메뉴 건너뛰기




Volumn 6, Issue 4, 2005, Pages 320-326

Red cell membrane lipid changes at 3500 m and on return to sea level

Author keywords

Altitude; Erythrocyte; Hypoxia reoxygenation; Oxidation; Phospholipids

Indexed keywords

LAURDAN; MALONALDEHYDE; MEMBRANE LIPID; PHOSPHOLIPID;

EID: 31344480965     PISSN: 15270297     EISSN: None     Source Type: Journal    
DOI: 10.1089/ham.2005.6.320     Document Type: Article
Times cited : (13)

References (30)
  • 1
    • 0033212099 scopus 로고    scopus 로고
    • A model for the interaction of 6-lauryl-2(N-N-dimethylamino) naphtalene with lipid environments: Implications for spectral properties
    • Bagatolli L.A., Parasassi T., Fidelio G.T., and Gratton E. (1999). A model for the interaction of 6-lauryl-2(N-N-dimethylamino) naphtalene with lipid environments: implications for spectral properties. Photochem. Photobiol. 70:557-564.
    • (1999) Photochem. Photobiol. , vol.70 , pp. 557-564
    • Bagatolli, L.A.1    Parasassi, T.2    Fidelio, G.T.3    Gratton, E.4
  • 2
    • 0019456631 scopus 로고
    • Aging of the erythrocyte. II. Activities of peroxide-detoxifying enzymes
    • Bartosz G., and Bartkowiak A. (1981). Aging of the erythrocyte. II. Activities of peroxide-detoxifying enzymes. Experientia. 37:722.
    • (1981) Experientia , vol.37 , pp. 722
    • Bartosz, G.1    Bartkowiak, A.2
  • 3
    • 0026036015 scopus 로고
    • Erythrocyte aging: Physical and chemical membrane changes
    • Bartosz G. (1991). Erythrocyte aging: physical and chemical membrane changes. Gerontology 37:33-67.
    • (1991) Gerontology , vol.37 , pp. 33-67
    • Bartosz, G.1
  • 4
    • 0032416857 scopus 로고    scopus 로고
    • Membrane lipid diffusion and band 3 protein changes in human erythrocytes due to acute hypobaric hypoxia
    • Celedón G., González G., Sotomayor C.P., and Behn C. (1998). Membrane lipid diffusion and band 3 protein changes in human erythrocytes due to acute hypobaric hypoxia. Am. J. Physiol. 275:C1429-C1431.
    • (1998) Am. J. Physiol. , vol.275
    • Celedón, G.1    González, G.2    Sotomayor, C.P.3    Behn, C.4
  • 5
    • 0035185268 scopus 로고    scopus 로고
    • Free-radical-induced protein degradation of erythrocyte membrane is influenced by the localization of radical generation
    • Celedón G., González G., Lissi E.A., and Hidalgo G. (2001a). Free-radical-induced protein degradation of erythrocyte membrane is influenced by the localization of radical generation. IUBMB Life 51:377-380.
    • (2001) IUBMB Life , vol.51 , pp. 377-380
    • Celedón, G.1    González, G.2    Lissi, E.A.3    Hidalgo, G.4
  • 6
    • 0035117422 scopus 로고    scopus 로고
    • Contribution of hemoglobin and membrane constituents modification to human erythrocyte damage promoted by peroxyl radicals of different charge and hydrophobicity
    • Celedón G., Rodriguez I., España J., Escobar J., and Lissi E.A. (2001b). Contribution of hemoglobin and membrane constituents modification to human erythrocyte damage promoted by peroxyl radicals of different charge and hydrophobicity. Free Radical Res. 34:17-31.
    • (2001) Free Radical Res. , vol.34 , pp. 17-31
    • Celedón, G.1    Rodriguez, I.2    España, J.3    Escobar, J.4    Lissi, E.A.5
  • 7
    • 0024512739 scopus 로고
    • Hypoxia, reactive oxygen and cell injury
    • Degroot H., and Littauer A. (1989). Hypoxia, reactive oxygen and cell injury. Free Radical Biol. Med. 6:541-551.
    • (1989) Free Radical Biol. Med. , vol.6 , pp. 541-551
    • Degroot, H.1    Littauer, A.2
  • 8
    • 0035122243 scopus 로고    scopus 로고
    • Malondialdehyde, glutathion peroxidase and superoxide dismutase in peripheral blood erythrocytes of patients with acute cerebral ischemia
    • Demirkaya S., Topcuoglu M.A., Aydin A., Ulas U.H., Isimer A.I., and Vural O. (2001). Malondialdehyde, glutathion peroxidase and superoxide dismutase in peripheral blood erythrocytes of patients with acute cerebral ischemia. Eur. J. Neurol. 8:43-51.
    • (2001) Eur. J. Neurol. , vol.8 , pp. 43-51
    • Demirkaya, S.1    Topcuoglu, M.A.2    Aydin, A.3    Ulas, U.H.4    Isimer, A.I.5    Vural, O.6
  • 9
    • 50549175610 scopus 로고
    • The preparation and chemical characterization of hemoglobin-free ghosts of human erythrocytes
    • Dodge J.T., Mitchell C., and Hanahan D.J. (1963). The preparation and chemical characterization of hemoglobin-free ghosts of human erythrocytes. Arch. Biochem. Biophys. 100:119-130.
    • (1963) Arch. Biochem. Biophys. , vol.100 , pp. 119-130
    • Dodge, J.T.1    Mitchell, C.2    Hanahan, D.J.3
  • 10
    • 0021288842 scopus 로고
    • Detection of malondialdehyde by high-performance liquid chromatography
    • Esterbauer H., Lang J., Zadravec S., and Slater T.F. (1984). Detection of malondialdehyde by high-performance liquid chromatography. Methods Enzymol. 105:319-328.
    • (1984) Methods Enzymol. , vol.105 , pp. 319-328
    • Esterbauer, H.1    Lang, J.2    Zadravec, S.3    Slater, T.F.4
  • 11
    • 0019156271 scopus 로고
    • Changes in some cytoplasmic enzymes from red cells fractionated into age groups by centrifugation in Ficoll-Triosil gradients. Comparison of normal humans with with Duchenne muscular dystrophy
    • Galbraith D.A., and Watts D.C. (1980). Changes in some cytoplasmic enzymes from red cells fractionated into age groups by centrifugation in Ficoll-Triosil gradients. Comparison of normal humans with with Duchenne muscular dystrophy. Biochem J. 191:63-70.
    • (1980) Biochem J. , vol.191 , pp. 63-70
    • Galbraith, D.A.1    Watts, D.C.2
  • 13
    • 0024989557 scopus 로고
    • Oxidation-induced changes in microrheological properties of the red blood cell membrane
    • Hebbel R.P., Leung A., and Mohandas N. (1990) Oxidation-induced changes in microrheological properties of the red blood cell membrane. Blood 76:1015-1020.
    • (1990) Blood , vol.76 , pp. 1015-1020
    • Hebbel, R.P.1    Leung, A.2    Mohandas, N.3
  • 14
    • 0011928018 scopus 로고
    • Metabolic processes involved in the formation and reduction of methemoglobin in erythrocytes
    • C. Bishop and D.M. Surgenor, eds. New York: Academic Press
    • Jaffe E.R. (1964). Metabolic processes involved in the formation and reduction of methemoglobin in erythrocytes. In: The Red Blood Cell - A Comprehensive Treatise. C. Bishop and D.M. Surgenor, eds. New York: Academic Press; pp. 397-422.
    • (1964) The Red Blood Cell - A Comprehensive Treatise , pp. 397-422
    • Jaffe, E.R.1
  • 15
    • 0023853772 scopus 로고
    • Evidence for membrane lipid peroxidation during the in vivo aging of human erythrocytes
    • Jain S.K. (1988). Evidence for membrane lipid peroxidation during the in vivo aging of human erythrocytes. Biochim. Biophys. Acta 937:205-210.
    • (1988) Biochim. Biophys. Acta , vol.937 , pp. 205-210
    • Jain, S.K.1
  • 16
    • 0003023897 scopus 로고
    • The role of oxygen concentration in oxidative stress: Hypoxic and hyperoxic models
    • H. Sies, ed. London: Academic Press
    • Jones D.P. (1985). The role of oxygen concentration in oxidative stress: hypoxic and hyperoxic models. In: Oxidative Stress. H. Sies, ed. London: Academic Press; pp. 151-195.
    • (1985) Oxidative Stress , pp. 151-195
    • Jones, D.P.1
  • 17
    • 0028264418 scopus 로고
    • Measuring relative rates of hemoglobin oxidation and denaturation
    • MacDonald V.W. (1994). Measuring relative rates of hemoglobin oxidation and denaturation. Methods Enzymol. 231:480-490.
    • (1994) Methods Enzymol. , vol.231 , pp. 480-490
    • MacDonald, V.W.1
  • 18
    • 0025082043 scopus 로고
    • Free-radical initiators as source of water- or lipid-soluble peroxyl radicals
    • Niki E. (1990). Free-radical initiators as source of water- or lipid-soluble peroxyl radicals. Methods Enzymol. 186:100-108.
    • (1990) Methods Enzymol. , vol.186 , pp. 100-108
    • Niki, E.1
  • 19
    • 0024203361 scopus 로고
    • Oxidative hemolysis of erythrocytes and its inhibition by free radical scavengers
    • Niki E., Komuro E., Takahashi M., Urano S., Ito E., and Terao K. (1988). Oxidative hemolysis of erythrocytes and its inhibition by free radical scavengers. J. Biol. Chem. 263:19809-19814.
    • (1988) J. Biol. Chem. , vol.263 , pp. 19809-19814
    • Niki, E.1    Komuro, E.2    Takahashi, M.3    Urano, S.4    Ito, E.5    Terao, K.6
  • 20
    • 0025295884 scopus 로고
    • Phase fluctuation in phospholipid membranes revealed by Laurdan fluorescence
    • Parasassi T., De Stasio G., d'Ubaldo A., and Gratton E. (1990). Phase fluctuation in phospholipid membranes revealed by Laurdan fluorescence. Biophys. J. 57:1179-1186.
    • (1990) Biophys. J. , vol.57 , pp. 1179-1186
    • Parasassi, T.1    De Stasio, G.2    d'Ubaldo, A.3    Gratton, E.4
  • 21
    • 0025742883 scopus 로고
    • Quantitation of lipid phases in phospholipid vesicles by the generalized polarization of Laurdan fluorescence
    • Parasassi T., De Stasio G., Ravagnan G., Rusch R.M., and Gratton E. (1991). Quantitation of lipid phases in phospholipid vesicles by the generalized polarization of Laurdan fluorescence. Biophys. J. 60:179-189.
    • (1991) Biophys. J. , vol.60 , pp. 179-189
    • Parasassi, T.1    De Stasio, G.2    Ravagnan, G.3    Rusch, R.M.4    Gratton, E.5
  • 22
    • 0028346769 scopus 로고
    • Evidence for an increase in water concentration in bilayers after oxidative damage of phospholipids induced by ionizing radiation
    • Parasassi T., Giusti A.M., Gratton E., Monaco E., Raimondi M., Ravagnan G., and Sapora O. (1994). Evidence for an increase in water concentration in bilayers after oxidative damage of phospholipids induced by ionizing radiation. Int. J. Radiat. Biol. 65:329-334.
    • (1994) Int. J. Radiat. Biol. , vol.65 , pp. 329-334
    • Parasassi, T.1    Giusti, A.M.2    Gratton, E.3    Monaco, E.4    Raimondi, M.5    Ravagnan, G.6    Sapora, O.7
  • 24
    • 0017613512 scopus 로고
    • A simplification of the protein assay method of Lowry et al. which is more generally applicable
    • Peterson G.L. (1977). A simplification of the protein assay method of Lowry et al. which is more generally applicable. Anal. Biochem. 83:346-356.
    • (1977) Anal. Biochem. , vol.83 , pp. 346-356
    • Peterson, G.L.1
  • 25
    • 84907037913 scopus 로고
    • The hypoxic stress on erythrocytes associated with superoxide formation
    • Rifkind J.M., Zhang L., Levy A., and Manoharan P.T. (1991). The hypoxic stress on erythrocytes associated with superoxide formation. Free Rad. Res. Comm. 12: 645-652.
    • (1991) Free Rad. Res. Comm. , vol.12 , pp. 645-652
    • Rifkind, J.M.1    Zhang, L.2    Levy, A.3    Manoharan, P.T.4
  • 26
    • 0029135068 scopus 로고
    • Effect of lipid ozonation products on liposomal membranes detected by Laurdan fluorescence
    • Salgo M.G., Cueto R., and Pryor W.A. (1995). Effect of lipid ozonation products on liposomal membranes detected by Laurdan fluorescence. Free Rad. Biol. Med. 19:609-616.
    • (1995) Free Rad. Biol. Med. , vol.19 , pp. 609-616
    • Salgo, M.G.1    Cueto, R.2    Pryor, W.A.3
  • 27
    • 0027373213 scopus 로고
    • Human red blood cell aging at 5050-m altitude: A role during adaptation to hypoxia
    • Samaja M., Brenna L., Allibardi S., and Cerretelli P. (1993). Human red blood cell aging at 5050-m altitude: a role during adaptation to hypoxia. J. Appl. Physiol. 75: 1696-1701.
    • (1993) J. Appl. Physiol. , vol.75 , pp. 1696-1701
    • Samaja, M.1    Brenna, L.2    Allibardi, S.3    Cerretelli, P.4
  • 28
    • 0026474211 scopus 로고
    • Peroxyl radical-mediated hemolysis: Role of lipid, protein and sulfhydryl oxidation
    • Sandhu I.S., Ware K., and Grisham M.B. (1992). Peroxyl radical-mediated hemolysis: role of lipid, protein and sulfhydryl oxidation. Free Rad. Res. Comm. 16:111-122.
    • (1992) Free Rad. Res. Comm. , vol.16 , pp. 111-122
    • Sandhu, I.S.1    Ware, K.2    Grisham, M.B.3
  • 30
    • 0022408547 scopus 로고
    • Effect of hydrogen peroxide exposure on normal human erythrocyte deformability, morphology, surface characteristics, and spectrin-hemoglobin cross-linking
    • Synder L.M., Fortier N.L., Trainor J., Jacobs J., Leb L., Lubin B., Chiu D., Shohet S., and Mohandas N. (1985). Effect of hydrogen peroxide exposure on normal human erythrocyte deformability, morphology, surface characteristics, and spectrin-hemoglobin cross-linking. J. Clin. Invest. 76:1971-1977.
    • (1985) J. Clin. Invest. , vol.76 , pp. 1971-1977
    • Synder, L.M.1    Fortier, N.L.2    Trainor, J.3    Jacobs, J.4    Leb, L.5    Lubin, B.6    Chiu, D.7    Shohet, S.8    Mohandas, N.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.