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Volumn 57, Issue , 2015, Pages 81-91

Microscopy of membrane lipids: How precisely can we define their distribution?

Author keywords

Aldehyde; Cryosection; Electron microscopy; Fixation; Freeze fracture replica; Lipid; Quick freezing; Resin section

Indexed keywords

ALDEHYDE; COLLOIDAL GOLD; EPOXY RESIN; MEMBRANE LIPID; MEMBRANE PROTEIN; ORGANOMETALLIC COMPOUND; URANYL ACETATE;

EID: 84922469431     PISSN: 00711365     EISSN: None     Source Type: Journal    
DOI: 10.1042/bse0570081     Document Type: Review
Times cited : (6)

References (33)
  • 1
    • 0015514472 scopus 로고
    • The fluid mosaic model of the structure of cell membranes
    • Singer, S.J. and Nicolson, G.L. (1972) The fluid mosaic model of the structure of cell membranes. Science 175, 720-731
    • (1972) Science , vol.175 , pp. 720-731
    • Singer, S.J.1    Nicolson, G.L.2
  • 2
    • 17844364513 scopus 로고    scopus 로고
    • Paradigm shift of the plasma membrane concept from the two-dimensional continuum fluid to the partitioned fluid: High-speed single-molecule tracking of membrane molecules
    • Kusumi, A., Nakada, C., Ritchie, K., Murase, K., Suzuki, K., Murakoshi, H., Kasai, R.S., Kondo, J. and Fujiwara, T. (2005) Paradigm shift of the plasma membrane concept from the two-dimensional continuum fluid to the partitioned fluid: high-speed single-molecule tracking of membrane molecules. Annu. Rev. Biophys. Biomol. Struct. 34, 351-378
    • (2005) Annu. Rev. Biophys. Biomol. Struct. , vol.34 , pp. 351-378
    • Kusumi, A.1    Nakada, C.2    Ritchie, K.3    Murase, K.4    Suzuki, K.5    Murakoshi, H.6    Kasai, R.S.7    Kondo, J.8    Fujiwara, T.9
  • 3
    • 84899444997 scopus 로고    scopus 로고
    • The fluid-mosaic model of membrane structure: Still relevant to understanding the structure, function and dynamics of biological membranes after more than 40 years
    • Nicolson, G.L. (2013) The fluid-mosaic model of membrane structure: still relevant to understanding the structure, function and dynamics of biological membranes after more than 40 years. Biochim. Biophys. Acta 1838, 1451-1466
    • (2013) Biochim. Biophys. Acta , vol.1838 , pp. 1451-1466
    • Nicolson, G.L.1
  • 4
    • 0023652259 scopus 로고
    • Parallax method for direct measurement of membrane penetration depth utilizing fluorescence quenching by spin-labeled phospholipids
    • Chattopadhyay, A. and London, E. (1987) Parallax method for direct measurement of membrane penetration depth utilizing fluorescence quenching by spin-labeled phospholipids. Biochemistry 26, 39-45
    • (1987) Biochemistry , vol.26 , pp. 39-45
    • Chattopadhyay, A.1    London, E.2
  • 5
    • 0032532696 scopus 로고    scopus 로고
    • Determination of the depth of BODIPY probes in model membranes by parallax analysis of fluorescence quenching
    • Kaiser, R.D. and London, E. (1998) Determination of the depth of BODIPY probes in model membranes by parallax analysis of fluorescence quenching. Biochim. Biophys. Acta 1375, 13-22
    • (1998) Biochim. Biophys. Acta , vol.1375 , pp. 13-22
    • Kaiser, R.D.1    London, E.2
  • 7
    • 56249127812 scopus 로고    scopus 로고
    • Live cell imaging of phosphoinositides with expressed inositide binding protein domains
    • Varnai, P. and Balla, T. (2008) Live cell imaging of phosphoinositides with expressed inositide binding protein domains. Methods 46, 167-176
    • (2008) Methods , vol.46 , pp. 167-176
    • Varnai, P.1    Balla, T.2
  • 9
    • 0032547744 scopus 로고    scopus 로고
    • 3H] inositol-labeled phosphoinositide pools
    • 3H] inositol-labeled phosphoinositide pools. J. Cell Biol. 143, 501-510
    • (1998) J. Cell Biol. , vol.143 , pp. 501-510
    • Varnai, P.1    Balla, T.2
  • 10
    • 84878763652 scopus 로고    scopus 로고
    • Consequences of membrane topography
    • Parmryd, I. and Onfelt, B. (2013) Consequences of membrane topography. FEBS J. 280, 2775-2784
    • (2013) FEBS J. , vol.280 , pp. 2775-2784
    • Parmryd, I.1    Onfelt, B.2
  • 11
    • 0038576209 scopus 로고    scopus 로고
    • Kinetic analysis of receptor-activated phosphoinositide turnover
    • Xu, C., Watras, J. and Loew, L.M. (2003) Kinetic analysis of receptor-activated phosphoinositide turnover. J. Cell Biol. 161, 779-791
    • (2003) J. Cell Biol. , vol.161 , pp. 779-791
    • Xu, C.1    Watras, J.2    Loew, L.M.3
  • 12
    • 0034695461 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate functions as a second messenger that regulates cytoskeleton-plasma membrane adhesion
    • Raucher, D., Stauffer, T., Chen, W., Shen, K., Guo, S., York, J.D., Sheetz, M.P. and Meyer, T. (2000) Phosphatidylinositol 4,5-bisphosphate functions as a second messenger that regulates cytoskeleton-plasma membrane adhesion. Cell 100, 221-228
    • (2000) Cell , vol.100 , pp. 221-228
    • Raucher, D.1    Stauffer, T.2    Chen, W.3    Shen, K.4    Guo, S.5    York, J.D.6    Sheetz, M.P.7    Meyer, T.8
  • 13
    • 0014505028 scopus 로고
    • Fixatives and fixation: A review
    • Hopwood, D. (1969) Fixatives and fixation: a review. Histochem. J. 1, 323-360
    • (1969) Histochem. J. , vol.1 , pp. 323-360
    • Hopwood, D.1
  • 15
    • 0014450636 scopus 로고
    • Quantitative studies on the preservation of choline and ethanolamine phosphatides during tissue preparation for electron microscopy. I. Glutaraldehyde, osmium tetroxide, Araldite methods
    • Cope, G.H. and Williams, M.A. (1969) Quantitative studies on the preservation of choline and ethanolamine phosphatides during tissue preparation for electron microscopy. I. Glutaraldehyde, osmium tetroxide, Araldite methods. J. Microsc. 90, 31-46
    • (1969) J. Microsc. , vol.90 , pp. 31-46
    • Cope, G.H.1    Williams, M.A.2
  • 16
    • 11144344415 scopus 로고    scopus 로고
    • Membrane redistribution of gangliosides and glycosylphosphatidylinositol-anchored proteins in brain tissue sections under conditions of lipid raft isolation
    • Heffer-Lauc, M., Lauc, G., Nimrichter, L., Fromholt, S.E. and Schnaar, R.L. (2005) Membrane redistribution of gangliosides and glycosylphosphatidylinositol-anchored proteins in brain tissue sections under conditions of lipid raft isolation. Biochim. Biophys. Acta 1686, 200-208
    • (2005) Biochim. Biophys. Acta , vol.1686 , pp. 200-208
    • Heffer-Lauc, M.1    Lauc, G.2    Nimrichter, L.3    Fromholt, S.E.4    Schnaar, R.L.5
  • 17
    • 0017365231 scopus 로고
    • Lateral transport of a lipid probe and labeled proteins on a cell membrane
    • Schlessinger, J., Axelrod, D., Koppel, D.E., Webb, W.W. and Elson, E.L. (1977) Lateral transport of a lipid probe and labeled proteins on a cell membrane. Science 195, 307-309
    • (1977) Science , vol.195 , pp. 307-309
    • Schlessinger, J.1    Axelrod, D.2    Koppel, D.E.3    Webb, W.W.4    Elson, E.L.5
  • 18
    • 0029757511 scopus 로고    scopus 로고
    • GPI-anchored proteins, glycosphingolipids, and sphingomyelin are sequestered to caveolae only after crosslinking
    • Fujimoto, T. (1996) GPI-anchored proteins, glycosphingolipids, and sphingomyelin are sequestered to caveolae only after crosslinking. J. Histochem. Cytochem. 44, 929-941
    • (1996) J. Histochem. Cytochem. , vol.44 , pp. 929-941
    • Fujimoto, T.1
  • 19
    • 0034717707 scopus 로고    scopus 로고
    • GAP43, MARCKS, and CAP23 modulate PI(4,5)P2 at plasmalemmal rafts, and regulate cell cortex actin dynamics through a common mechanism
    • Laux, T., Fukami, K., Thelen, M., Golub, T., Frey, D. and Caroni, P. (2000) GAP43, MARCKS, and CAP23 modulate PI(4,5)P2 at plasmalemmal rafts, and regulate cell cortex actin dynamics through a common mechanism. J. Cell Biol. 149, 1455-1472
    • (2000) J. Cell Biol. , vol.149 , pp. 1455-1472
    • Laux, T.1    Fukami, K.2    Thelen, M.3    Golub, T.4    Frey, D.5    Caroni, P.6
  • 20
    • 0018746093 scopus 로고
    • Synaptic vesicle exocytosis captured by quick freezing and correlated with quantal transmitter release
    • Heuser, J.E., Reese, T.S., Dennis, M.J., Jan, Y., Jan, L. and Evans, L. (1979) Synaptic vesicle exocytosis captured by quick freezing and correlated with quantal transmitter release. J. Cell Biol. 81, 275-300
    • (1979) J. Cell Biol. , vol.81 , pp. 275-300
    • Heuser, J.E.1    Reese, T.S.2    Dennis, M.J.3    Jan, Y.4    Jan, L.5    Evans, L.6
  • 21
    • 0029831541 scopus 로고    scopus 로고
    • Comparison of slam-freezing and high-pressure freezing effects on the DNA cholesteric liquid crystalline structure. J.?
    • Leforestier, A., Richter, K., Livolant, F. and Dubochet, J. (1996) Comparison of slam-freezing and high-pressure freezing effects on the DNA cholesteric liquid crystalline structure. J.?Microsc. 184, 4-13
    • (1996) Microsc. , vol.184 , pp. 4-13
    • Leforestier, A.1    Richter, K.2    Livolant, F.3    Dubochet, J.4
  • 22
    • 84985180850 scopus 로고
    • Application of cryoultramicrotomy to immunocytochemistry
    • Tokuyasu, K.T. (1986) Application of cryoultramicrotomy to immunocytochemistry. J. Microsc. 143, 139-149
    • (1986) J. Microsc. , vol.143 , pp. 139-149
    • Tokuyasu, K.T.1
  • 23
  • 24
    • 0342829114 scopus 로고
    • Effects of uranyl ions on lipid bilayer membranes
    • Ginsburg, H. and Wolosin, J.M. (1979) Effects of uranyl ions on lipid bilayer membranes. Chem. Phys. Lipids 23, 125-131
    • (1979) Chem. Phys. Lipids , vol.23 , pp. 125-131
    • Ginsburg, H.1    Wolosin, J.M.2
  • 25
    • 0024042513 scopus 로고
    • Nuclear magnetic resonance and calorimetric study of the structure, dynamics, and phase behavior of uranyl ion/dipalmitoylphosphatidylcholine complexes
    • Huang, T.H., Blume, A., Das Gupta, S.K. and Griffin, R.G. (1988) Nuclear magnetic resonance and calorimetric study of the structure, dynamics, and phase behavior of uranyl ion/dipalmitoylphosphatidylcholine complexes. Biophys. J. 54, 173-179
    • (1988) Biophys. J. , vol.54 , pp. 173-179
    • Huang, T.H.1    Blume, A.2    Das Gupta, S.K.3    Griffin, R.G.4
  • 28
    • 0013905124 scopus 로고
    • Fracture faces of frozen membranes
    • Branton, D. (1966) Fracture faces of frozen membranes. Proc. Natl. Acad. Sci. U.S.A. 55, 1048-1056
    • (1966) Proc. Natl. Acad. Sci. U.S.A. , vol.55 , pp. 1048-1056
    • Branton, D.1
  • 29
    • 0029969182 scopus 로고    scopus 로고
    • Transmembrane phospholipid distribution revealed by freeze-fracture replica labeling
    • Fujimoto, K., Umeda, M. and Fujimoto, T. (1996) Transmembrane phospholipid distribution revealed by freeze-fracture replica labeling. J. Cell Sci. 109, 2453-2460
    • (1996) J. Cell Sci. , vol.109 , pp. 2453-2460
    • Fujimoto, K.1    Umeda, M.2    Fujimoto, T.3
  • 30
    • 34250368055 scopus 로고    scopus 로고
    • Gangliosides GM1 and GM3 in the living cell membrane form clusters susceptible to cholesterol depletion and chilling
    • Fujita, A., Cheng, J., Hirakawa, M., Furukawa, K., Kusunoki, S. and Fujimoto, T. (2007) Gangliosides GM1 and GM3 in the living cell membrane form clusters susceptible to cholesterol depletion and chilling. Mol. Biol. Cell 18, 2112-2122
    • (2007) Mol. Biol. Cell , vol.18 , pp. 2112-2122
    • Fujita, A.1    Cheng, J.2    Hirakawa, M.3    Furukawa, K.4    Kusunoki, S.5    Fujimoto, T.6
  • 31
    • 67249137553 scopus 로고    scopus 로고
    • A distinct pool of phosphatidylinositol 4,5-bisphosphate in caveolae revealed by a nanoscale labeling technique
    • Fujita, A., Cheng, J., Tauchi-Sato, K., Takenawa, T. and Fujimoto, T. (2009) A distinct pool of phosphatidylinositol 4,5-bisphosphate in caveolae revealed by a nanoscale labeling technique. Proc. Natl. Acad. Sci. U.S.A. 106, 9256-9261
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 9256-9261
    • Fujita, A.1    Cheng, J.2    Tauchi-Sato, K.3    Takenawa, T.4    Fujimoto, T.5
  • 32
    • 0027179487 scopus 로고
    • Phospholipids in animal eukaryotic membranes: Transverse asymmetry and movement
    • Zachowski, A. (1993) Phospholipids in animal eukaryotic membranes: transverse asymmetry and movement. Biochem. J. 294, 1-14
    • (1993) Biochem. J. , vol.294 , pp. 1-14
    • Zachowski, A.1


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