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Volumn 97, Issue 12, 2009, Pages 3206-3214

New insight into erythrocyte through in vivo surface-enhanced Raman spectroscopy

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EID: 73449087660     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2009.09.029     Document Type: Article
Times cited : (89)

References (44)
  • 1
    • 0021818674 scopus 로고
    • Structure, dynamics, and reactivity in hemoglobin
    • Friedman, J. M. 1985. Structure, dynamics, and reactivity in hemoglobin. Science. 228:1273-1280.
    • (1985) Science , vol.228 , pp. 1273-1280
    • Friedman, J.M.1
  • 2
    • 33847210722 scopus 로고    scopus 로고
    • Resonance Raman spectroscopy of red blood cells using near-infrared laser excitation
    • Wood, B. R., P. Caspers, G. J. Puppels, S. Pandiancherri, and D. McNaughton. 2007. Resonance Raman spectroscopy of red blood cells using near-infrared laser excitation. Anal. Bioanal. Chem. 387: 1691-1703.
    • (2007) Anal. Bioanal. Chem , vol.387 , pp. 1691-1703
    • Wood, B.R.1    Caspers, P.2    Puppels, G.J.3    Pandiancherri, S.4    McNaughton, D.5
  • 3
    • 57149132073 scopus 로고    scopus 로고
    • Ex vivo and in vivo imaging of myelin fibers in mouse brain by coherent anti-Stokes Raman scattering microscopy
    • Fu, Y., H. Wang, T. B. Huff, H.-W. Wang, J. X. Cheng, et al. 2008. Ex vivo and in vivo imaging of myelin fibers in mouse brain by coherent anti-Stokes Raman scattering microscopy. Opt. Express. 16:19396- 19409.
    • (2008) Opt. Express , vol.16 , pp. 19396-19409
    • Fu, Y.1    Wang, H.2    Huff, T.B.3    Wang, H.-W.4    Cheng, J.X.5
  • 4
    • 47549086779 scopus 로고
    • Raman spectra of pyridine adsorbed at a silver electrode
    • Fleishmann, M., P. J. Hendra, and A. J. McAuillan. 1974. Raman spectra of pyridine adsorbed at a silver electrode. Chem. Phys. Lett. 26:163-166.
    • (1974) Chem. Phys. Lett , vol.26 , pp. 163-166
    • Fleishmann, M.1    Hendra, P.J.2    McAuillan, A.J.3
  • 5
    • 0000698565 scopus 로고
    • Surface-enhanced spectroscopy
    • Moskovits, M. 1985. Surface-enhanced spectroscopy. Rev. Mod. Phys. 57:783-827.
    • (1985) Rev. Mod. Phys , vol.57 , pp. 783-827
    • Moskovits, M.1
  • 6
    • 0041306001 scopus 로고    scopus 로고
    • The structural basis for giant enhancement enabling single-molecule Raman scattering
    • Wang, Z., S. Pan, T. D. Krauss, H. Du, and L. J. Rothberg. 2003. The structural basis for giant enhancement enabling single-molecule Raman scattering. Proc. Natl. Acad. Sci. USA. 100:8638-8643.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 8638-8643
    • Wang, Z.1    Pan, S.2    Krauss, T.D.3    Du, H.4    Rothberg, L.J.5
  • 8
    • 34547366796 scopus 로고    scopus 로고
    • Distance dependence of surface plasmon-coupled emission observed using Langmuir-Blodgett films
    • Ray, K., H. Szmacinski, J. Enderlein, and J. R. Lakowicz. 2007. Distance dependence of surface plasmon-coupled emission observed using Langmuir-Blodgett films. Appl. Phys. Lett. 90:251116.
    • (2007) Appl. Phys. Lett , vol.90 , pp. 251116
    • Ray, K.1    Szmacinski, H.2    Enderlein, J.3    Lakowicz, J.R.4
  • 9
    • 52749088153 scopus 로고    scopus 로고
    • Plasmon-controlled fluorescence: A new paradigm in fluorescence spectroscopy
    • Lakowicz, J. R., K. Ray, M. Chowdhury, H. Szmacinski, Y. Fu, et al. 2008. Plasmon-controlled fluorescence: a new paradigm in fluorescence spectroscopy. Analyst (Lond.). 133:1308-1346.
    • (2008) Analyst (Lond.) , vol.133 , pp. 1308-1346
    • Lakowicz, J.R.1    Ray, K.2    Chowdhury, M.3    Szmacinski, H.4    Fu, Y.5
  • 10
    • 11144289677 scopus 로고    scopus 로고
    • Single-molecule detection of yeast cytochrome c by surface-enhanced Raman spectroscopy
    • Delfino, I., A. R. Bizzarri, and S. Cannistraro. 2005. Single-molecule detection of yeast cytochrome c by surface-enhanced Raman spectroscopy. Biophys. Chem. 113:41-51.
    • (2005) Biophys. Chem , vol.113 , pp. 41-51
    • Delfino, I.1    Bizzarri, A.R.2    Cannistraro, S.3
  • 11
    • 33751235879 scopus 로고    scopus 로고
    • Two-photon vibrational spectroscopy for biosciences based on surface-enhanced hyper-Raman scattering
    • Kneipp, J., H. Kneipp, and K. Kneipp. 2006. Two-photon vibrational spectroscopy for biosciences based on surface-enhanced hyper-Raman scattering. Proc. Natl. Acad. Sci. USA. 103:17149-17153.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 17149-17153
    • Kneipp, J.1    Kneipp, H.2    Kneipp, K.3
  • 12
    • 34547676383 scopus 로고    scopus 로고
    • Resonance surface enhanced Raman optical activity of myoglobin as a result of optimized resonance surface enhanced Raman scattering conditions
    • Abdali, S., C. Johannessen, J. Nygaard, and T. Norbygaard. 2007. Resonance surface enhanced Raman optical activity of myoglobin as a result of optimized resonance surface enhanced Raman scattering conditions. J. Phys. Condens. Matter. 103:285205-1-285205-8.
    • (2007) J. Phys. Condens. Matter , vol.103
    • Abdali, S.1    Johannessen, C.2    Nygaard, J.3    Norbygaard, T.4
  • 13
    • 65249131715 scopus 로고    scopus 로고
    • Nuclear targeted nanoprobe for single living cell detection by surface-enhanced Raman scattering
    • Xie, W., L. Wang, Y. Zhang, L. Su, A. Shen, et al. 2009. Nuclear targeted nanoprobe for single living cell detection by surface-enhanced Raman scattering. Bioconjug. Chem. 20:768-773.
    • (2009) Bioconjug. Chem , vol.20 , pp. 768-773
    • Xie, W.1    Wang, L.2    Zhang, Y.3    Su, L.4    Shen, A.5
  • 15
    • 0017588035 scopus 로고
    • Interaction of hemoglobin with red blood cell membranes as shown by a fluorescent chromophore
    • Shaklai, N., J. Yguerabide, and H. M. Ranney. 1977. Interaction of hemoglobin with red blood cell membranes as shown by a fluorescent chromophore. Biochemistry. 16:5585-5592.
    • (1977) Biochemistry , vol.16 , pp. 5585-5592
    • Shaklai, N.1    Yguerabide, J.2    Ranney, H.M.3
  • 16
    • 0021260876 scopus 로고
    • The interaction of hemoglobin with the cytoplasmic domain of band 3 of the human erythrocyte membrane
    • Walder, J.A.,R.Chatterjee, T. L. Steck, P.S. Low,G. F.Musso, et al. 1984. The interaction of hemoglobin with the cytoplasmic domain of band 3 of the human erythrocyte membrane. J. Biol. Chem. 259:10238-10246.
    • (1984) J. Biol. Chem , vol.259 , pp. 10238-10246
    • Walder, J.A.1    Chatterjee, R.2    Steck, T.L.3    Low, P.S.4    Musso, G.F.5
  • 17
    • 33746371697 scopus 로고    scopus 로고
    • Human and mouse hemoglobin association with the transgenic mouse erythrocyte membrane
    • Chen, Q., T. C. Balazs, R. L. Nagel, and R. E. Hirsch. 2006. Human and mouse hemoglobin association with the transgenic mouse erythrocyte membrane. FEBS Lett. 580:4485-4490.
    • (2006) FEBS Lett , vol.580 , pp. 4485-4490
    • Chen, Q.1    Balazs, T.C.2    Nagel, R.L.3    Hirsch, R.E.4
  • 18
    • 0017608285 scopus 로고
    • Classification and localization of hemoglobin binding sites on the red blood cell membrane
    • Shaklai, N., J. Yguerabide, and H. M. Ranney. 1977. Classification and localization of hemoglobin binding sites on the red blood cell membrane. Biochemistry. 16:5593-5597.
    • (1977) Biochemistry , vol.16 , pp. 5593-5597
    • Shaklai, N.1    Yguerabide, J.2    Ranney, H.M.3
  • 19
    • 0018256711 scopus 로고
    • Interaction of hemoglobin with membrane lipids: A source of pathological phenomena
    • Shaklai, N., and H. R. Ranney. 1978. Interaction of hemoglobin with membrane lipids: a source of pathological phenomena. Isr. J. Med. Sci. 14:1152-1156.
    • (1978) Isr. J. Med. Sci , vol.14 , pp. 1152-1156
    • Shaklai, N.1    Ranney, H.R.2
  • 20
    • 0019344450 scopus 로고
    • Interactions of hemoglobin S with the red cell membrane
    • Shaklai, N., H. M. Ranney, and V. Sharma. 1981. Interactions of hemoglobin S with the red cell membrane. Prog. Clin. Biol. Res. 51:1-16.
    • (1981) Prog. Clin. Biol. Res , vol.51 , pp. 1-16
    • Shaklai, N.1    Ranney, H.M.2    Sharma, V.3
  • 21
    • 0022344550 scopus 로고
    • Visualization of the protein associations in the erythrocyte membrane skeleton
    • Byers, T. J., and D. Branton. 1985. Visualization of the protein associations in the erythrocyte membrane skeleton. Proc. Natl. Acad. Sci. USA. 82:6153-6157.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 6153-6157
    • Byers, T.J.1    Branton, D.2
  • 22
    • 0025284142 scopus 로고
    • On the structure of erythrocyte spectrin in partially expanded membrane skeletons
    • McGough, A. M., and R. Josephs. 1990. On the structure of erythrocyte spectrin in partially expanded membrane skeletons. Proc. Natl. Acad. Sci. USA. 87:5208-5212.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 5208-5212
    • McGough, A.M.1    Josephs, R.2
  • 23
    • 2142845951 scopus 로고    scopus 로고
    • Sample preparation and imaging of erythrocyte cytoskeleton with the atomic force microscopy
    • Liu, F., J. Burgess, H. Mizukami, and A. Ostafin. 2003. Sample preparation and imaging of erythrocyte cytoskeleton with the atomic force microscopy. Cell Biochem. Biophys. 38:251-270.
    • (2003) Cell Biochem. Biophys , vol.38 , pp. 251-270
    • Liu, F.1    Burgess, J.2    Mizukami, H.3    Ostafin, A.4
  • 24
    • 0009470593 scopus 로고
    • Purification of two spectrin-binding proteins: Biochemical and electron microscopic evidence for site-specific reassociation between spectrin and bands 2.1 and 4.1
    • Tyler, J. M., W. R. Hargreaves, and D. Branton. 1979. Purification of two spectrin-binding proteins: biochemical and electron microscopic evidence for site-specific reassociation between spectrin and bands 2.1 and 4.1. Proc. Natl. Acad. Sci. USA. 76:5192-5196.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 5192-5196
    • Tyler, J.M.1    Hargreaves, W.R.2    Branton, D.3
  • 25
    • 0034329189 scopus 로고    scopus 로고
    • Crystallographic structure and functional interpretation of the cytoplasmic domain of erythrocyte membrane band 3
    • Zhang, D., A. Kiyatkin, J. T. Bolin, and P. S. Low. 2000. Crystallographic structure and functional interpretation of the cytoplasmic domain of erythrocyte membrane band 3. Blood. 96:2925-2933.
    • (2000) Blood , vol.96 , pp. 2925-2933
    • Zhang, D.1    Kiyatkin, A.2    Bolin, J.T.3    Low, P.S.4
  • 26
    • 0021003005 scopus 로고
    • Spectrophotometry of hemoglobin and hemoglobin derivatives
    • van Kampen, E. J., and W. G. Zijlstra. 1983. Spectrophotometry of hemoglobin and hemoglobin derivatives. Adv. Clin. Chem. 23:199-257.
    • (1983) Adv. Clin. Chem , vol.23 , pp. 199-257
    • van Kampen, E.J.1    Zijlstra, W.G.2
  • 27
    • 0141891239 scopus 로고    scopus 로고
    • Human erythrocyte membrane band 3 protein influences hemoglobin cooperativity. Possible effect on oxygen transport
    • Zhang, Y., L. R. Manning, J. Falcones, O. Platt, and V. Manning. 2003. Human erythrocyte membrane band 3 protein influences hemoglobin cooperativity. Possible effect on oxygen transport. J. Biol. Chem. 278:39565-39571.
    • (2003) J. Biol. Chem , vol.278 , pp. 39565-39571
    • Zhang, Y.1    Manning, L.R.2    Falcones, J.3    Platt, O.4    Manning, V.5
  • 28
    • 56849093676 scopus 로고    scopus 로고
    • The measurement of dyshemoglobins and total hemoglobin by pulse oximetry
    • Barker, S. J., and J. J. Badal. 2008. The measurement of dyshemoglobins and total hemoglobin by pulse oximetry. Curr. Opin. Anaesthesiol. 21:805-810.
    • (2008) Curr. Opin. Anaesthesiol , vol.21 , pp. 805-810
    • Barker, S.J.1    Badal, J.J.2
  • 29
    • 0038238001 scopus 로고    scopus 로고
    • A new method for fast preparation of highly surface-enhanced Raman scattering (SERS) active silver colloids at room temperature by reduction of silver nitrate with hydroxylamine hydrochloride
    • Leopold, N., and B. Lendl. 2003. A new method for fast preparation of highly surface-enhanced Raman scattering (SERS) active silver colloids at room temperature by reduction of silver nitrate with hydroxylamine hydrochloride. J. Phys. Chem. B. 107:5723-5727.
    • (2003) J. Phys. Chem. B , vol.107 , pp. 5723-5727
    • Leopold, N.1    Lendl, B.2
  • 30
    • 0032557188 scopus 로고    scopus 로고
    • Characterization of the pH dependence of hemoglobin binding to band 3. Evidence for a pH-dependent conformational changes within the hemoglobin-band 3 complex
    • Salhany, J. M., K. A. Cordes, and R. L. Sloan. 2007. Characterization of the pH dependence of hemoglobin binding to band 3. Evidence for a pH-dependent conformational changes within the hemoglobin-band 3 complex. Biochim. Biophys. Acta. 1371:107-113.
    • (2007) Biochim. Biophys. Acta , vol.1371 , pp. 107-113
    • Salhany, J.M.1    Cordes, K.A.2    Sloan, R.L.3
  • 31
    • 0017253370 scopus 로고
    • Monitoring the permeability profile of lipid membranes with spin probes
    • Schreier-Muccillo, S., and O. Marsh. 1976. Monitoring the permeability profile of lipid membranes with spin probes. Arch. Biochem. Biophys. 172:1-11.
    • (1976) Arch. Biochem. Biophys , vol.172 , pp. 1-11
    • Schreier-Muccillo, S.1    Marsh, O.2
  • 32
    • 34247379102 scopus 로고    scopus 로고
    • Ion transport, membrane fluidity and hemoglobin conformation in erythrocyte from patients with cardiovascular diseases: Role of augmented plasma cholesterol
    • Luneva, O. G., N. A. Brazhe, N. V. Maksimova, O. V. Rodnenkov, E. Y. Parshina, et al. 2007. Ion transport, membrane fluidity and hemoglobin conformation in erythrocyte from patients with cardiovascular diseases: role of augmented plasma cholesterol. Pathophysiology. 14:41-46.
    • (2007) Pathophysiology , vol.14 , pp. 41-46
    • Luneva, O.G.1    Brazhe, N.A.2    Maksimova, N.V.3    Rodnenkov, O.V.4    Parshina, E.Y.5
  • 33
    • 0033044499 scopus 로고    scopus 로고
    • Resolution of the paradox of red cell shape changes in low and high pH
    • Gedde, M. M., E. Yang, and W. H. Huestis. 1999. Resolution of the paradox of red cell shape changes in low and high pH. Biochim. Biophys. Acta. 1417:246-253.
    • (1999) Biochim. Biophys. Acta , vol.1417 , pp. 246-253
    • Gedde, M.M.1    Yang, E.2    Huestis, W.H.3
  • 34
    • 0037168535 scopus 로고    scopus 로고
    • Stomatocyte-discocyte-echinocyte sequence of the human red blood cell: Evidence for the bilayer-couple hypothesis from membrane mechanics
    • Gerald, L. H. W., M. Wortis, and R. Mukhopadhyay. 2002. Stomatocyte-discocyte-echinocyte sequence of the human red blood cell: evidence for the bilayer-couple hypothesis from membrane mechanics. Proc. Natl. Acad. Sci. USA. 99:16766-16769.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 16766-16769
    • Gerald, L.H.W.1    Wortis, M.2    Mukhopadhyay, R.3
  • 35
    • 85031333792 scopus 로고    scopus 로고
    • Deuticke, B. 2003. Membrane lipids and proteins as a basis of red cell shape and its alterations. In Red Cell Membrane Transport in Health and Disease. I. Bernhardt and C. Ellory, editors. Springer, Heidelberg. 36. Owen, J. S., D. J. Brown, D. S. Harry, N. McIntyre, G. H. Beaven, et al. 1985. Erythrocyte echinocytosis in liver disease. Role of abnormal plasma high density lipoproteins. J. Clin. Invest. 76:2275-2285.
    • Deuticke, B. 2003. Membrane lipids and proteins as a basis of red cell shape and its alterations. In Red Cell Membrane Transport in Health and Disease. I. Bernhardt and C. Ellory, editors. Springer, Heidelberg. 36. Owen, J. S., D. J. Brown, D. S. Harry, N. McIntyre, G. H. Beaven, et al. 1985. Erythrocyte echinocytosis in liver disease. Role of abnormal plasma high density lipoproteins. J. Clin. Invest. 76:2275-2285.
  • 37
    • 0016854458 scopus 로고
    • Structural interpretation of heme protein resonance Raman frequencies. Preliminary normal coordinate analysis results
    • Stein, P., I. M. Burke, and T. G. Spiro. 1975. Structural interpretation of heme protein resonance Raman frequencies. Preliminary normal coordinate analysis results. J. Am. Chem. Soc. 97:2304-2305.
    • (1975) J. Am. Chem. Soc , vol.97 , pp. 2304-2305
    • Stein, P.1    Burke, I.M.2    Spiro, T.G.3
  • 38
    • 0017310256 scopus 로고
    • Nature of the iron ligand bond in ferrous low spin hemoproteins studied by resonance Raman scattering
    • Kitagawa, T., Y. Kyogoku, and T. Iizuka. 1976. Nature of the iron ligand bond in ferrous low spin hemoproteins studied by resonance Raman scattering. J. Am. Chem. Soc. 98:5169-5173.
    • (1976) J. Am. Chem. Soc , vol.98 , pp. 5169-5173
    • Kitagawa, T.1    Kyogoku, Y.2    Iizuka, T.3
  • 39
    • 2842546487 scopus 로고
    • Structural correlations and vinyl influences in resonance Raman spectra of protoheme complexes and proteins
    • Choi, S., T. G. Spiro, K. C. Langry, K. M. Smith, D. L. Budd, et al. 1982. Structural correlations and vinyl influences in resonance Raman spectra of protoheme complexes and proteins. J. Am. Chem. Soc. 104:4345-4351.
    • (1982) J. Am. Chem. Soc , vol.104 , pp. 4345-4351
    • Choi, S.1    Spiro, T.G.2    Langry, K.C.3    Smith, K.M.4    Budd, D.L.5
  • 40
    • 33845470757 scopus 로고
    • Surface selection rules for surfaceenhanced Raman spectroscopy: Calculations and application to the surface-enhanced Raman spectrum of phthalazine on silver
    • Moskovits, M., and J. S. Suh. 1984. Surface selection rules for surfaceenhanced Raman spectroscopy: calculations and application to the surface-enhanced Raman spectrum of phthalazine on silver. J. Chem. Phys. 88:5526-5530.
    • (1984) J. Chem. Phys , vol.88 , pp. 5526-5530
    • Moskovits, M.1    Suh, J.S.2
  • 41
    • 0037541502 scopus 로고    scopus 로고
    • The orientation of 2,2́-bipyridine adsorbed at a SERS-active Au111 electrode surface
    • Brolo, A. G., Z. Jiang, and D. E. Irish. 2003. The orientation of 2,2́-bipyridine adsorbed at a SERS-active Au111 electrode surface. J. Electroanal. Chem. 547:163-172.
    • (2003) J. Electroanal. Chem , vol.547 , pp. 163-172
    • Brolo, A.G.1    Jiang, Z.2    Irish, D.E.3
  • 42
    • 33749261592 scopus 로고    scopus 로고
    • Surface enhanced Raman optical activity of molecules on orientationally averaged substrates: Theory of electromagnetic effects
    • Janesko, B. G., and G. E. Scuseria. 2006. Surface enhanced Raman optical activity of molecules on orientationally averaged substrates: theory of electromagnetic effects. J. Chem. Phys. 125:124704.
    • (2006) J. Chem. Phys , vol.125 , pp. 124704
    • Janesko, B.G.1    Scuseria, G.E.2
  • 43
    • 49649123883 scopus 로고    scopus 로고
    • Measurement of hemoglobin oxygen saturation using Raman microspectroscopy and 532-nm excitation
    • Filho, I. P. T., J. Terner, R. N. Pittman, E. Proffitt, and K. R. Ward. 2008. Measurement of hemoglobin oxygen saturation using Raman microspectroscopy and 532-nm excitation. J. Appl. Physiol. 104:1809-1817.
    • (2008) J. Appl. Physiol , vol.104 , pp. 1809-1817
    • Filho, I.P.T.1    Terner, J.2    Pittman, R.N.3    Proffitt, E.4    Ward, K.R.5
  • 44
    • 0023099564 scopus 로고
    • The binding of hemoglobin to red cell membrane lowers its oxygen affinity
    • Tsuneshige, A., K. Imai, and I. Tyuma. 1987. The binding of hemoglobin to red cell membrane lowers its oxygen affinity. J. Biol. Chem. 101:695-704.
    • (1987) J. Biol. Chem , vol.101 , pp. 695-704
    • Tsuneshige, A.1    Imai, K.2    Tyuma, I.3


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