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Volumn 212, Issue 1, 2011, Pages 86-94

Spin-label saturation-recovery EPR at W-band: Applications to eye lens lipid membranes

Author keywords

Cholesterol; Cholesterol bilayer domain; EPR; Eye lens; Spin label; W band

Indexed keywords

CHOLESTEROL; LIPIDS; MEMBRANES; MICROCOMPUTERS; OXYGEN; PARAMAGNETIC RESONANCE;

EID: 84855404181     PISSN: 10907807     EISSN: 10960856     Source Type: Journal    
DOI: 10.1016/j.jmr.2011.06.014     Document Type: Article
Times cited : (20)

References (42)
  • 1
    • 0039441201 scopus 로고    scopus 로고
    • Saturation recovery
    • G.R. Eaton, S.S. Eaton, K.M. Salikhov (Eds.), World Scientific, Singapore
    • J.S. Hyde, Saturation recovery, in: G.R. Eaton, S.S. Eaton, K.M. Salikhov (Eds.), Foundations of Modern EPR, World Scientific, Singapore, 1998, pp. 607-618.
    • (1998) Foundations of Modern EPR , pp. 607-618
    • Hyde, J.S.1
  • 2
    • 0029761813 scopus 로고    scopus 로고
    • Effects of lutein and cholesterol on alkyl chain bending in lipid bilayers: A pulse electron spin resonance spin labeling study
    • J.J. Yin, W.K. Subczynski, Effects of lutein and cholesterol on alkyl chain bending in lipid bilayers: a pulse electron spin resonance spin labeling study, Biophys. J. 71 (1996) 832-839.
    • (1996) Biophys. J. , vol.71 , pp. 832-839
    • Yin, J.J.1    Subczynski, W.K.2
  • 6
    • 34249028659 scopus 로고    scopus 로고
    • Physical properties of the lipid bilayer membrane made of calf lens lipids: EPR spin labeling studies
    • J. Widomska, M. Raguz, J. Dillon, E.R. Gaillard, W.K. Subczynski, Physical properties of the lipid bilayer membrane made of calf lens lipids: EPR spin labeling studies, Biochim. Biophys. Acta 1768 (2007) 1454-1465.
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 1454-1465
    • Widomska, J.1    Raguz, M.2    Dillon, J.3    Gaillard, E.R.4    Subczynski, W.K.5
  • 7
    • 34948859469 scopus 로고    scopus 로고
    • Oxygen permeability of the lipid bilayer membrane made of calf lens lipids
    • J. Widomska, M. Raguz, W.K. Subczynski, Oxygen permeability of the lipid bilayer membrane made of calf lens lipids, Biochim. Biophys. Acta 1768 (2007) 2636-2645.
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 2636-2645
    • Widomska, J.1    Raguz, M.2    Subczynski, W.K.3
  • 8
    • 40949085124 scopus 로고    scopus 로고
    • Characterization of lipid domains in reconstituted porcine lens membranes using EPR spin-labeling approaches
    • M. Raguz, J. Widomska, J. Dillon, E.R. Gaillard, W.K. Subczynski, Characterization of lipid domains in reconstituted porcine lens membranes using EPR spin-labeling approaches, Biochim. Biophys. Acta 1778 (2008) 1079- 1090.
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 1079-1090
    • Raguz, M.1    Widomska, J.2    Dillon, J.3    Gaillard, E.R.4    Subczynski, W.K.5
  • 9
    • 71149093497 scopus 로고    scopus 로고
    • Physical properties of the lipid bilayer membrane made of cortical and nuclear bovine lens lipids: EPR spin-labeling studies
    • M. Raguz, J. Widomska, J. Dillon, E.R. Gaillard, W.K. Subczynski, Physical properties of the lipid bilayer membrane made of cortical and nuclear bovine lens lipids: EPR spin-labeling studies, Biochim. Biophys. Acta 1788 (2009) 2380-2388.
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 2380-2388
    • Raguz, M.1    Widomska, J.2    Dillon, J.3    Gaillard, E.R.4    Subczynski, W.K.5
  • 10
    • 38949101213 scopus 로고    scopus 로고
    • Saturation-recovery electron paramagnetic resonance discrimination by oxygen transport (DOT) method for characterizing membrane domains
    • W.K. Subczynski, J. Widomska, A. Wisniewska, A. Kusumi, Saturation-recovery electron paramagnetic resonance discrimination by oxygen transport (DOT) method for characterizing membrane domains, Methods Mol. Biol. 398 (2007) 143-157.
    • (2007) Methods Mol. Biol. , vol.398 , pp. 143-157
    • Subczynski, W.K.1    Widomska, J.2    Wisniewska, A.3    Kusumi, A.4
  • 11
    • 77649228493 scopus 로고    scopus 로고
    • Studying lipid organization in biological membranes using liposomes and EPR spin labeling
    • W.K. Subczynski, M. Raguz, J. Widomska, Studying lipid organization in biological membranes using liposomes and EPR spin labeling, Methods Mol. Biol. 606 (2010) 247-269.
    • (2010) Methods Mol. Biol. , vol.606 , pp. 247-269
    • Subczynski, W.K.1    Raguz, M.2    Widomska, J.3
  • 12
    • 0019400060 scopus 로고
    • Electron spin resonance: Spin labels
    • E. Grell (Ed.), Springer-Verlag, Berlin
    • D. Marsh, Electron spin resonance: spin labels, in: E. Grell (Ed.), Membrane Spectroscopy, Springer-Verlag, Berlin, 1981, pp. 51-142.
    • (1981) Membrane Spectroscopy , pp. 51-142
    • Marsh, D.1
  • 13
    • 0028341889 scopus 로고
    • Hydrophobic barriers of lipid bilayer membranes formed by reduction of water penetration by alkyl chain unsaturation and cholesterol
    • W.K. Subczynski, A. Wisniewska, J.J. Yin, J.S. Hyde, A. Kusumi, Hydrophobic barriers of lipid bilayer membranes formed by reduction of water penetration by alkyl chain unsaturation and cholesterol, Biochemistry 33 (1994) 7670-7681.
    • (1994) Biochemistry , vol.33 , pp. 7670-7681
    • Subczynski, W.K.1    Wisniewska, A.2    Yin, J.J.3    Hyde, J.S.4    Kusumi, A.5
  • 14
    • 0037617781 scopus 로고
    • Oxygen transport parameter in membranes as deduced by saturation recovery measurements of spin-lattice relaxation times of spin labels
    • A. Kusumi, W.K. Subczynski, J.S. Hyde, Oxygen transport parameter in membranes as deduced by saturation recovery measurements of spin-lattice relaxation times of spin labels, Proc. Natl. Acad. Sci. U. S. A. 79 (1982) 1854- 1858.
    • (1982) Proc. Natl. Acad. Sci. U. S. A. , vol.79 , pp. 1854-1858
    • Kusumi, A.1    Subczynski, W.K.2    Hyde, J.S.3
  • 15
    • 79751538528 scopus 로고    scopus 로고
    • The immiscible cholesterol bilayer domain exists as an integral part of phospholipid bilayer membranes
    • M. Raguz, L. Mainali, J. Widomska, W.K. Subczynski, The immiscible cholesterol bilayer domain exists as an integral part of phospholipid bilayer membranes, Biochim. Biophys. Acta 1808 (2011) 1072-1080.
    • (2011) Biochim. Biophys. Acta , vol.1808 , pp. 1072-1080
    • Raguz, M.1    Mainali, L.2    Widomska, J.3    Subczynski, W.K.4
  • 16
    • 0025731907 scopus 로고
    • The effect of protons or calcium ions on the phase behavior of phosphatidylserine-cholesterol mixtures
    • E.J. Wachtel, N. Borochov, D. Bach, The effect of protons or calcium ions on the phase behavior of phosphatidylserine-cholesterol mixtures, Biochim. Biophys. Acta 1066 (1991) 63-69.
    • (1991) Biochim. Biophys. Acta , vol.1066 , pp. 63-69
    • Wachtel, E.J.1    Borochov, N.2    Bach, D.3
  • 17
    • 0029053291 scopus 로고
    • Phase behavior of mixtures of cholesterol and saturated phosphatidylglycerols
    • N. Borochov, E.J. Wachtel, D. Bach, Phase behavior of mixtures of cholesterol and saturated phosphatidylglycerols, Chem. Phys. Lipids 76 (1995) 85-92.
    • (1995) Chem. Phys. Lipids , vol.76 , pp. 85-92
    • Borochov, N.1    Wachtel, E.J.2    Bach, D.3
  • 18
    • 0038637713 scopus 로고    scopus 로고
    • Cholesterol in bilayers of sphingomyelin or dihydrosphingomyelin at concentrations found in ocular lens membranes
    • R.M. Epand, Cholesterol in bilayers of sphingomyelin or dihydrosphingomyelin at concentrations found in ocular lens membranes, Biophys. J. 84 (2003) 3102- 3110.
    • (2003) Biophys. J. , vol.84 , pp. 3102-3110
    • Epand, R.M.1
  • 19
    • 0347572922 scopus 로고    scopus 로고
    • Direct evidence for cholesterol crystalline domains in biological membranes: Role in human pathobiology
    • R.P. Mason, T.N. Tulenko, R.F. Jacob, Direct evidence for cholesterol crystalline domains in biological membranes: role in human pathobiology, Biochim. Biophys. Acta 1610 (2003) 198-207.
    • (2003) Biochim. Biophys. Acta , vol.1610 , pp. 198-207
    • Mason, R.P.1    Tulenko, T.N.2    Jacob, R.F.3
  • 20
    • 0024452439 scopus 로고
    • Role of the stereochemistry of the hydroxyl group of cholesterol and the formation of nonbilayer structures in phosphatidylethanolamines
    • J.J. Cheetham, E. Wachtel, D. Bach, R.M. Epand, Role of the stereochemistry of the hydroxyl group of cholesterol and the formation of nonbilayer structures in phosphatidylethanolamines, Biochemistry 28 (1989) 8928-8934.
    • (1989) Biochemistry , vol.28 , pp. 8928-8934
    • Cheetham, J.J.1    Wachtel, E.2    Bach, D.3    Epand, R.M.4
  • 21
    • 0022422934 scopus 로고
    • Small-angle neutron scattering study of lateral phase separation in dimyristoylphosphatidylcholine- cholesterol mixed membranes
    • W. Knoll, G. Schmidt, K. Ibel, E. Sackmann, Small-angle neutron scattering study of lateral phase separation in dimyristoylphosphatidylcholine- cholesterol mixed membranes, Biochemistry 24 (1985) 5240-5246.
    • (1985) Biochemistry , vol.24 , pp. 5240-5246
    • Knoll, W.1    Schmidt, G.2    Ibel, K.3    Sackmann, E.4
  • 22
    • 0019975413 scopus 로고
    • Lens plasma membrane: Isolation and biochemical characterization
    • D. Roy, L. Rosenfeld, A. Spector, Lens plasma membrane: isolation and biochemical characterization, Exp. Eye Res. 35 (1982) 113-129.
    • (1982) Exp. Eye Res. , vol.35 , pp. 113-129
    • Roy, D.1    Rosenfeld, L.2    Spector, A.3
  • 23
    • 70449158340 scopus 로고
    • Stanley a simple method for the isolation and purification of total lipids from animal tissues
    • J. Folch, M. Lees, G.H. Sloane Stanley, A simple method for the isolation and purification of total lipids from animal tissues, J. Biol. Chem. 226 (1957) 497- 509.
    • (1957) J. Biol. Chem. , vol.226 , pp. 497-509
    • Folch, J.1    Lees, M.2    Sloane, G.H.3
  • 24
    • 0001300193 scopus 로고
    • Spin-label oximetry
    • L.J. Berliner, J. Reuben (Eds.), Plenum Press, New York
    • J.S. Hyde, W.K. Subczynski, Spin-label oximetry, in: L.J. Berliner, J. Reuben (Eds.), Spin Labeling: Theory and Applications, vol. 8, Plenum Press, New York, 1989, pp. 399-425.
    • (1989) Spin Labeling: Theory and Applications , vol.8 , pp. 399-425
    • Hyde, J.S.1    Subczynski, W.K.2
  • 25
    • 25144497630 scopus 로고    scopus 로고
    • Concentration by centrifugation for gas exchange EPR oximetry measurements with loop-gap resonators
    • W.K. Subczynski, C.C. Felix, C.S. Klug, J.S. Hyde, Concentration by centrifugation for gas exchange EPR oximetry measurements with loop-gap resonators, J. Magn. Reson. 176 (2005) 244-248.
    • (2005) J. Magn. Reson. , vol.176 , pp. 244-248
    • Subczynski, W.K.1    Felix, C.C.2    Klug, C.S.3    Hyde, J.S.4
  • 27
    • 0014969210 scopus 로고
    • Kinetic class analysis of hydrogen-exchange data
    • S.L. Laiken, M.P. Printz, Kinetic class analysis of hydrogen-exchange data, Biochemistry 9 (1970) 1547-1553.
    • (1970) Biochemistry , vol.9 , pp. 1547-1553
    • Laiken, S.L.1    Printz, M.P.2
  • 28
  • 29
    • 0014331504 scopus 로고
    • Spin-label studies of the excitable membranes of nerve and muscle
    • W.L. Hubbell, H.M. McConnell, Spin-label studies of the excitable membranes of nerve and muscle, Proc. Natl. Acad. Sci. U. S. A. 61 (1968) 12-16.
    • (1968) Proc. Natl. Acad. Sci. U. S. A. , vol.61 , pp. 12-16
    • Hubbell, W.L.1    McConnell, H.M.2
  • 31
    • 33645868674 scopus 로고    scopus 로고
    • High-field ESR on aligned membranes: A simple method to record spectra from different membrane orientations in the magnetic field
    • B. Dzikovski, K. Earle, S. Pachtchenko, J. Freed, High-field ESR on aligned membranes: a simple method to record spectra from different membrane orientations in the magnetic field, J. Magn. Reson. 179 (2006) 273-279.
    • (2006) J. Magn. Reson. , vol.179 , pp. 273-279
    • Dzikovski, B.1    Earle, K.2    Pachtchenko, S.3    Freed, J.4
  • 32
    • 0035892170 scopus 로고    scopus 로고
    • A multifrequency ESR study of the complex dynamics of membranes
    • Y. Lou, M. Ge, J.H. Freed, A multifrequency ESR study of the complex dynamics of membranes, J. Phys. Chem. B 105 (2001) 11053-11056.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 11053-11056
    • Lou, Y.1    Ge, M.2    Freed, J.H.3
  • 33
    • 68349130628 scopus 로고    scopus 로고
    • Multifrequency ESR study of spin-labeled molecules in inclusion compounds with cyclodextrins
    • B. Dzikovski, D. Tipikin, V. Livshits, K. Earle, J. Freed, Multifrequency ESR study of spin-labeled molecules in inclusion compounds with cyclodextrins, Phys. Chem. Chem. Phys. 11 (2009) 6676-6688.
    • (2009) Phys. Chem. Chem. Phys. , vol.11 , pp. 6676-6688
    • Dzikovski, B.1    Tipikin, D.2    Livshits, V.3    Earle, K.4    Freed, J.5
  • 34
    • 0021798840 scopus 로고
    • Membrane cholesterol and phospholipid in consecutive concentric sections of human lenses
    • L.K. Li, L. So, A. Spector, Membrane cholesterol and phospholipid in consecutive concentric sections of human lenses, J. Lipid Res. 26 (1985) 600-609.
    • (1985) J. Lipid Res. , vol.26 , pp. 600-609
    • Li, L.K.1    So, L.2    Spector, A.3
  • 35
    • 0023070521 scopus 로고
    • Age-dependent changes in the distribution and concentration of human lens cholesterol and phospholipids
    • L.K. Li, L. So, A. Spector, Age-dependent changes in the distribution and concentration of human lens cholesterol and phospholipids, Biochim. Biophys. Acta 917 (1987) 112-120.
    • (1987) Biochim. Biophys. Acta , vol.917 , pp. 112-120
    • Li, L.K.1    So, L.2    Spector, A.3
  • 37
    • 0023111375 scopus 로고
    • Age dependent lipid and protein changes in individual bovine lenses
    • L.K. Li, L. So, Age dependent lipid and protein changes in individual bovine lenses, Curr. Eye Res. 6 (1987) 599-605.
    • (1987) Curr. Eye Res. , vol.6 , pp. 599-605
    • Li, L.K.1    So, L.2
  • 38
    • 0345697981 scopus 로고
    • ESR linewidth in solution. II. Analysis of spinrotational relaxation data
    • P.W. Atkins, D. Kivelson, ESR linewidth in solution. II. Analysis of spinrotational relaxation data, J. Chem. Phys. 44 (1966) 169-174.
    • (1966) J. Chem. Phys. , vol.44 , pp. 169-174
    • Atkins, P.W.1    Kivelson, D.2
  • 39
    • 19944417905 scopus 로고    scopus 로고
    • Explanation of spin-lattice relaxation rates of spin labels obtained with multifrequency saturation recovery EPR
    • C. Mailer, R.D. Nielsen, B.H. Robinson, Explanation of spin-lattice relaxation rates of spin labels obtained with multifrequency saturation recovery EPR, J. Phys. Chem. A 109 (2005) 4049-4061.
    • (2005) J. Phys. Chem. A , vol.109 , pp. 4049-4061
    • Mailer, C.1    Nielsen, R.D.2    Robinson, B.H.3
  • 40
    • 33847770910 scopus 로고    scopus 로고
    • Three-dimensional dynamic structure of the liquid-ordered domain in lipid membranes as examined by pulse-EPR oxygen probing
    • W.K. Subczynski, A. Wisniewska, J.S. Hyde, A. Kusumi, Three-dimensional dynamic structure of the liquid-ordered domain in lipid membranes as examined by pulse-EPR oxygen probing, Biophys. J. 92 (2007) 1573-1584.
    • (2007) Biophys. J. , vol.92 , pp. 1573-1584
    • Subczynski, W.K.1    Wisniewska, A.2    Hyde, J.S.3    Kusumi, A.4
  • 41
    • 0028343033 scopus 로고
    • Molecular organization and dynamics in bacteriorhodopsin-rich reconstituted membranes: Discrimination of lipid environments by the oxygen transport parameter using a pulse ESR spin-labeling technique
    • I. Ashikawa, J.J. Yin, W.K. Subczynski, T. Kouyama, J.S. Hyde, A. Kusumi, Molecular organization and dynamics in bacteriorhodopsin-rich reconstituted membranes: discrimination of lipid environments by the oxygen transport parameter using a pulse ESR spin-labeling technique, Biochemistry 33 (1994) 4947-4952.
    • (1994) Biochemistry , vol.33 , pp. 4947-4952
    • Ashikawa, I.1    Yin, J.J.2    Subczynski, W.K.3    Kouyama, T.4    Hyde, J.S.5    Kusumi, A.6
  • 42
    • 0035142949 scopus 로고    scopus 로고
    • Pulse EPR detection of lipid exchange between protein-rich raft and bulk domains in the membrane: Methodology development and its application to studies of influenza viral membrane
    • K. Kawasaki, J.J. Yin, W.K. Subczynski, J.S. Hyde, A. Kusumi, Pulse EPR detection of lipid exchange between protein-rich raft and bulk domains in the membrane: methodology development and its application to studies of influenza viral membrane, Biophys. J. 80 (2001) 738-748.
    • (2001) Biophys. J. , vol.80 , pp. 738-748
    • Kawasaki, K.1    Yin, J.J.2    Subczynski, W.K.3    Hyde, J.S.4    Kusumi, A.5


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