. W., and Weinshilboum, R. M. (1985) Human phenol sulfotransferase: correlation of brain and platelet activities. J. Neurochem. 44, 1131-1137
    • (1985) J. Neurochem. , vol.44 , pp. 1131-1137
    • Young Jr., W.F.1    Laws, E.R.2    Sharbrough, F.W.3    Weinshilboum, R.M.4
  • 99
    • 0022497866 scopus 로고
    • Sublobular distribution of transferases and hydrolases associated with glucuronide, sulfate and glutathione conjugation in human liver
    • Moueli, M. E., and Kaufman, F. C. (1986) Sublobular distribution of transferases and hydrolases associated with glucuronide, sulfate and glutathione conjugation in human liver. Hepatology 6, 450-456
    • (1986) Hepatology , vol.6 , pp. 450-456
    • Moueli, M.E.1    Kaufman, F.C.2
  • 100
    • 0024998355 scopus 로고
    • Immunohistochemical detection of phenol sulfotransferase-containing Neurons in human brain
    • Zou, J., Pentney, R., and Roth, J. A. (1990) Immunohistochemical detection of phenol sulfotransferase-containing Neurons in human brain. J. Neurochem. 55, 1154-1158
    • (1990) J. Neurochem. , vol.55 , pp. 1154-1158
    • Zou, J.1    Pentney, R.2    Roth, J.A.3
  • 101
    • 0028035145 scopus 로고
    • Phenolsulfotransferase: Localization in kidney during human embryonic and fetal development
    • Hume, R., and Coughtrie, M. W. H. (1994) Phenolsulfotransferase: localization in kidney during human embryonic and fetal development. Histochem. J. 26, 850-855
    • (1994) Histochem. J. , vol.26 , pp. 850-855
    • Hume, R.1    Coughtrie, M.W.H.2
  • 102
    • 0030047401 scopus 로고    scopus 로고
    • Differential expression and immunohistochemical localisation of the phenol and hydroxysteroid sulfotransferase enzyme families in the developing lung
    • Hume, R., Barker, E. V., and Coughtrie, M. W. H. (1996) Differential expression and immunohistochemical localisation of the phenol and hydroxysteroid sulfotransferase enzyme families in the developing lung. Histochem. Cell Biol. 105, 147-152
    • (1996) Histochem. Cell Biol. , vol.105 , pp. 147-152
    • Hume, R.1    Barker, E.V.2    Coughtrie, M.W.H.3
  • 104
    • 0020322836 scopus 로고
    • Does sulfate conjugation contribute to the metabolic inactivation of catecholamines in humans?
    • Roth, J. A., and Rivett, A. J. (1982) Does sulfate conjugation contribute to the metabolic inactivation of catecholamines in humans? Biochem. Pharmacol. 31, 3017-3021
    • (1982) Biochem. Pharmacol. , vol.31 , pp. 3017-3021
    • Roth, J.A.1    Rivett, A.J.2
  • 105
    • 84985448376 scopus 로고
    • Sulfuric acid esters as ultimate electrophilic and carcinogenic metabolites of some alkenylbenzenes and aromatic amines in mouse liver
    • Miller, E. C., Miller, J. A., Boberg, E. W., Delclos, K. B., Lai, C. C., Fennell, T. R., Wiseman, R. W., and Liem, A. (1985) Sulfuric acid esters as ultimate electrophilic and carcinogenic metabolites of some alkenylbenzenes and aromatic amines in mouse liver. Carcinogenesis (London) 11, 93-107
    • (1985) Carcinogenesis (London) , vol.11 , pp. 93-107
    • Miller, E.C.1    Miller, J.A.2    Boberg, E.W.3    Delclos, K.B.4    Lai, C.C.5    Fennell, T.R.6    Wiseman, R.W.7    Liem, A.8
  • 106
    • 0030934879 scopus 로고    scopus 로고
    • Bioactivation of mutagens via sulfation
    • In press
    • Glatt, H. Bioactivation of mutagens via sulfation. FASEB J. 11. In press
    • FASEB J. , vol.11
    • Glatt, H.1


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