메뉴 건너뛰기




Volumn 270, Issue 12, 2003, Pages 2652-2662

Expression, localization and potential physiological significance of alcohol dehydrogenase in the gastrointestinal tract

Author keywords

Ethanol; Immunohistochemistry; In situ hybridization; Retinoic acid; Retinol

Indexed keywords

ALCOHOL DEHYDROGENASE; ALCOHOL DEHYDROGENASE (NAD(P)); ALCOHOL DEHYDROGENASE 1; ALCOHOL DEHYDROGENASE 4; ENZYME; RETINOL DEHYDROGENASE; UNCLASSIFIED DRUG;

EID: 0038650796     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2003.03642.x     Document Type: Article
Times cited : (47)

References (68)
  • 1
    • 0002965778 scopus 로고
    • The absorption, distribution and metabolism of ethanol and its effects on nutrition and hepatic function
    • Tabakoff, B., Sutker, P.B. & Randall, C.L., eds. Plenum Press, New york
    • Li, T.-K. (1983) The absorption, distribution and metabolism of ethanol and its effects on nutrition and hepatic function. In Medical and Social Aspects of Ethanol. Abuse (Tabakoff, B., Sutker, P.B. & Randall, C.L., eds), pp. 47-77. Plenum Press, New york.
    • (1983) Medical and Social Aspects of Ethanol. Abuse , pp. 47-77
    • Li, T.-K.1
  • 2
    • 0024456817 scopus 로고
    • Role of extrahepatic alcohol dehydrogenase in rat ethanol metabolism
    • Boleda, M.D., Julià, P., Moreno, A. & Parés, X. (1989) Role of extrahepatic alcohol dehydrogenase in rat ethanol metabolism. Arch. Biochem. Biophys. 274, 74-81.
    • (1989) Arch. Biochem. Biophys. , vol.274 , pp. 74-81
    • Boleda, M.D.1    Julià, P.2    Moreno, A.3    Parés, X.4
  • 3
    • 77956937817 scopus 로고
    • Alcohol dehydrogenase
    • 3rd edn. Boyer, P.D., ed. Academic Press, New York
    • Brändén, C.I., Jörnvall, H., Eklund, H. & Furugren, B. (1975) Alcohol dehydrogenase. In The Enzymes, Vol. 11, 3rd edn. (Boyer, P.D., ed.), pp. 103-190. Academic Press, New York.
    • (1975) The Enzymes , vol.11 , pp. 103-190
    • Brändén, C.I.1    Jörnvall, H.2    Eklund, H.3    Furugren, B.4
  • 4
    • 0036308448 scopus 로고    scopus 로고
    • Differential multiplicity of MDR alcohol dehydrogenases: Enzyme genes in the human genome versus those in organisms initially studied
    • Nordling, E., Persson, B. & Jörnvall, H. (2002) Differential multiplicity of MDR alcohol dehydrogenases: enzyme genes in the human genome versus those in organisms initially studied. Cell. Mol. Life Sci. 59, 1070-1075.
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 1070-1075
    • Nordling, E.1    Persson, B.2    Jörnvall, H.3
  • 5
    • 0028999761 scopus 로고
    • Nomenclature of alcohol dehydrogenases
    • Jörnvall, H. & Höög, J.-O. (1995) Nomenclature of alcohol dehydrogenases. Alcohol 30, 153-161.
    • (1995) Alcohol , vol.30 , pp. 153-161
    • Jörnvall, H.1    Höög, J.-O.2
  • 7
    • 0023093115 scopus 로고
    • Characterization of three isoenzymes of rat alcohol dehydrogenase. Tissue distribution and physical and enzymatic properties
    • Julià, P., Farrés, J. & Parés, X. (1987) Characterization of three isoenzymes of rat alcohol dehydrogenase. Tissue distribution and physical and enzymatic properties. Eur. J. Biochem. 162, 179-189.
    • (1987) Eur. J. Biochem. , vol.162 , pp. 179-189
    • Julià, P.1    Farrés, J.2    Parés, X.3
  • 8
    • 0344132637 scopus 로고    scopus 로고
    • A novel subtype of class II alcohol dehydrogenase in rodents. Unique Pro (47) and Ser (182) modulate hydride transfer in the mouse enzyme
    • Svensson, S., Stromberg, P. & Höög, J.-O. (1999) A novel subtype of class II alcohol dehydrogenase in rodents. Unique Pro (47) and Ser (182) modulate hydride transfer in the mouse enzyme. J. Biol. Chem. 274, 29712-29719.
    • (1999) J. Biol. Chem. , vol.274 , pp. 29712-29719
    • Svensson, S.1    Stromberg, P.2    Höög, J.-O.3
  • 11
    • 0034787867 scopus 로고    scopus 로고
    • Distribution of alcohol dehydrogenase mRNA in the rat central nervous system: Consequences for brain ethanol and retinoid metabolism
    • Martínez, S.E., Vaglenova, J., Sabrià, J., Martínez, M.C., Farrés, J. & Parés, X. (2001) Distribution of alcohol dehydrogenase mRNA in the rat central nervous system: Consequences for brain ethanol and retinoid metabolism. Eur. J. Biochem. 268, 5045-5056.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 5045-5056
    • Martínez, S.E.1    Vaglenova, J.2    Sabrià, J.3    Martínez, M.C.4    Farrés, J.5    Parés, X.6
  • 13
    • 0027428440 scopus 로고
    • Physiological substrates for rat alcohol dehydrogenase classes: Aldehydes of lipid peroxidation, ω-hydroxyfatty acids, and retinoids
    • Boleda, M.D., Saubi, N., Farrés, J. & Parés, X. (1993) Physiological substrates for rat alcohol dehydrogenase classes: Aldehydes of lipid peroxidation, ω-hydroxyfatty acids, and retinoids. Arch. Biochem. Biophys. 307, 85-90.
    • (1993) Arch. Biochem. Biophys. , vol.307 , pp. 85-90
    • Boleda, M.D.1    Saubi, N.2    Farrés, J.3    Parés, X.4
  • 14
    • 0034682830 scopus 로고    scopus 로고
    • Molecular basis for differential substrate specificity in class IV alcohol dehydrogenases: A conserved function in retinoid metabolism but not in ethanol metabolism
    • Crosas, B., Allali-Hassani, A., Martínez, S.E., Martras, S., Persson, B., Jörnvall, H., Parés, X. & Farrés, J. (2000) Molecular basis for differential substrate specificity in class IV alcohol dehydrogenases: a conserved function in retinoid metabolism but not in ethanol metabolism. J. Biol. Chem. 275, 25180-25187.
    • (2000) J. Biol. Chem. , vol.275 , pp. 25180-25187
    • Crosas, B.1    Allali-Hassani, A.2    Martínez, S.E.3    Martras, S.4    Persson, B.5    Jörnvall, H.6    Parés, X.7    Farrés, J.8
  • 17
    • 0028245725 scopus 로고
    • Catalytic efficiency of human alcohol dehydrogenase for retinol oxidation and retinal reduction
    • Yang, Z.-N., Davis, G.J., Hurley, T.D., Stone, C.L., Li, T.-K. & Bosron, W.F. (1994) Catalytic efficiency of human alcohol dehydrogenase for retinol oxidation and retinal reduction. Alcohol. Clin. Exp. Res. 18, 587-591.
    • (1994) Alcohol. Clin. Exp. Res. , vol.18 , pp. 587-591
    • Yang, Z.-N.1    Davis, G.J.2    Hurley, T.D.3    Stone, C.L.4    Li, T.-K.5    Bosron, W.F.6
  • 18
    • 0033546155 scopus 로고    scopus 로고
    • Metabolic deficiencies in alcohol dehydrogenase Adhl, Adh3, and Adh4 null mutant mice
    • Deltour, L., Foglio, M.H. & Duester, G. (1999) Metabolic deficiencies in alcohol dehydrogenase Adhl, Adh3, and Adh4 null mutant mice. J. Biol. Chem. 274, 16796-16801.
    • (1999) J. Biol. Chem. , vol.274 , pp. 16796-16801
    • Deltour, L.1    Foglio, M.H.2    Duester, G.3
  • 19
    • 0032974743 scopus 로고    scopus 로고
    • Impaired retinol utilization in Adh4 alcohol dehydrogenase mutant mice
    • Deltour, L., Foglio, M.H. & Duester, G. (1999) Impaired retinol utilization in Adh4 alcohol dehydrogenase mutant mice. Dev. Genet. 25, 1-10.
    • (1999) Dev. Genet. , vol.25 , pp. 1-10
    • Deltour, L.1    Foglio, M.H.2    Duester, G.3
  • 20
    • 0027283696 scopus 로고
    • Distribution of alcohol and sorbitol dehydrogenases. Assessment of mRNA species in mammalian tissues
    • Estonius, M., Danielsson, O., Karlsson, C., Persson, H., Jörnvall, H. & Höög, J.-O. (1993) Distribution of alcohol and sorbitol dehydrogenases. Assessment of mRNA species in mammalian tissues. Eur. J. Biochem. 215, 497-503.
    • (1993) Eur. J. Biochem. , vol.215 , pp. 497-503
    • Estonius, M.1    Danielsson, O.2    Karlsson, C.3    Persson, H.4    Jörnvall, H.5    Höög, J.-O.6
  • 21
    • 0030692056 scopus 로고    scopus 로고
    • Regional restriction of alcohol/retinol dehydrogenases along the mouse gastrointestinal epithelium
    • Haselbeck, R.J. & Duester, G. (1997) Regional restriction of alcohol/retinol dehydrogenases along the mouse gastrointestinal epithelium. Alcohol. Clin. Exp. Res. 21, 1484-1490.
    • (1997) Alcohol. Clin. Exp. Res. , vol.21 , pp. 1484-1490
    • Haselbeck, R.J.1    Duester, G.2
  • 22
    • 0029925516 scopus 로고    scopus 로고
    • Aldehyde dehydrogenases of the rat colon: Comparison with other tissues of the alimentary tract and the liver
    • Koivisto, T. & Salaspuro, M. (1996) Aldehyde dehydrogenases of the rat colon: comparison with other tissues of the alimentary tract and the liver. Alcohol. Clin. Exp. Res. 20, 551-555.
    • (1996) Alcohol. Clin. Exp. Res. , vol.20 , pp. 551-555
    • Koivisto, T.1    Salaspuro, M.2
  • 23
    • 0029979542 scopus 로고    scopus 로고
    • Expression and activities of class TV alcohol dehydrogenase and class III aldehyde dehydrogenase in human mouth
    • Dong, Y.J., Peng, T.K. & Yin, S.J. (1996) Expression and activities of class TV alcohol dehydrogenase and class III aldehyde dehydrogenase in human mouth. Alcohol 13, 257-262.
    • (1996) Alcohol , vol.13 , pp. 257-262
    • Dong, Y.J.1    Peng, T.K.2    Yin, S.J.3
  • 24
    • 0030592763 scopus 로고    scopus 로고
    • Alcohol dehydrogenase in human tissues: Localisation of transcripts coding for five classes of the enzyme
    • Estonius, M., Svensson, S. & Höög, J.-O. (1996) Alcohol dehydrogenase in human tissues: localisation of transcripts coding for five classes of the enzyme. FEBS Lett. 397, 338-342.
    • (1996) FEBS Lett. , vol.397 , pp. 338-342
    • Estonius, M.1    Svensson, S.2    Höög, J.-O.3
  • 25
    • 84994438858 scopus 로고    scopus 로고
    • Alcohol and aldehyde dehydrogenases in the gastrointestinal tract
    • Preedy, V.R. & Watson, R.R., eds. CRC Press, Boca Raton
    • Parés, X. & Farrés, J. (1996) Alcohol and aldehyde dehydrogenases in the gastrointestinal tract. In Alcohol and the Gastrointestinal Tract (Preedy, V.R. & Watson, R.R., eds), pp. 41-56. CRC Press, Boca Raton.
    • (1996) Alcohol and the Gastrointestinal Tract , pp. 41-56
    • Parés, X.1    Farrés, J.2
  • 26
    • 4244008662 scopus 로고    scopus 로고
    • Distribution of alcohol dehydrogenase in human organs. Relevance for alcohol metabolism and pathology
    • Agarwal, D. P. & Seitz H. K., eds. Marcel Dekker Inc., New York
    • Parés, X., Martínez, S.E., Allali-Hassani, A., Borràs, E., Farrés, J., Martras, S., Rosell, A. & Vaglenova, J. (2001) Distribution of alcohol dehydrogenase in human organs. Relevance for alcohol metabolism and pathology. In Alcohol in Health and Disease (Agarwal, D. P. & Seitz H. K., eds), pp. 87-102. Marcel Dekker Inc., New York.
    • (2001) Alcohol in Health and Disease , pp. 87-102
    • Parés, X.1    Martínez, S.E.2    Allali-Hassani, A.3    Borràs, E.4    Farrés, J.5    Martras, S.6    Rosell, A.7    Vaglenova, J.8
  • 27
    • 0020513935 scopus 로고
    • Immunohistochemical localization of alcohol dehydrogenase in the human gastrointestinal tract
    • Pestalozzi, D.M., Bühler, R., von Wartburg, J.P. & Hess, M. (1983) Immunohistochemical localization of alcohol dehydrogenase in the human gastrointestinal tract. Gastroenterology 85, 1011-1016.
    • (1983) Gastroenterology , vol.85 , pp. 1011-1016
    • Pestalozzi, D.M.1    Bühler, R.2    Von Wartburg, J.P.3    Hess, M.4
  • 30
    • 0031051848 scopus 로고    scopus 로고
    • Human stomach alcohol and aldehyde dehydrogenases: Comparison of expression pattern and activities in alimentary tract
    • Yin, S.J., Liao, C.S., Wu, C.W., Li, T.T., Chen, L.L., Lai, C.L. & Tsao, T.Y. (1997) Human stomach alcohol and aldehyde dehydrogenases: comparison of expression pattern and activities in alimentary tract. Gastroenterology 112, 766-775.
    • (1997) Gastroenterology , vol.112 , pp. 766-775
    • Yin, S.J.1    Liao, C.S.2    Wu, C.W.3    Li, T.T.4    Chen, L.L.5    Lai, C.L.6    Tsao, T.Y.7
  • 31
    • 0020791660 scopus 로고
    • Steady-state kinetic properties of purified rat liver alcohol dehydrogenase: Application to predicting alcohol elimination rates in vivo
    • Crabb, D.W., Bosron, W.F. & Li, T.K. (1983) Steady-state kinetic properties of purified rat liver alcohol dehydrogenase: application to predicting alcohol elimination rates in vivo. Arch. Biochem. Biophys. 224, 299-309.
    • (1983) Arch. Biochem. Biophys. , vol.224 , pp. 299-309
    • Crabb, D.W.1    Bosron, W.F.2    Li, T.K.3
  • 32
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitative determination of microgram quantifies of protein utilising the principle of protein-dye binding
    • Bradford, M.M. (1976) A rapid and sensitive method for the quantitative determination of microgram quantifies of protein utilising the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 34
    • 0000593282 scopus 로고    scopus 로고
    • Expression patterns of class I and class IV alcohol dehydrogenase genes in developing epithelia suggest a role for alcohol dehydrogenase in local retinoic acid synthesis
    • Ang, H.L., Deltour, L., Zgombic-Knight, M., Wagner, M.A. & Duester, G. (1996) Expression patterns of class I and class IV alcohol dehydrogenase genes in developing epithelia suggest a role for alcohol dehydrogenase in local retinoic acid synthesis. Alcohol. Clin. Exp. Res. 20, 1050-1064.
    • (1996) Alcohol. Clin. Exp. Res. , vol.20 , pp. 1050-1064
    • Ang, H.L.1    Deltour, L.2    Zgombic-Knight, M.3    Wagner, M.A.4    Duester, G.5
  • 35
    • 0028947552 scopus 로고
    • Cloning of the mouse class IV alcohol dehydrogenase (retinol dehydrogenase) cDNA and tissue-specific expression patterns of the murine ADH gene family
    • Zgombic-Knight, M., Ang, H.L., Foglio, M.H. & Duester, G. (1995) Cloning of the mouse class IV alcohol dehydrogenase (retinol dehydrogenase) cDNA and tissue-specific expression patterns of the murine ADH gene family. J. Biol. Chem. 270, 10868-10877.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10868-10877
    • Zgombic-Knight, M.1    Ang, H.L.2    Foglio, M.H.3    Duester, G.4
  • 36
    • 0022400581 scopus 로고
    • Cell-specific immunohistochemical localization of a cellular retinol-binding protein (type two) in the small intestine of rat
    • Crow, J.A. & Ong, D.E. (1985) Cell-specific immunohistochemical localization of a cellular retinol-binding protein (type two) in the small intestine of rat. Proc. Natl Acad. Sci. USA 82, 4707-4711.
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 4707-4711
    • Crow, J.A.1    Ong, D.E.2
  • 38
    • 0026576327 scopus 로고
    • Purification and partial characterization of cellular retinol-binding protein, type two, from human small intestine
    • Inagami, S. & Ong, D.E. (1992) Purification and partial characterization of cellular retinol-binding protein, type two, from human small intestine. J. Nutr. 122, 450-456.
    • (1992) J. Nutr. , vol.122 , pp. 450-456
    • Inagami, S.1    Ong, D.E.2
  • 39
    • 0032897401 scopus 로고    scopus 로고
    • Expression of nuclear retinoid receptors in normal, premalignant and malignant gastric tissues determined by in situ hybridization
    • Jiang, S.Y., Shen, S.R. & Shyu, R.Y., Yu, J.C., Ham, H.J., Yeh, M.Y., Lee, M.M. & Chang, Y.C. (1999) Expression of nuclear retinoid receptors in normal, premalignant and malignant gastric tissues determined by in situ hybridization. Br. J. Cancer 80, 206-214.
    • (1999) Br. J. Cancer , vol.80 , pp. 206-214
    • Jiang, S.Y.1    Shen, S.R.2    Shyu, R.Y.3    Yu, J.C.4    Ham, H.J.5    Yeh, M.Y.6    Lee, M.M.7    Chang, Y.C.8
  • 40
    • 0026688249 scopus 로고
    • Effect of retinoid status on alpha, beta and gamma retinoic acid receptor mRNA levels in various rat tissues
    • Kato, S., Mano, H., Kumazawa, T., Yoshizawa, Y., Kojima, R. & Masushige, S. (1992) Effect of retinoid status on alpha, beta and gamma retinoic acid receptor mRNA levels in various rat tissues. Biochem. J. 286, 755-760.
    • (1992) Biochem. J. , vol.286 , pp. 755-760
    • Kato, S.1    Mano, H.2    Kumazawa, T.3    Yoshizawa, Y.4    Kojima, R.5    Masushige, S.6
  • 41
    • 0032540448 scopus 로고    scopus 로고
    • Retinal dehydrogenase gene expression in stomach and small intestine of rats during postnatal development and in vitamin A deficiency
    • Bhat, P.V. (1998) Retinal dehydrogenase gene expression in stomach and small intestine of rats during postnatal development and in vitamin A deficiency. FEBS Lett. 426, 260-262.
    • (1998) FEBS Lett. , vol.426 , pp. 260-262
    • Bhat, P.V.1
  • 42
    • 0033670445 scopus 로고    scopus 로고
    • Localization of retinal dehydrogenase type 1 in the stomach and intestine
    • Frota-Ruchon, A., Marcinkiewicz, M. & Bhat, P.V. (2000) Localization of retinal dehydrogenase type 1 in the stomach and intestine. Cell Tissue Res. 302, 397-400.
    • (2000) Cell Tissue Res. , vol.302 , pp. 397-400
    • Frota-Ruchon, A.1    Marcinkiewicz, M.2    Bhat, P.V.3
  • 43
    • 0037134450 scopus 로고    scopus 로고
    • Distinct retinoid metabolic functions for alcohol dehydrogenase genes Adh1 and Adh4 in protection against vitamin A toxicity or deficiency revealed in double null mutant mice
    • Molotkov, A., Deltour, L., Foglio, M.H., Cuenca, A.E. & Duester, G. (2002) Distinct retinoid metabolic functions for alcohol dehydrogenase genes Adh1 and Adh4 in protection against vitamin A toxicity or deficiency revealed in double null mutant mice. J. Biol. Chem. 277, 13804-13811.
    • (2002) J. Biol. Chem. , vol.277 , pp. 13804-13811
    • Molotkov, A.1    Deltour, L.2    Foglio, M.H.3    Cuenca, A.E.4    Duester, G.5
  • 45
    • 0034990089 scopus 로고    scopus 로고
    • Nicotinamide adenine dinucleotide-dependent retinoic acid formation from retinol in the human gastric mucosa: Inhibition by ethanol, acetaldehyde, and H2 blockers
    • Yokoyama, H., Matsumoto, M., Shiraishi, H., Miyagi, M., Kato, S. & Ishii, H. (2001) Nicotinamide adenine dinucleotide-dependent retinoic acid formation from retinol in the human gastric mucosa: inhibition by ethanol, acetaldehyde, and H2 blockers. Alcohol. Clin. Exp. Res. 2, 24S-28S.
    • (2001) Alcohol. Clin. Exp. Res. , vol.2
    • Yokoyama, H.1    Matsumoto, M.2    Shiraishi, H.3    Miyagi, M.4    Kato, S.5    Ishii, H.6
  • 47
    • 0023712276 scopus 로고
    • Reduction of retinaldehyde bound to cellular retinol-binding protein (type II) by microsomes from rat small intestine
    • Kakkad, B.P. & Ong, D.E. (1988) Reduction of retinaldehyde bound to cellular retinol-binding protein (type II) by microsomes from rat small intestine. J. Biol. Chem. 263, 12916-12919.
    • (1988) J. Biol. Chem. , vol.263 , pp. 12916-12919
    • Kakkad, B.P.1    Ong, D.E.2
  • 49
    • 0023182575 scopus 로고
    • The contribution of the stomach to ethanol oxidation in the rat
    • Caballería, J., Barahona, E. & Lieber, C.S. (1986) The contribution of the stomach to ethanol oxidation in the rat. Life Sci. 41, 1021-1027.
    • (1986) Life Sci. , vol.41 , pp. 1021-1027
    • Caballería, J.1    Barahona, E.2    Lieber, C.S.3
  • 51
    • 0032523816 scopus 로고    scopus 로고
    • Contribution to first-pass metabolism of ethanol and inhibition by ethanol for retinol oxidation in human alcohol dehydrogenase family
    • Han, C.-L., Liao, C.-S., Wu, C.-W., Hwong, C.-L., Lee, A.-R. & Yin, S.-J. (1998) Contribution to first-pass metabolism of ethanol and inhibition by ethanol for retinol oxidation in human alcohol dehydrogenase family. Eur. J. Biochem. 254, 25-31.
    • (1998) Eur. J. Biochem. , vol.254 , pp. 25-31
    • Han, C.-L.1    Liao, C.-S.2    Wu, C.-W.3    Hwong, C.-L.4    Lee, A.-R.5    Yin, S.-J.6
  • 54
    • 0014813667 scopus 로고
    • The physiological role of liver alcohol dehydrogenase
    • Krebs, H.A. & Perkins, J.R. (1970) The physiological role of liver alcohol dehydrogenase. Biochem. J. 118, 635-644.
    • (1970) Biochem. J. , vol.118 , pp. 635-644
    • Krebs, H.A.1    Perkins, J.R.2
  • 55
    • 0022657702 scopus 로고
    • Role of intestinal bacterial overgrowth in ethanol production and metabolism in rats
    • Baraona, E., Julkunen, R., Tannenbaum, L. & Lieber, C.S. (1986) Role of intestinal bacterial overgrowth in ethanol production and metabolism in rats. Gastroenterology 90, 103-110.
    • (1986) Gastroenterology , vol.90 , pp. 103-110
    • Baraona, E.1    Julkunen, R.2    Tannenbaum, L.3    Lieber, C.S.4
  • 56
    • 0030462286 scopus 로고    scopus 로고
    • Aldehyde dehydrogenase activity and acetate production by aerobic bacteria representing the normal flora of human large intestine
    • Nosova, T., Jokelainen, K., Kaihovaara, P., Jousimies-Somer, H., Siitonen, A., Heine, R. & Salaspuro, M. (1996) Aldehyde dehydrogenase activity and acetate production by aerobic bacteria representing the normal flora of human large intestine Alcohol Alcohol. 31, 555-564.
    • (1996) Alcohol Alcohol. , vol.31 , pp. 555-564
    • Nosova, T.1    Jokelainen, K.2    Kaihovaara, P.3    Jousimies-Somer, H.4    Siitonen, A.5    Heine, R.6    Salaspuro, M.7
  • 57
    • 0028951793 scopus 로고
    • Alcohol consumption and risk of cancer in humans: An overview
    • Longnecker, M.P. (1995) Alcohol consumption and risk of cancer in humans: an overview. Alcohol 12, 87-96.
    • (1995) Alcohol , vol.12 , pp. 87-96
    • Longnecker, M.P.1
  • 60
    • 0028079763 scopus 로고
    • Vitamin A, differentiation and cancer
    • Love, J.M. & Gudas, L.J. (1994) Vitamin A, differentiation and cancer. Curr. Opin. Cell Biol. 6, 825-831.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 825-831
    • Love, J.M.1    Gudas, L.J.2
  • 61
    • 0023194984 scopus 로고
    • Effect of ethanol and vitamin A deficiency on epithelial cell proliferation and structure in the rat esophagus
    • Mak, K.M., Leo, M.A. & Lieber, C.S. (1987) Effect of ethanol and vitamin A deficiency on epithelial cell proliferation and structure in the rat esophagus. Gastroenterology 93, 362-370.
    • (1987) Gastroenterology , vol.93 , pp. 362-370
    • Mak, K.M.1    Leo, M.A.2    Lieber, C.S.3
  • 62
    • 0022975520 scopus 로고
    • Serum retinol and subsequent risk of cancer
    • Wald, N., Boreham, J. & Bailey, A. (1986) Serum retinol and subsequent risk of cancer. Br. J. Cancer 54, 957-961.
    • (1986) Br. J. Cancer , vol.54 , pp. 957-961
    • Wald, N.1    Boreham, J.2    Bailey, A.3
  • 63
    • 0022495147 scopus 로고
    • Ocular alcohol dehydrogenase in the rat: Regional distribution and kinetics of the ADH-1 isoenzyme with retinol and retinal
    • Julià, P., Farrés, J. & Parés, X. (1986) Ocular alcohol dehydrogenase in the rat: Regional distribution and kinetics of the ADH-1 isoenzyme with retinol and retinal. Exp. Eye Res. 42, 305-314.
    • (1986) Exp. Eye Res. , vol.42 , pp. 305-314
    • Julià, P.1    Farrés, J.2    Parés, X.3
  • 64
    • 0032504680 scopus 로고    scopus 로고
    • Effect of cellular retinol-binding protein on retinol oxidation by human class IV retinol/alcohol dehydrogenase and inhibition by ethanol
    • Kedishvili, N.Y., Gough, W.H., Wilhelmina, I.D., Parsons, S., Li, T.-K. & Bosron, W.F. (1998) Effect of cellular retinol-binding protein on retinol oxidation by human class IV retinol/alcohol dehydrogenase and inhibition by ethanol. Biochem. Biophys. Res. Commun. 249, 191-196.
    • (1998) Biochem. Biophys. Res. Commun. , vol.249 , pp. 191-196
    • Kedishvili, N.Y.1    Gough, W.H.2    Wilhelmina, I.D.3    Parsons, S.4    Li, T.-K.5    Bosron, W.F.6
  • 65
    • 0015145188 scopus 로고
    • The inhibitory effect of ethanol on retinol oxidation by human liver and cattle retina
    • Mezey, E. & Holt, P.R. (1971) The inhibitory effect of ethanol on retinol oxidation by human liver and cattle retina. Exp. Mol. Pathol. 15, 148-156.
    • (1971) Exp. Mol. Pathol. , vol.15 , pp. 148-156
    • Mezey, E.1    Holt, P.R.2
  • 66
    • 0037151082 scopus 로고    scopus 로고
    • Retinol/ethanol drug interaction during acute alcohol intoxication in mice involves inhibition of retinol metabolism to retinoic acid by alcohol dehydrogenase
    • Molotkov, A. & Duester, G. (2002) Retinol/ethanol drug interaction during acute alcohol intoxication in mice involves inhibition of retinol metabolism to retinoic acid by alcohol dehydrogenase. J. Biol. Chem. 277, 22553-22557.
    • (2002) J. Biol. Chem. , vol.277 , pp. 22553-22557
    • Molotkov, A.1    Duester, G.2
  • 67
    • 0032831815 scopus 로고    scopus 로고
    • Interactions of retinoid proteins and enzymes in retinoid metabolism
    • Napoli, J.L. (1999) Interactions of retinoid proteins and enzymes in retinoid metabolism. Biochim. Biophys. Acta 1440, 139-162.
    • (1999) Biochim. Biophys. Acta , vol.1440 , pp. 139-162
    • Napoli, J.L.1
  • 68
    • 0033911401 scopus 로고    scopus 로고
    • Families of retinoid dehydrogenases regulating vitamin A function: Production of visual pigment and retinoic acid
    • Duester, G. (2000) Families of retinoid dehydrogenases regulating vitamin A function: production of visual pigment and retinoic acid. Eur. J. Biochem. 267, 4315-4324.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 4315-4324
    • Duester, G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.