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Volumn 274, Issue 5 18-5, 1998, Pages

Ascorbate-mediated transplasma membrane electron transport in pulmonary arterial endothelial cells

Author keywords

Ascorbic acid transport; Cytochrome c; Dehydroascorbic acid; Dehydroascorbic acid transport; Endothelial cell column; Ferricyanide; Methylene blue

Indexed keywords

CYTOCHROME C; DEHYDROASCORBIC ACID; FERRICYANIDE; FREE RADICAL; METHYLENE BLUE;

EID: 0031862303     PISSN: 10400605     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajplung.1998.274.5.l685     Document Type: Article
Times cited : (26)

References (26)
  • 1
    • 0018718024 scopus 로고
    • A novel lipid hydroperoxide-reducing enzyme in human erythrocyte membranes
    • Agutter, P. S., R. V. Sherriff, and M. Kadlubowski. A novel lipid hydroperoxide-reducing enzyme in human erythrocyte membranes. Biochem. Soc. Trans. 7: 710-711, 1979.
    • (1979) Biochem. Soc. Trans. , vol.7 , pp. 710-711
    • Agutter, P.S.1    Sherriff, R.V.2    Kadlubowski, M.3
  • 3
    • 0029150534 scopus 로고
    • Reduction of thiazine dyes by bovine pulmonary arterial endothelial cells in culture
    • Lung Cell. Mol. Physiol. 13
    • Bongard, R. D., M. P. Merker, R. Shundo, Y. Okamoto, D. L. Roerig, J. H. Linehan, and C. A. Dawson. Reduction of thiazine dyes by bovine pulmonary arterial endothelial cells in culture. Am. J. Physiol. 269 (Lung Cell. Mol. Physiol. 13): L78-L84, 1995.
    • (1995) Am. J. Physiol. , vol.269
    • Bongard, R.D.1    Merker, M.P.2    Shundo, R.3    Okamoto, Y.4    Roerig, D.L.5    Linehan, J.H.6    Dawson, C.A.7
  • 4
    • 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. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248-252, 1976.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-252
    • Bradford, M.M.1
  • 6
    • 0027313602 scopus 로고
    • Transplasma membrane redox system in HL-60 cells is modulated during TPA-induced differentiation
    • Buron, M. I., J. C. Rodriguez-Aguilera, F. J. Alcain, and P. Navas. Transplasma membrane redox system in HL-60 cells is modulated during TPA-induced differentiation. Biochem. Biophys. Res. Commun. 192: 439-445, 1993.
    • (1993) Biochem. Biophys. Res. Commun. , vol.192 , pp. 439-445
    • Buron, M.I.1    Rodriguez-Aguilera, J.C.2    Alcain, F.J.3    Navas, P.4
  • 7
    • 0026092089 scopus 로고
    • Electron and proton transport across the plasma membrane
    • Crane, F., I. L. Sun, R. Barr, and H. Low. Electron and proton transport across the plasma membrane. J. Bioenerg. Biomembr. 23: 773-803, 1991.
    • (1991) J. Bioenerg. Biomembr. , vol.23 , pp. 773-803
    • Crane, F.1    Sun, I.L.2    Barr, R.3    Low, H.4
  • 9
    • 0028802762 scopus 로고
    • The uptake of ascorbic acid into human umbilical vein endothelial cells and its effect on oxidant insult
    • Ek, A., K. Strom, and I. A. Cotgreave. The uptake of ascorbic acid into human umbilical vein endothelial cells and its effect on oxidant insult. Biochem. Pharmacol. 50: 1339-1346, 1995.
    • (1995) Biochem. Pharmacol. , vol.50 , pp. 1339-1346
    • Ek, A.1    Strom, K.2    Cotgreave, I.A.3
  • 10
    • 0028902789 scopus 로고
    • Reduction of Fe(III) is required for uptake of nonheme iron by Caco-2 cells
    • Han, O., M. L. Failla, A. D. Hill, E. R. Morris, and J. C. Smith. Reduction of Fe(III) is required for uptake of nonheme iron by Caco-2 cells. J. Nutr. 125: 1291-1299, 1995.
    • (1995) J. Nutr. , vol.125 , pp. 1291-1299
    • Han, O.1    Failla, M.L.2    Hill, A.D.3    Morris, E.R.4    Smith, J.C.5
  • 11
    • 4544230423 scopus 로고    scopus 로고
    • Technical bulletin
    • Hyclone Laboratories. Technical bulletin. Art to Science 15: 1-5, 1996.
    • (1996) Art to Science , vol.15 , pp. 1-5
  • 12
    • 0029045698 scopus 로고
    • Ascorbate is the major electron donor for a transmembrane oxidoreductase of human erythrocytes
    • May, J. M., Z. Qu, and R. R. Whitesell. Ascorbate is the major electron donor for a transmembrane oxidoreductase of human erythrocytes. Biochim. Biophys. Acta 1238: 127-136, 1995.
    • (1995) Biochim. Biophys. Acta , vol.1238 , pp. 127-136
    • May, J.M.1    Qu, Z.2    Whitesell, R.R.3
  • 17
    • 0018426388 scopus 로고
    • An ascorbate-mediated transmembrane-reducing system of the human erythrocyte
    • Orringer, E. P., and M. E. S. Roer. An ascorbate-mediated transmembrane-reducing system of the human erythrocyte. J. Clin. Invest. 63: 53-58, 1979.
    • (1979) J. Clin. Invest. , vol.63 , pp. 53-58
    • Orringer, E.P.1    Roer, M.E.S.2
  • 18
    • 0027057945 scopus 로고
    • Tissue-mediated regeneration of ascorbic acid: Is the process enzymatic?
    • Rose, R. C., and A. M. Bode. Tissue-mediated regeneration of ascorbic acid: is the process enzymatic? Enzymes 46: 196-203, 1992.
    • (1992) Enzymes , vol.46 , pp. 196-203
    • Rose, R.C.1    Bode, A.M.2
  • 19
    • 0027327373 scopus 로고
    • Biology of free radical scavengers: An evaluation of ascorbate
    • Rose, R. C., and A. M. Bode. Biology of free radical scavengers: an evaluation of ascorbate. FASEB J. 7: 1135-1142, 1993.
    • (1993) FASEB J. , vol.7 , pp. 1135-1142
    • Rose, R.C.1    Bode, A.M.2
  • 20
    • 0021859814 scopus 로고
    • Reduction of extracellular potassium ferricyanide by transmembrane NADH: (acceptor) oxidoreductase of human erythrocytes
    • Schipfer, W., B. Neophytou, R. Trobisch, O. Groiss, and H. Goldenberg. Reduction of extracellular potassium ferricyanide by transmembrane NADH: (acceptor) oxidoreductase of human erythrocytes. Int. J. Biochem. 17: 819-823, 1985.
    • (1985) Int. J. Biochem. , vol.17 , pp. 819-823
    • Schipfer, W.1    Neophytou, B.2    Trobisch, R.3    Groiss, O.4    Goldenberg, H.5
  • 21
    • 0029065701 scopus 로고
    • Coenzyme Q reductase from liver plasma membrane: Purification and role in transplasma-membrane electron transport
    • Villalba, J. M., F. Navarro, F. Cordoba, A. Serrano, A. Arroyo, F. L. Crane, and P. Navas. Coenzyme Q reductase from liver plasma membrane: purification and role in transplasma-membrane electron transport. Proc. Natl. Acad. Sci. USA 92: 4887-4891, 1995.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 4887-4891
    • Villalba, J.M.1    Navarro, F.2    Cordoba, F.3    Serrano, A.4    Arroyo, A.5    Crane, F.L.6    Navas, P.7
  • 22
    • 0019132671 scopus 로고
    • Human erythrocyte NADH: (acceptor) oxidoreductase. Kinetic properties and competitive substrate inhibition by ferricyanide
    • Wang, C. S. Human erythrocyte NADH: (acceptor) oxidoreductase. Kinetic properties and competitive substrate inhibition by ferricyanide. Biochim. Biophys. Acta 616: 22-29, 1980.
    • (1980) Biochim. Biophys. Acta , vol.616 , pp. 22-29
    • Wang, C.S.1
  • 23
    • 0030154883 scopus 로고    scopus 로고
    • Ascorbate uptake by microvascular endothelial cells of rat skeletal muscle
    • Wilson, J. X., S. J. Dixon, J. Yu, S. Nees, and K. Tyml. Ascorbate uptake by microvascular endothelial cells of rat skeletal muscle. Microcirculation 3: 211-221, 1996.
    • (1996) Microcirculation , vol.3 , pp. 211-221
    • Wilson, J.X.1    Dixon, S.J.2    Yu, J.3    Nees, S.4    Tyml, K.5
  • 25
    • 0029194524 scopus 로고
    • Release of hydrogen peroxide in response to hypoxia-reoxygenation: Role of an NAD(P)H oxidase-like enzyme in endothelial cell plasma membrane
    • Zulueta, J. J., F.-S. Yu, I. A. Hertig, and V. J. Thanickal. Release of hydrogen peroxide in response to hypoxia-reoxygenation: role of an NAD(P)H oxidase-like enzyme in endothelial cell plasma membrane. Am. J. Respir. Cell Mol. Biol. 12: 41-49, 1995.
    • (1995) Am. J. Respir. Cell Mol. Biol. , vol.12 , pp. 41-49
    • Zulueta, J.J.1    Yu, F.-S.2    Hertig, I.A.3    Thanickal, V.J.4
  • 26
    • 0028118478 scopus 로고
    • An NADH-diaphorase is located at the cell plasma membrane in a mouse neuroblastoma cell line NB41A3
    • Zurbriggen, R., and J. L. Dreyer. An NADH-diaphorase is located at the cell plasma membrane in a mouse neuroblastoma cell line NB41A3. Biochim. Biophys. Acta 1183: 513-520, 1994.
    • (1994) Biochim. Biophys. Acta , vol.1183 , pp. 513-520
    • Zurbriggen, R.1    Dreyer, J.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.