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Volumn 26, Issue 3, 1998, Pages 388-394

Metal Storage and Transport Proteins Increase After Exposure of the Rat Lung to an Air Pollution Particle

Author keywords

Air pollution; ferritin; iron; lactoferrin; transferrin

Indexed keywords

CARRIER PROTEIN; FERRITIN; IRON BINDING PROTEIN; LACTOFERRIN; METAL; TRANSFERRIN;

EID: 0031965963     PISSN: 01926233     EISSN: None     Source Type: Journal    
DOI: 10.1177/019262339802600313     Document Type: Article
Times cited : (30)

References (31)
  • 1
    • 0018850440 scopus 로고
    • Iron transport and storage proteins
    • Aisen P and Listowsky I (1980). Iron transport and storage proteins. Anmi. Rev. Biochem. 49: 357-393.
    • (1980) Anmi. Rev. Biochem. , vol.49 , pp. 357-393
    • Aisen, P.1    Listowsky, I.2
  • 2
    • 0027502831 scopus 로고
    • An enzyme-linked immunosorbent assay for plasma-lactoferrin. Concentrations in 362 healthy, adult blood donors
    • Antonsen S, Wiggers P, Dalhoj J, and Blaabjerg O (1993). An enzyme-linked immunosorbent assay for plasma-lactoferrin. Concentrations in 362 healthy, adult blood donors. Scand. J. Clin. Lab. Invest. 53: 133-144.
    • (1993) Scand. J. Clin. Lab. Invest. , vol.53 , pp. 133-144
    • Antonsen, S.1    Wiggers, P.2    Dalhoj, J.3    Blaabjerg, O.4
  • 4
    • 0021635457 scopus 로고
    • The biological significance of lactoferrin in hematology
    • Birgens HS (1984). The biological significance of lactoferrin in hematology. Scand. J. Haematol. 33: 225-230.
    • (1984) Scand. J. Haematol. , vol.33 , pp. 225-230
    • Birgens, H.S.1
  • 6
    • 0019457092 scopus 로고
    • Ultrastructural localization of lactoferrin and glycoprotein in human bronchial glands
    • Bowes D, Clark AE, and Corin B (1981). Ultrastructural localization of lactoferrin and glycoprotein in human bronchial glands. Thorax 36: 108-115.
    • (1981) Thorax , vol.36 , pp. 108-115
    • Bowes, D.1    Clark, A.E.2    Corin, B.3
  • 7
    • 0021746936 scopus 로고
    • Effect of iron chelators on the transferrin receptor in K562 cells
    • Bridges KR and Cudkowicz A (1984). Effect of iron chelators on the transferrin receptor in K562 cells. J. Biol. Chem. 259: 12970-12977.
    • (1984) J. Biol. Chem. , vol.259 , pp. 12970-12977
    • Bridges, K.R.1    Cudkowicz, A.2
  • 10
    • 0025612310 scopus 로고
    • Iron detoxifying activity of ferritin. Effects of H and L human apoferritins on lipid peroxidation in vitro
    • Cozzi A, Santambrogio P, Levi S, and Arosio P (1990). Iron detoxifying activity of ferritin. Effects of H and L human apoferritins on lipid peroxidation in vitro. FEBS Lett. 277: 119-122.
    • (1990) FEBS Lett. , vol.277 , pp. 119-122
    • Cozzi, A.1    Santambrogio, P.2    Levi, S.3    Arosio, P.4
  • 12
    • 0030614430 scopus 로고    scopus 로고
    • Non-heme [Fe3+] in the lung increases with age in both the rat and man
    • Ghio AJ, Pritchard RJ, Dietrich K, and Samet JM (1997). Non-heme [Fe3+] in the lung increases with age in both the rat and man. J. Lab. Clin. Med. 129: 53-61.
    • (1997) J. Lab. Clin. Med. , vol.129 , pp. 53-61
    • Ghio, A.J.1    Pritchard, R.J.2    Dietrich, K.3    Samet, J.M.4
  • 13
    • 0029893572 scopus 로고    scopus 로고
    • Pro-oxidant iron is present in human pulmonary epithelial lining fluid: Implications for oxidative stress in the lung
    • Gutteridge JMC, Mumby S, Quinlan GJ, Chung KF, and Evans TW (1996). Pro-oxidant iron is present in human pulmonary epithelial lining fluid: Implications for oxidative stress in the lung. Biochem. Biophys. Res. Commim. 220: 1024-1027.
    • (1996) Biochem. Biophys. Res. Commim. , vol.220 , pp. 1024-1027
    • Gutteridge, J.M.C.1    Mumby, S.2    Quinlan, G.J.3    Chung, K.F.4    Evans, T.W.5
  • 14
    • 0030823134 scopus 로고    scopus 로고
    • In vivo evidence of free radical formation in the rat lung after exposure to an emission source air pollution particle
    • Kadiiska MB, Mason RP, Dreher KL, Costa DL, and Ghio AJ (1997). In vivo evidence of free radical formation in the rat lung after exposure to an emission source air pollution particle. Chem. Res. Toxicol. 10: 1104-1108.
    • (1997) Chem. Res. Toxicol. , vol.10 , pp. 1104-1108
    • Kadiiska, M.B.1    Mason, R.P.2    Dreher, K.L.3    Costa, D.L.4    Ghio, A.J.5
  • 15
    • 0028881483 scopus 로고
    • Iron metabolism and its regulation Ann
    • Lash A and Saleem A (1995). Iron metabolism and its regulation Ann. Clin. Lab. Set. 25: 20-30.
    • (1995) Clin. Lab. Set. , vol.25 , pp. 20-30
    • Lash, A.1    Saleem, A.2
  • 16
    • 0026684574 scopus 로고
    • Iron-dependent regulation of ferritin and transferrin receptor expression by the iron-responsive element binding protein
    • Leibold EA and Guo B (1992). Iron-dependent regulation of ferritin and transferrin receptor expression by the iron-responsive element binding protein. Annu. Rev. Nutr. 12: 345-368.
    • (1992) Annu. Rev. Nutr. , vol.12 , pp. 345-368
    • Leibold, E.A.1    Guo, B.2
  • 17
    • 0026580685 scopus 로고
    • Antioxidant activity of bronchoalveolar lavage fluid in the adult respiratory distress syn. drome
    • Lykens MG, Davis WB, and Pacht ER (1992). Antioxidant activity of bronchoalveolar lavage fluid in the adult respiratory distress syn. drome. Am. J. Physiol. 262: L169–L175.
    • (1992) Am. J. Physiol. , vol.262 , pp. L169-L175
    • Lykens, M.G.1    Davis, W.B.2    Pacht, E.R.3
  • 18
    • 0018756880 scopus 로고
    • Binding and ingestion of human lactoferrin by mouse alveolar macrophages
    • Markowetz B, Van Snick JL, and Masson PL (1979). Binding and ingestion of human lactoferrin by mouse alveolar macrophages Thorax 34: 209-212.
    • (1979) Thorax , vol.34 , pp. 209-212
    • Markowetz, B.1    Van Snick, J.L.2    Masson, P.L.3
  • 19
    • 0020960235 scopus 로고
    • Comparative study of the iron-binding properties of human transferrins. Electron paramagnetic resonance of mixed metal complexes of human lactotransferrin
    • Mazurier J, Lhoste JM, Montreuil J, and Spik G (1983). Comparative study of the iron-binding properties of human transferrins. Electron paramagnetic resonance of mixed metal complexes of human lactotransferrin. Biochim. Biophys. Acta 745: 44-49.
    • (1983) Biochim. Biophys. Acta , vol.745 , pp. 44-49
    • Mazurier, J.1    Lhoste, J.M.2    Montreuil, J.3    Spik, G.4
  • 20
    • 0027502154 scopus 로고
    • Iron sequestration by macrophages decreases the potential for extracellular hydroxyl radical formation
    • Olakanmi O, McGowan SE, Hayek MB, and Britigan BE (1993). Iron sequestration by macrophages decreases the potential for extracellular hydroxyl radical formation. J. Clin. Invest. 91: 889-899.
    • (1993) J. Clin. Invest. , vol.91 , pp. 889-899
    • Olakanmi, O.1    McGowan, S.E.2    Hayek, M.B.3    Britigan, B.E.4
  • 21
    • 0023923526 scopus 로고
    • Role of transferrin and cerulo-plasmin in antioxidant activity of lung epithelial lining fluid
    • Pacht ER and Davis WB (1988). Role of transferrin and cerulo-plasmin in antioxidant activity of lung epithelial lining fluid. J. Appl. Physiol. 64: 2092-2099.
    • (1988) J. Appl. Physiol. , vol.64 , pp. 2092-2099
    • Pacht, E.R.1    Davis, W.B.2
  • 22
    • 0029788182 scopus 로고    scopus 로고
    • Oxidant generation and lung injury after exposure to particulate air pollutants are associated with concentrations of complexed iron
    • Pritchard RJ, Ghio AJ, Park P, Gilmour MI, Lehmann J, Winsett DW, Dreher KL, and Costa DL (1996). Oxidant generation and lung injury after exposure to particulate air pollutants are associated with concentrations of complexed iron. Inhal. Toxicol. 8: 457-477.
    • (1996) Inhal. Toxicol. , vol.8 , pp. 457-477
    • Pritchard, R.J.1    Ghio, A.J.2    Park, P.3    Gilmour, M.I.4    Lehmann, J.5    Winsett, D.W.6    Dreher, K.L.7    Costa, D.L.8
  • 23
    • 0021919938 scopus 로고
    • Effects of alterations in cellular iron on biosynthesis of the transferrin receptor in K562 cells
    • Rao KK, Schapiro D, Mattia E, Bridges K, and Klausner RD (1985). Effects of alterations in cellular iron on biosynthesis of the transferrin receptor in K562 cells. Mol. Cell. Biol. 5: 595-600.
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 595-600
    • Rao, K.K.1    Schapiro, D.2    Mattia, E.3    Bridges, K.4    Klausner, R.D.5
  • 24
    • 0023713448 scopus 로고
    • Binding of a cytosolic protein to the iron-responsive element of human ferritin messenger RNA
    • Rouault TA, Hentze MW, Wright-Caughman S, Harford JB, and Klausner RD (1988). Binding of a cytosolic protein to the iron-responsive element of human ferritin messenger RNA. Science 241: 1207-1210.
    • (1988) Science , vol.241 , pp. 1207-1210
    • Rouault, T.A.1    Hentze, M.W.2    Wright-Caughman, S.3    Harford, J.B.4    Klausner, R.D.5
  • 25
    • 0030010952 scopus 로고    scopus 로고
    • Metal-ion binding properties of the transferrins: A vanadium-51 NMR study
    • Saponja JA and Vogel HJ (1996). Metal-ion binding properties of the transferrins: A vanadium-51 NMR study. J. Inorg. Biochem. 62: 253-270.
    • (1996) J. Inorg. Biochem. , vol.62 , pp. 253-270
    • Saponja, J.A.1    Vogel, H.J.2
  • 27
    • 0028798434 scopus 로고
    • Oxidative mechanisms in the toxicity of metal ions
    • Stohs SJ and Bagchi D (1995). Oxidative mechanisms in the toxicity of metal ions. Free Radical Biol. Med. 18: 321-336.
    • (1995) Free Radical Biol. Med. , vol.18 , pp. 321-336
    • Stohs, S.J.1    Bagchi, D.2
  • 28
    • 0025255103 scopus 로고
    • Lower respiratory tract lactoferrin and lysozyme arise primarily in the airways and are elevated in association with chronic bronchitis
    • Thompson AB, Bohling T, Payvandi F, and Rennard SI (1990). Lower respiratory tract lactoferrin and lysozyme arise primarily in the airways and are elevated in association with chronic bronchitis. J. Lab. Clin. Med. 115: 148-158.
    • (1990) J. Lab. Clin. Med. , vol.115 , pp. 148-158
    • Thompson, A.B.1    Bohling, T.2    Payvandi, F.3    Rennard, S.I.4
  • 29
    • 0025094141 scopus 로고
    • The role of transferrin in the mechanism of cellular iron uptake
    • Thorstensen K and Romslo I (1990). The role of transferrin in the mechanism of cellular iron uptake. Biochem. J. 271: 1-9.
    • (1990) Biochem. J. , vol.271 , pp. 1-9
    • Thorstensen, K.1    Romslo, I.2
  • 30
    • 0017746767 scopus 로고
    • The ingestion and digestion of human lactoferrin by mouse peritoneal macrophages and the transfer of its iron into ferritin
    • Van Snick JL, Markowetz B, and Masson PL (1977). The ingestion and digestion of human lactoferrin by mouse peritoneal macrophages and the transfer of its iron into ferritin. J. Exp. Med. 146: 817-827.
    • (1977) J. Exp. Med. , vol.146 , pp. 817-827
    • Van Snick, J.L.1    Markowetz, B.2    Masson, P.L.3
  • 31
    • 0021719812 scopus 로고
    • Heme regulation of HeLa cell transferrin receptor number
    • Ward JH, Jordan I, Kushner JP, and Kaplan J (1984). Heme regulation of HeLa cell transferrin receptor number. J. Biol. Chem. 259: 13235-13240.
    • (1984) J. Biol. Chem. , vol.259 , pp. 13235-13240
    • Ward, J.H.1    Jordan, I.2    Kushner, J.P.3    Kaplan, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.