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Volumn 25, Issue 7, 1999, Pages 631-646

Survival, lung injury, and lung protein nitration in heterozygous MnSOD knockout mice in hyperoxia

Author keywords

Hyperoxia; Lung injury; Mice; Mitochondria; Superoxide dismutase

Indexed keywords

3 NITROTYROSINE; GLUTATHIONE PEROXIDASE; GLUTATHIONE REDUCTASE; LACTATE DEHYDROGENASE; MANGANESE SUPEROXIDE DISMUTASE; NITRITE; OXYGEN; STRUCTURAL PROTEIN;

EID: 0032730408     PISSN: 01902148     EISSN: None     Source Type: Journal    
DOI: 10.1080/019021499270060     Document Type: Article
Times cited : (22)

References (28)
  • 1
    • 0024308039 scopus 로고
    • Superoxide dismutases. An adaptation to a paramagnetic gas
    • 1. Fridovich I: Superoxide dismutases. An adaptation to a paramagnetic gas. J Biol Chem. 1989;264:7761-7764.
    • (1989) J Biol Chem , vol.264 , pp. 7761-7764
    • Fridovich, I.1
  • 2
    • 0029781555 scopus 로고    scopus 로고
    • The protective role of MnSOD against adriamycin-induced acute cardiac toxicity in transgenic mice
    • 2. Yen H, Oberly T, Vichitbandha S, Ho Y, St. Clair D: The protective role of MnSOD against adriamycin-induced acute cardiac toxicity in transgenic mice. J Clin Invest. 1996;98:1253-1260.
    • (1996) J Clin Invest , vol.98 , pp. 1253-1260
    • Yen, H.1    Oberly, T.2    Vichitbandha, S.3    Ho, Y.4    St. Clair, D.5
  • 3
    • 0018876186 scopus 로고
    • Structural and biochemical changes in rat lungs occurring during exposures to lethal and adaptive doses of oxygen
    • 3. Crapo JD, Barry BE, Foscue HA, Shelburne J: Structural and biochemical changes in rat lungs occurring during exposures to lethal and adaptive doses of oxygen. Am Rev Respir Dis. 1980;122:123-143.
    • (1980) Am Rev Respir Dis , vol.122 , pp. 123-143
    • Crapo, J.D.1    Barry, B.E.2    Foscue, H.A.3    Shelburne, J.4
  • 4
    • 33745368131 scopus 로고    scopus 로고
    • Antioxidant enzyme expression in rat lungs during hyperoxia
    • 4. Ho Y, Dey MS, Crapo J: Antioxidant enzyme expression in rat lungs during hyperoxia. Am J Physiol. 1996;270:L810-L818.
    • (1996) Am J Physiol , vol.270
    • Ho, Y.1    Dey, M.S.2    Crapo, J.3
  • 5
    • 0027398030 scopus 로고
    • Tolerance of rats to hyperoxia: Lung antioxidant enzyme gene expression
    • 5. Clerch LB, Massaro D: Tolerance of rats to hyperoxia: lung antioxidant enzyme gene expression. J Clin Invest. 1993;91:499-508.
    • (1993) J Clin Invest , vol.91 , pp. 499-508
    • Clerch, L.B.1    Massaro, D.2
  • 6
    • 0028364341 scopus 로고
    • Pertussis toxin treatment alters manganese superoxide dismutase activity in lung: Evidence for lung oxygen toxicity in air-breathing rats
    • 6. Clerch LB, Neithardt G, Spencer U, Melendez JA, Massaro GD, Massaro D: Pertussis toxin treatment alters manganese superoxide dismutase activity in lung: evidence for lung oxygen toxicity in air-breathing rats. J Clin Invest. 1994;93:2482-2489.
    • (1994) J Clin Invest , vol.93 , pp. 2482-2489
    • Clerch, L.B.1    Neithardt, G.2    Spencer, U.3    Melendez, J.A.4    Massaro, G.D.5    Massaro, D.6
  • 7
    • 0002782889 scopus 로고    scopus 로고
    • Lung antioxidant enzyme gene expression and tolerance to hyperoxia
    • Clerch L, Massaro D, eds. New York: Marcel Dekker
    • 7. Clerch L, Massaro D: Lung antioxidant enzyme gene expression and tolerance to hyperoxia. In: Clerch L, Massaro D, eds. Oxygen, Gene Expression and Cellular Function. New York: Marcel Dekker; 1997:399-424.
    • (1997) Oxygen, Gene Expression and Cellular Function , pp. 399-424
    • Clerch, L.1    Massaro, D.2
  • 9
    • 0027536243 scopus 로고
    • Immunolocalization of manganese superoxide dismutase in normal and transgenic mice expressing the human enzyme
    • 9. Oberley TD, Coursin DB, Cihla HP, Oberley LW, El-Sayyad N, Ho Y: Immunolocalization of manganese superoxide dismutase in normal and transgenic mice expressing the human enzyme. Histochem J. 1993;25:267-279.
    • (1993) Histochem J , vol.25 , pp. 267-279
    • Oberley, T.D.1    Coursin, D.B.2    Cihla, H.P.3    Oberley, L.W.4    El-Sayyad, N.5    Ho, Y.6
  • 11
    • 0029064257 scopus 로고
    • Superoxide radical and iron modulate aconitase activity in mammalian cells
    • 11. Gardner P, Raineri I, Epstein L, White C: Superoxide radical and iron modulate aconitase activity in mammalian cells. J Biol Chem. 1995;270:13399-13405.
    • (1995) J Biol Chem , vol.270 , pp. 13399-13405
    • Gardner, P.1    Raineri, I.2    Epstein, L.3    White, C.4
  • 14
    • 0028007172 scopus 로고
    • Quantitation of nitrotyrosine levels in lung sections of patients and animals with acute lung injury
    • 14. Haddad IY, Pataki G, Hu P, Galliani C, Beckman JS, Matalon, S: Quantitation of nitrotyrosine levels in lung sections of patients and animals with acute lung injury. J Clin Invest. 1994;94:2407-2413.
    • (1994) J Clin Invest , vol.94 , pp. 2407-2413
    • Haddad, I.Y.1    Pataki, G.2    Hu, P.3    Galliani, C.4    Beckman, J.S.5    Matalon, S.6
  • 15
    • 0017148259 scopus 로고
    • A general method for isolation of high molecular weight DNA from eukaryotes
    • 15. Blin N, Stafford D: A general method for isolation of high molecular weight DNA from eukaryotes. Nucleic Acids Res. 1976;3:2303-2308.
    • (1976) Nucleic Acids Res , vol.3 , pp. 2303-2308
    • Blin, N.1    Stafford, D.2
  • 16
    • 0014691242 scopus 로고
    • An enzymic function for erythrocuprein
    • 16. McCord J, Fridovich I: An enzymic function for erythrocuprein. J Biol Chem. 1969;22:6049-6055.
    • (1969) J Biol Chem , vol.22 , pp. 6049-6055
    • McCord, J.1    Fridovich, I.2
  • 17
    • 0015848173 scopus 로고
    • Superoxide dismutase: Organelle specificity
    • 17. Weisenger R, Fridovich I: Superoxide dismutase: Organelle specificity. J Biol Chem. 1973;28:3582-3592.
    • (1973) J Biol Chem , vol.28 , pp. 3582-3592
    • Weisenger, R.1    Fridovich, I.2
  • 18
    • 0014108436 scopus 로고
    • Studies on the quantitative and qualitative characterization of erythrocyte glutathione peroxidase
    • 18. Paglia DE, Valentine WN: Studies on the quantitative and qualitative characterization of erythrocyte glutathione peroxidase. J Lab Clin Med. 1967;70:158-169.
    • (1967) J Lab Clin Med , vol.70 , pp. 158-169
    • Paglia, D.E.1    Valentine, W.N.2
  • 19
    • 0003108672 scopus 로고
    • Glutathione reductase
    • Bergmeyer HU, ed. New York: Academic Press
    • 19. Horn HD: Glutathione reductase. In: Methods of Enzymatic Analysis, Bergmeyer HU, ed. New York: Academic Press: 1965:875-879.
    • (1965) Methods of Enzymatic Analysis , pp. 875-879
    • Horn, H.D.1
  • 20
    • 41049100518 scopus 로고
    • A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase
    • 20. Beers RF, Sizer JW: A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase. J Biol Chem. 1952;195:133-140.
    • (1952) J Biol Chem , vol.195 , pp. 133-140
    • Beers, R.F.1    Sizer, J.W.2
  • 21
    • 75449147506 scopus 로고
    • Serum lactic dehydrogenase activity: An analytical assessment of current assays
    • 21. Amador E, Dorfman LE, Wacker WEC: Serum lactic dehydrogenase activity: an analytical assessment of current assays. Clin Chem. 1963;9:391-399.
    • (1963) Clin Chem , vol.9 , pp. 391-399
    • Amador, E.1    Dorfman, L.E.2    Wacker, W.E.C.3
  • 22
    • 0030969993 scopus 로고    scopus 로고
    • Adaptation of the nitrate reductase and Griess reaction methods for the measurement of serum nitrate plus nitrite levels
    • 22. Giovannoni G, Land JM, Keir G, Thompson EJ, Heales SJ: Adaptation of the nitrate reductase and Griess reaction methods for the measurement of serum nitrate plus nitrite levels. Ann Clin Biochem. 1997;34 (Pt 2):193-198.
    • (1997) Ann Clin Biochem , vol.34 , Issue.PT 2 , pp. 193-198
    • Giovannoni, G.1    Land, J.M.2    Keir, G.3    Thompson, E.J.4    Heales, S.J.5
  • 24
    • 0021362496 scopus 로고
    • Some statistical and experimental considerations in the use of analysis of variance procedures
    • 24. Denenburg V: Some statistical and experimental considerations in the use of analysis of variance procedures. Am J Physiol. 1984;246(4 Pt 2):R403-R408.
    • (1984) Am J Physiol , vol.246 , Issue.4 PT 2
    • Denenburg, V.1
  • 25
    • 0039604509 scopus 로고
    • A yeast mutant lacking mitochondrial manganese-superoxide dismutase is hypersensitive to oxygen
    • 25. van Loon APGM, Pesold-Hurt B, Schatz G: A yeast mutant lacking mitochondrial manganese-superoxide dismutase is hypersensitive to oxygen. Proc Natl Acad Sci USA. 1986;83:3820-3824.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 3820-3824
    • Van Loon, A.P.G.M.1    Pesold-Hurt, B.2    Schatz, G.3
  • 26
    • 0027491617 scopus 로고
    • The inactivation of Fe-S cluster containing hydro-lyases by superoxide
    • 26. Flint DH, Tuminello JF, Emptage M: The inactivation of Fe-S cluster containing hydro-lyases by superoxide. J Biol Chem. 1993;268:22369-22376.
    • (1993) J Biol Chem , vol.268 , pp. 22369-22376
    • Flint, D.H.1    Tuminello, J.F.2    Emptage, M.3
  • 27
    • 0028075773 scopus 로고
    • Aconitase is a sensitive and critical target of oxygen poisoning in cultured mammalian cells and in rat lungs
    • 27. Gardner PR, Nguyen DH, White CW: Aconitase is a sensitive and critical target of oxygen poisoning in cultured mammalian cells and in rat lungs. Proc Natl Acad Sci USA. 1994;91:12248-12252.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 12248-12252
    • Gardner, P.R.1    Nguyen, D.H.2    White, C.W.3
  • 28
    • 0032561328 scopus 로고    scopus 로고
    • Increased oxidative damage is correlated to altered mitochondrial function in heterozygous manganese superoxide dismutase knockout mice
    • 28. Williams M, Van Remmen H, Conrad C, Huang T, Epstein C, Richardson A: Increased oxidative damage is correlated to altered mitochondrial function in heterozygous manganese superoxide dismutase knockout mice. J Biol Chem. 1998;273:28510-28515.
    • (1998) J Biol Chem , vol.273 , pp. 28510-28515
    • Williams, M.1    Van Remmen, H.2    Conrad, C.3    Huang, T.4    Epstein, C.5    Richardson, A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.