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Volumn 11, Issue 1, 1999, Pages 19-35

Xenobiotic-metabolizing enzymes in the canine respiratory tract

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALIA; CANIS FAMILIARIS;

EID: 0032917712     PISSN: 08958378     EISSN: None     Source Type: Journal    
DOI: 10.1080/089583799197249     Document Type: Article
Times cited : (8)

References (43)
  • 1
    • 0021950853 scopus 로고
    • 4-Hydroxy-2-enals are substrates for glutathione transferases
    • Alin, P., Danielson, U. H., and Mannervik, B. 1985. 4-Hydroxy-2-enals are substrates for glutathione transferases. FEBS Lett. 179:267-270.
    • (1985) FEBS Lett. , vol.179 , pp. 267-270
    • Alin, P.1    Danielson, U.H.2    Mannervik, B.3
  • 2
    • 0027235508 scopus 로고
    • Organisation and characterization of the rat class 3 aldehyde dehydrogenase gene
    • Asman, D. C., Takimoto, K., Pilot, H. C., Dunn, T. J., and Lindahl, R. 1993. Organisation and characterization of the rat class 3 aldehyde dehydrogenase gene. J. Biol. Chem. 268:12530-12536.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12530-12536
    • Asman, D.C.1    Takimoto, K.2    Pilot, H.C.3    Dunn, T.J.4    Lindahl, R.5
  • 3
    • 0021809363 scopus 로고
    • Effect of sulfite on the energy metabolism of mammalian tissues in correlation to sulfite oxidase activity
    • Beck-Speier, I., Hinze, H., and Holzer, H. 1985. Effect of sulfite on the energy metabolism of mammalian tissues in correlation to sulfite oxidase activity. Biochim. Biophys. Acta 841:81-89.
    • (1985) Biochim. Biophys. Acta , vol.841 , pp. 81-89
    • Beck-Speier, I.1    Hinze, H.2    Holzer, H.3
  • 4
    • 0002754935 scopus 로고
    • Metabolism of xenobiotics by the respiratory tract
    • eds. D. E. Gardner, J. D. Crapo, and R. O. McClellan, 2nd ed., New York: Raven Press
    • Bond, J. A. 1993. Metabolism of xenobiotics by the respiratory tract. In Toxicology of the lung, eds. D. E. Gardner, J. D. Crapo, and R. O. McClellan, 2nd ed., pp. 187-215. New York: Raven Press.
    • (1993) Toxicology of the Lung , pp. 187-215
    • Bond, J.A.1
  • 5
    • 0023852210 scopus 로고
    • Regional distribution of xenobiotic metabolizing enzymes in respiratory airways of dogs
    • Bond, J. A., Harkema, J. R., and Russell, V. I. 1988. Regional distribution of xenobiotic metabolizing enzymes in respiratory airways of dogs. Drug Metab. Dispos. 16:116-124.
    • (1988) Drug Metab. Dispos. , vol.16 , pp. 116-124
    • Bond, J.A.1    Harkema, J.R.2    Russell, V.I.3
  • 6
    • 0017741869 scopus 로고
    • Evidence for the Clara cell as a site of cytochrome P450-dependent mixed function oxidase in the lung
    • Boyd, M. R. 1977. Evidence for the Clara cell as a site of cytochrome P450-dependent mixed function oxidase in the lung. Nature 269:713-717.
    • (1977) Nature , vol.269 , pp. 713-717
    • Boyd, M.R.1
  • 7
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 8
    • 0028855791 scopus 로고
    • Relationship of cytochrome P450 activity to Clara cell cytotoxicity. IV. Metabolism of naphthalene and natpthalene oxide in microdissected airways from mice, rats, and hamsters
    • Buckpitt, A., Chang, A. M., Weir, A., van Winkle, L., Duan X., Philpot, R., and Plopper, C. 1995. Relationship of cytochrome P450 activity to clara cell cytotoxicity. IV. Metabolism of naphthalene and natpthalene oxide in microdissected airways from mice, rats, and hamsters. Mol. Pharmacol. 47:74-81.
    • (1995) Mol. Pharmacol. , vol.47 , pp. 74-81
    • Buckpitt, A.1    Chang, A.M.2    Weir, A.3    Van Winkle, L.4    Duan, X.5    Philpot, R.6    Plopper, C.7
  • 10
    • 0026110377 scopus 로고
    • Characterization of the cytochrome P-450 monooxygenase system in nonciliated bronchiolar epithelial (Clara) cells isolated from mouse lung
    • Chichester, C. H., Philpot, R. M., Weir, A. J., Buckpitt, A. R., and Plopper, C. G. 1991. Characterization of the cytochrome P-450 monooxygenase system in nonciliated bronchiolar epithelial (Clara) cells isolated from mouse lung. Am. J. Respir. Cell Mol. Biol. 4:179-186.
    • (1991) Am. J. Respir. Cell Mol. Biol. , vol.4 , pp. 179-186
    • Chichester, C.H.1    Philpot, R.M.2    Weir, A.J.3    Buckpitt, A.R.4    Plopper, C.G.5
  • 11
    • 0015239046 scopus 로고
    • Hepatic sulfite oxidase
    • Cohen, H. J., and Fridovich, I. 1971. Hepatic sulfite oxidase. J. Biol. Chem. 246:359-366.
    • (1971) J. Biol. Chem. , vol.246 , pp. 359-366
    • Cohen, H.J.1    Fridovich, I.2
  • 13
    • 0027486972 scopus 로고
    • Expired breath hydrogen peroxide is a marker of acute airway inflammation in pediatric patients with asthma
    • Dohlman, A. W., Black, H. R., and Royall, J. A. 1993. Expired breath hydrogen peroxide is a marker of acute airway inflammation in pediatric patients with asthma. Am. Rev. Respir. Dis. 148:955-960.
    • (1993) Am. Rev. Respir. Dis. , vol.148 , pp. 955-960
    • Dohlman, A.W.1    Black, H.R.2    Royall, J.A.3
  • 14
    • 0015385650 scopus 로고
    • Retention of inhaled formaldehyde, propionaldehyde and aciolein in the dog
    • Egle, J. L. 1972. Retention of inhaled formaldehyde, propionaldehyde and aciolein in the dog. Arch. Environ. Health 25:119-124.
    • (1972) Arch. Environ. Health , vol.25 , pp. 119-124
    • Egle, J.L.1
  • 16
    • 0028905428 scopus 로고
    • Role of the lung in accumulation and metabolism of xenobiotic compounds -Implications for chemically induced toxicity
    • Foth, H. 1995. Role of the lung in accumulation and metabolism of xenobiotic compounds -Implications for chemically induced toxicity. Crit. Rev. Toxicol. 25:165-205.
    • (1995) Crit. Rev. Toxicol. , vol.25 , pp. 165-205
    • Foth, H.1
  • 17
    • 0014475638 scopus 로고
    • 35S labeled) absorption by the nose and mouth under conditions of varying concentrations and flow
    • 35S labeled) absorption by the nose and mouth under conditions of varying concentrations and flow. Arch. Environ. Health 18:315-22.
    • (1969) Arch. Environ. Health , vol.18 , pp. 315-322
    • Frank, N.R.1    Yoder, R.E.2    Brain, J.D.3    Yokoyama, E.4
  • 18
    • 0016275313 scopus 로고
    • Glutathione S-transferases, the first enzymatic step in mercapturic acid formation
    • Habig, W. H., Pabst, M. J., and Jakoby, W. B. 1974. Glutathione S-transferases, the first enzymatic step in mercapturic acid formation. J. Biol. Chem. 249:7130-7139.
    • (1974) J. Biol. Chem. , vol.249 , pp. 7130-7139
    • Habig, W.H.1    Pabst, M.J.2    Jakoby, W.B.3
  • 20
    • 84907038085 scopus 로고
    • Early response of the canine respiratory tract following long-term exposure to a sulfur(IV) aerosol at low concentration. I rationale, design and summary report
    • Heyder, J., Beck-Speier, I., Ferron, G., Heilmann, P., Karg, E., Kreyling, W. G., Lenz, A., Maier, K., Schulz, H., Takenaka, S., and Tuch, T. 1992. Early response of the canine respiratory tract following long-term exposure to a sulfur(IV) aerosol at low concentration. I Rationale, design and summary report, Inhal. Toxicol. 4:159-174.
    • (1992) Inhal. Toxicol. , vol.4 , pp. 159-174
    • Heyder, J.1    Beck-Speier, I.2    Ferron, G.3    Heilmann, P.4    Karg, E.5    Kreyling, W.G.6    Lenz, A.7    Maier, K.8    Schulz, H.9    Takenaka, S.10    Tuch, T.11
  • 21
    • 0028566888 scopus 로고
    • Cloning of a cDNA encoding human ALDH7, a new member of the aldehyde dehydrogenase family
    • Hsu, L. C., Chang, W.-C, and Yoshida, A. 1994. Cloning of a cDNA encoding human ALDH7, a new member of the aldehyde dehydrogenase family. Gene 151::285-289
    • (1994) Gene , vol.151 , pp. 285-289
    • Hsu, L.C.1    Chang, W.-C.2    Yoshida, A.3
  • 22
    • 0002341229 scopus 로고
    • Automotive emissions
    • eds. A. Y. Watson, R. R. Bates, and D. Kennedy, Washington, DC: National Academy Press
    • Johnson, J. H. 1988. Automotive emissions. In Air pollution, the automobile, and public health, eds. A. Y. Watson, R. R. Bates, and D. Kennedy, pp. 39-75. Washington, DC: National Academy Press.
    • (1988) Air Pollution, the Automobile, and Public Health , pp. 39-75
    • Johnson, J.H.1
  • 23
    • 0017087201 scopus 로고
    • Purification and properties of sulfite oxidase from human liver
    • Johnson, J. L., and Rajagopalan, K. V. 1976a. Purification and properties of sulfite oxidase from human liver. J. Clin. Invest. 58:543-550.
    • (1976) J. Clin. Invest. , vol.58 , pp. 543-550
    • Johnson, J.L.1    Rajagopalan, K.V.2
  • 25
  • 27
    • 0026098629 scopus 로고
    • Increased levels of oxidized methionine residues in bronchoalveolar lavage fluid proteins from patients with idiopathic pulmonary fibrosis
    • Maier, K., Leuschel, L., and Costabel, U. 1991. Increased levels of oxidized methionine residues in bronchoalveolar lavage fluid proteins from patients with idiopathic pulmonary fibrosis. Am. Rev. Respir. Dis. 143:271-274.
    • (1991) Am. Rev. Respir. Dis. , vol.143 , pp. 271-274
    • Maier, K.1    Leuschel, L.2    Costabel, U.3
  • 28
    • 0026650664 scopus 로고
    • Increased oxidized methionine residues in BAL fluid proteins in acute and chronic bronchitis
    • Maier, K. L., Leuschel, L., and Costabel, U. 1992a. Increased oxidized methionine residues in BAL fluid proteins in acute and chronic bronchitis. Eur. Respir. J. 5:651-658.
    • (1992) Eur. Respir. J. , vol.5 , pp. 651-658
    • Maier, K.L.1    Leuschel, L.2    Costabel, U.3
  • 29
    • 0003716958 scopus 로고
    • Early response of the canine respiratory tract following long-term exposure to a sulfur(IV) aerosol at low concentration. II. Biochemistry and cell biology of lung lavage fluid
    • Maier, K., Beck-Speier, I., Dayal, N., Heilmann, P., Hinze, H, Lenz, A.-G., Leuschel, L., Matejkova, E., Ruprecht, L., and Heyder, J. 1992b. Early response of the canine respiratory tract following long-term exposure to a sulfur(IV) aerosol at low concentration. II. Biochemistry and cell biology of lung lavage fluid, Inhal. Toxicol. 4:175-195.
    • (1992) Inhal. Toxicol. , vol.4 , pp. 175-195
    • Maier, K.1    Beck-Speier, I.2    Dayal, N.3    Heilmann, P.4    Hinze, H.5    Lenz, A.-G.6    Leuschel, L.7    Matejkova, E.8    Ruprecht, L.9    Heyder, J.10
  • 30
    • 0002348389 scopus 로고
    • Diesel exhaust
    • ed. M. Lippmann, New York: Van Nostrand Reinhold
    • Mauderly, J. L. 1992. Diesel exhaust. In Environmental toxicants, ed. M. Lippmann, pp. 119-162. New York: Van Nostrand Reinhold.
    • (1992) Environmental Toxicants , pp. 119-162
    • Mauderly, J.L.1
  • 32
    • 0025964511 scopus 로고
    • Use of microdissected airways to define metabolism and cytotoxicity in murine bronchiolar epithelium
    • Plopper, C. G., Chang, A. M., Pang, A., and Buckpitt, A. R. 1991. Use of microdissected airways to define metabolism and cytotoxicity in murine bronchiolar epithelium. Exp. Lung Res. 17:197-212.
    • (1991) Exp. Lung Res. , vol.17 , pp. 197-212
    • Plopper, C.G.1    Chang, A.M.2    Pang, A.3    Buckpitt, A.R.4
  • 36
    • 0023889046 scopus 로고
    • The distribution of cytochrome P450 monooxygenase in cells of the rabbit lung: An ultrastructural immunological characterization
    • Serbjit-Singh, C., Nishio, S., Philpot, R., and Plopper, C. 1988. The distribution of cytochrome P450 monooxygenase in cells of the rabbit lung: An ultrastructural immunological characterization. Mol. Pharmacol. 33:279-289.
    • (1988) Mol. Pharmacol. , vol.33 , pp. 279-289
    • Serbjit-Singh, C.1    Nishio, S.2    Philpot, R.3    Plopper, C.4
  • 37
    • 0026177929 scopus 로고
    • Glutathione S-transferase-catalyzed conjugation of 9,10-epoxystearic acid with glutathione
    • Sharma, R., Gupta, S., Singhal, S. S., Ansari, G. A. S., and Awasthi, Y. C. 1991. Glutathione S-transferase-catalyzed conjugation of 9,10-epoxystearic acid with glutathione. J. Biochem. Toxicol. 6:147-153.
    • (1991) J. Biochem. Toxicol. , vol.6 , pp. 147-153
    • Sharma, R.G.1    Upta, S.2    Singhal, S.S.3    Ansari, G.A.S.4    Awasthi, Y.C.5
  • 38
    • 0023140177 scopus 로고
    • Sulfur-dioxide induced bronchitis in dogs - Effects on airway responsiveness to inhaled and intravenously administered methacholine
    • Shore, S. A., Kariya, S. T., Anderson K., Skornik, W., Feldman, H. A., Pennington, J., Godleski, J., and Drazen, J. M. 1987. Sulfur-dioxide induced bronchitis in dogs - Effects on airway responsiveness to inhaled and intravenously administered methacholine. Am. Rev. Respir. Dis. 135:840-847.
    • (1987) Am. Rev. Respir. Dis. , vol.135 , pp. 840-847
    • Shore, S.A.1    Kariya, S.T.2    Anderson, K.3    Skornik, W.4    Feldman, H.A.5    Pennington, J.6    Godleski, J.7    Drazen, J.M.8
  • 39
    • 0027051610 scopus 로고
    • Glutathione S-transferases of human lung: Characterization and evaluation of the protective role of the alpha-class isoenzymes against lipid peroxidation
    • Singhal, S. S., Saxena, M., Ahmad, H., Awasthi, S., Haque, A. K., and Awasthi, Y. C. 1992. Glutathione S-transferases of human lung: characterization and evaluation of the protective role of the alpha-class isoenzymes against lipid peroxidation. Arch. Biochem. Biophys. 299:232-241.
    • (1992) Arch. Biochem. Biophys. , vol.299 , pp. 232-241
    • Singhal, S.S.1    Saxena, M.2    Ahmad, H.3    Awasthi, S.4    Haque, A.K.5    Awasthi, Y.C.6
  • 40
    • 0029052167 scopus 로고
    • Increased lipid peroxidation and decreased antioxidants in lungs of guinea pigs following an allergic pulmonary response
    • Shvedova, A. A., Kisin, E. R., Kagan, V. E., and Karol, M. H. 1995. Increased lipid peroxidation and decreased antioxidants in lungs of guinea pigs following an allergic pulmonary response. Tox. Appl. Pharmacol. 132:72-81.
    • (1995) Tox. Appl. Pharmacol. , vol.132 , pp. 72-81
    • Shvedova, A.A.1    Kisin, E.R.2    Kagan, V.E.3    Karol, M.H.4
  • 41
    • 0016343668 scopus 로고
    • Formaldehyde dehydrogenase from human liver
    • Uotila, L., and Koivusalo, M. 1974. Formaldehyde dehydrogenase from human liver. J. Biol. Chem. 249:7653-7663.
    • (1974) J. Biol. Chem. , vol.249 , pp. 7653-7663
    • Uotila, L.1    Koivusalo, M.2
  • 42
    • 0000221995 scopus 로고
    • Glutathione-dependent oxidoreductases: Formaldehyde dehydrogenase
    • eds. D. Dolphin, R. Poulson, and O. Avramovic, New York: John Wiley and Sons
    • Uotila, L., and Koivusalo, M. 1989. Glutathione-dependent oxidoreductases: Formaldehyde dehydrogenase. In Coenzymes and cofactors: Glutathione, eds. D. Dolphin, R. Poulson, and O. Avramovic, Vol. III, pp. 518-549. New York: John Wiley and Sons.
    • (1989) Coenzymes and Cofactors: Glutathione , vol.3 , pp. 518-549
    • Uotila, L.1    Koivusalo, M.2
  • 43
    • 0016411197 scopus 로고
    • Alcohol dehydrogenase from human liver
    • ed. W. A. Wood, New York: Academic Press
    • Woronik, C. L. 1975. Alcohol dehydrogenase from human liver. In Methods of enzymology, ed. W. A. Wood, Vol. XLI, Part B, pp. 369-374. New York: Academic Press.
    • (1975) Methods of Enzymology , vol.41 , Issue.PART B , pp. 369-374
    • Woronik, C.L.1


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