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Volumn 315, Issue , 2014, Pages 49-60

Inner ear tissue preservation by rapid freezing: Improving fixation by high-pressure freezing and hybrid methods

Author keywords

[No Author keywords available]

Indexed keywords

ADULT; ANIMAL CELL; ANIMAL TISSUE; ARTICLE; ARTIFACT REDUCTION; CILIATED EPITHELIUM; CONTROLLED STUDY; ELECTRON MICROSCOPY; INNER EAR; INTERMETHOD COMPARISON; MOUSE; NEUROEPITHELIUM; NONHUMAN; PRIORITY JOURNAL; PROCESS OPTIMIZATION; QUALITY CONTROL; RAPID FREEZE FIXATION; ROOM TEMPERATURE; TEMPERATURE SENSITIVITY; TISSUE PRESERVATION; ANIMAL; ANIMAL MODEL; ARTIFACT; C57BL MOUSE; CRYOPRESERVATION; GERBIL; GUINEA PIG; NOTOPHTHALMUS VIRIDESCENS; ORGAN PRESERVATION; PATHOLOGY; PROCEDURES; STEREOCILIUM; TIME; TISSUE FIXATION; ULTRASTRUCTURE;

EID: 84904467287     PISSN: 03785955     EISSN: 18785891     Source Type: Journal    
DOI: 10.1016/j.heares.2014.06.006     Document Type: Article
Times cited : (20)

References (42)
  • 2
    • 0018818037 scopus 로고
    • Further studies of specimen volume changes during processing for SEM: including some plant tissue
    • 132
    • Boyde A., Boyde S. Further studies of specimen volume changes during processing for SEM: including some plant tissue. Scanning Electron Microsc. 1980, 117-124. 132.
    • (1980) Scanning Electron Microsc. , pp. 117-124
    • Boyde, A.1    Boyde, S.2
  • 3
    • 0005930565 scopus 로고
    • Effects of varying the vehicle for OsO4 in tissue fixation
    • Caulfield J.B. Effects of varying the vehicle for OsO4 in tissue fixation. J.Biophys. Biochem. Cytol. 1957, 3:827-830.
    • (1957) J.Biophys. Biochem. Cytol. , vol.3 , pp. 827-830
    • Caulfield, J.B.1
  • 4
    • 8444239775 scopus 로고    scopus 로고
    • High-pressure freezing and freeze substitution of gravid Caenorhabditis elegans (Nematoda: Rhabditida) for transmission electron microscopy
    • Claeys M., Vanhecke D., Couvreur M., Tytgat T., Coomans A., Borgonie G. High-pressure freezing and freeze substitution of gravid Caenorhabditis elegans (Nematoda: Rhabditida) for transmission electron microscopy. Nematology 2004, 6:319-327.
    • (2004) Nematology , vol.6 , pp. 319-327
    • Claeys, M.1    Vanhecke, D.2    Couvreur, M.3    Tytgat, T.4    Coomans, A.5    Borgonie, G.6
  • 5
    • 0024426168 scopus 로고
    • High-pressure freezing for the preservation of biological structure: theory and practice
    • Dahl R., Staehelin L.A. High-pressure freezing for the preservation of biological structure: theory and practice. J.Electron Microsc. Tech. 1989, 13:165-174.
    • (1989) J.Electron Microsc. Tech. , vol.13 , pp. 165-174
    • Dahl, R.1    Staehelin, L.A.2
  • 6
    • 0019302885 scopus 로고
    • Actin in the inner-ear - the remarkable structure of the stereocilium
    • Derosier D.J., Tilney L.G., Egelman E. Actin in the inner-ear - the remarkable structure of the stereocilium. Nature 1980, 287:291-296.
    • (1980) Nature , vol.287 , pp. 291-296
    • Derosier, D.J.1    Tilney, L.G.2    Egelman, E.3
  • 9
    • 0017715603 scopus 로고
    • Actin-filaments in sensory hairs of inner-ear receptor cells
    • Flock A., Cheung H.C. Actin-filaments in sensory hairs of inner-ear receptor cells. J.Cell. Biol. 1977, 75:339-343.
    • (1977) J.Cell. Biol. , vol.75 , pp. 339-343
    • Flock, A.1    Cheung, H.C.2
  • 10
    • 0025809008 scopus 로고
    • Assessment of ultrastructure in isolated cochlear hair-cells using a procedure for rapid freezing before freeze-fracture and deep-etching
    • Forge A., Davies S., Zajic G. Assessment of ultrastructure in isolated cochlear hair-cells using a procedure for rapid freezing before freeze-fracture and deep-etching. J.Neurocytol. 1991, 20:471-484.
    • (1991) J.Neurocytol. , vol.20 , pp. 471-484
    • Forge, A.1    Davies, S.2    Zajic, G.3
  • 12
    • 0022653966 scopus 로고
    • Advances in ultra-rapid freezing for the preservation of cellular ultrastructure
    • Gilkey J.C., Staehelin L.A. Advances in ultra-rapid freezing for the preservation of cellular ultrastructure. J.Electron Microsc. Tech. 1986, 3:177-210.
    • (1986) J.Electron Microsc. Tech. , vol.3 , pp. 177-210
    • Gilkey, J.C.1    Staehelin, L.A.2
  • 14
    • 0020352825 scopus 로고
    • Interactions between actin-filaments and between actin-filaments and membranes in quick-frozen and deeply etched hair-cells of the chick ear
    • Hirokawa N., Tilney L.G. Interactions between actin-filaments and between actin-filaments and membranes in quick-frozen and deeply etched hair-cells of the chick ear. J.Cell. Biol. 1982, 95:249-261.
    • (1982) J.Cell. Biol. , vol.95 , pp. 249-261
    • Hirokawa, N.1    Tilney, L.G.2
  • 15
    • 0025285144 scopus 로고
    • Structural basis for mechanical transduction in the frog vestibular sensory apparatus .1. The otolithic membrane
    • Kachar B., Parakkal M., Fex J. Structural basis for mechanical transduction in the frog vestibular sensory apparatus .1. The otolithic membrane. Hear. Res. 1990, 45:179-190.
    • (1990) Hear. Res. , vol.45 , pp. 179-190
    • Kachar, B.1    Parakkal, M.2    Fex, J.3
  • 17
    • 0026092306 scopus 로고
    • The potential of cryofixation and freeze substitution: observations and theoretical considerations
    • Kellenberger E. The potential of cryofixation and freeze substitution: observations and theoretical considerations. J.Microsc. 1991, 161:183-203.
    • (1991) J.Microsc. , vol.161 , pp. 183-203
    • Kellenberger, E.1
  • 18
    • 0041837558 scopus 로고    scopus 로고
    • Electron microscopy in cell biology: integrating structure and function
    • Koster A.J., Klumperman J. Electron microscopy in cell biology: integrating structure and function. Nat. Cell. Biol. 2003, Ss6-Ss10.
    • (2003) Nat. Cell. Biol.
    • Koster, A.J.1    Klumperman, J.2
  • 19
    • 0029831541 scopus 로고    scopus 로고
    • Comparison of slam-freezing and high-pressure freezing effects on the DNA cholesteric liquid crystalline structure
    • Leforestier A., Richter K., Livolant F., Dubochet J. Comparison of slam-freezing and high-pressure freezing effects on the DNA cholesteric liquid crystalline structure. J.Microsc. 1996, 184:4-13.
    • (1996) J.Microsc. , vol.184 , pp. 4-13
    • Leforestier, A.1    Richter, K.2    Livolant, F.3    Dubochet, J.4
  • 20
    • 84884239080 scopus 로고    scopus 로고
    • Cryo-electron tomography: the challenge of doing structural biology in situ
    • Lucic V., Rigort A., Baumeister W. Cryo-electron tomography: the challenge of doing structural biology in situ. J.Cell. Biol. 2013, 202:407-419.
    • (2013) J.Cell. Biol. , vol.202 , pp. 407-419
    • Lucic, V.1    Rigort, A.2    Baumeister, W.3
  • 21
    • 79961226745 scopus 로고    scopus 로고
    • Freeze substitution in 3 hours or less
    • McDonald K.L., Webb R.I. Freeze substitution in 3 hours or less. J.Microsc. 2011, 243:227-233.
    • (2011) J.Microsc. , vol.243 , pp. 227-233
    • McDonald, K.L.1    Webb, R.I.2
  • 22
    • 33847186352 scopus 로고    scopus 로고
    • Recent advances in high-pressure freezing: equipment and specimen-loading methods
    • Humana Press, J. Kuo (Ed.)
    • McDonald K.L.M.,M., Verkade P., Muller-Reichert T. Recent advances in high-pressure freezing: equipment and specimen-loading methods. Electron Microscopy: Methods and Protocols 2007, 143-173. Humana Press. second ed. J. Kuo (Ed.).
    • (2007) Electron Microscopy: Methods and Protocols , pp. 143-173
    • McDonald, K.L.M.M.1    Verkade, P.2    Muller-Reichert, T.3
  • 23
    • 0025195494 scopus 로고
    • Improved cryoprotection and freeze-substitution of embryonic quail retina - a Tem study on ultrastructural preservation
    • Meissner D.H., Schwarz H. Improved cryoprotection and freeze-substitution of embryonic quail retina - a Tem study on ultrastructural preservation. J.Electron Microsc. Tech. 1990, 14:348-356.
    • (1990) J.Electron Microsc. Tech. , vol.14 , pp. 348-356
    • Meissner, D.H.1    Schwarz, H.2
  • 25
    • 8044255969 scopus 로고
    • Cryopreparation of microorganisms for electron microscopy
    • Academic Press Limited, F. Mayer (Ed.)
    • Muller M. Cryopreparation of microorganisms for electron microscopy. Electron Microscopy in Microbiology 1988, 1-28. Academic Press Limited. F. Mayer (Ed.).
    • (1988) Electron Microscopy in Microbiology , pp. 1-28
    • Muller, M.1
  • 26
    • 84857030159 scopus 로고    scopus 로고
    • Helical arrangement of filaments in microvillar actin bundles
    • Ohta K., Higashi R., Sawaguchi A., Nakamura K. Helical arrangement of filaments in microvillar actin bundles. J.Struct. Biol. 2012, 177:513-519.
    • (2012) J.Struct. Biol. , vol.177 , pp. 513-519
    • Ohta, K.1    Higashi, R.2    Sawaguchi, A.3    Nakamura, K.4
  • 27
    • 0036558286 scopus 로고    scopus 로고
    • Visualisation of the actin cytoskelton by cryo-electron microscopy
    • Resch G.P., Goldie K.N., Krebs A., Hoenger A., Small J.V. Visualisation of the actin cytoskelton by cryo-electron microscopy. J.Cell. Sci. 2002, 115:1877-1882.
    • (2002) J.Cell. Sci. , vol.115 , pp. 1877-1882
    • Resch, G.P.1    Goldie, K.N.2    Krebs, A.3    Hoenger, A.4    Small, J.V.5
  • 28
    • 1642322799 scopus 로고    scopus 로고
    • An actin molecular treadmill and myosins maintain stereocilia functional architecture and self-renewal
    • Rzadzinska A.K., Schneider M.E., Davies C., Riordan G.P., Kachar B. An actin molecular treadmill and myosins maintain stereocilia functional architecture and self-renewal. J.Cell. Biol. 2004, 164:887-897.
    • (2004) J.Cell. Biol. , vol.164 , pp. 887-897
    • Rzadzinska, A.K.1    Schneider, M.E.2    Davies, C.3    Riordan, G.P.4    Kachar, B.5
  • 30
    • 0031859879 scopus 로고    scopus 로고
    • High-pressure freezing causes structural alterations in phospholipid model membranes
    • Semmler K., Wunderlich J., Richter W., Meyer H.W. High-pressure freezing causes structural alterations in phospholipid model membranes. J.Microsc-Oxford 1998, 190:317-327.
    • (1998) J.Microsc-Oxford , vol.190 , pp. 317-327
    • Semmler, K.1    Wunderlich, J.2    Richter, W.3    Meyer, H.W.4
  • 31
    • 0019840118 scopus 로고
    • Organization of actin in the leading edge of cultured cells: influence of osmium tetroxide and dehydration on the ultrastructure of actin meshworks
    • Small J.V. Organization of actin in the leading edge of cultured cells: influence of osmium tetroxide and dehydration on the ultrastructure of actin meshworks. J.Cell. Biol. 1981, 91:695-705.
    • (1981) J.Cell. Biol. , vol.91 , pp. 695-705
    • Small, J.V.1
  • 33
    • 21344448644 scopus 로고    scopus 로고
    • Development of a model for microphysiological simulations: small nodes of ranvier from peripheral nerves of mice reconstructed by electron tomography
    • Sosinsky G.E., Deerinck T.J., Greco R., Buitenhuys C.H., Bartol T.M., Ellisman M.H. Development of a model for microphysiological simulations: small nodes of ranvier from peripheral nerves of mice reconstructed by electron tomography. Neuroinformatics 2005, 3:133-162.
    • (2005) Neuroinformatics , vol.3 , pp. 133-162
    • Sosinsky, G.E.1    Deerinck, T.J.2    Greco, R.3    Buitenhuys, C.H.4    Bartol, T.M.5    Ellisman, M.H.6
  • 34
    • 40649107390 scopus 로고    scopus 로고
    • The combination of chemical fixation procedures with high pressure freezing and freeze substitution preserves highly labile tissue ultrastructure for electron tomography applications
    • Sosinsky G.E., Crum J., Jones Y.Z., Lanman J., Smarr B., Terada M., Martone M.E., Deerinck T.J., Johnson J.E., Ellisman M.H. The combination of chemical fixation procedures with high pressure freezing and freeze substitution preserves highly labile tissue ultrastructure for electron tomography applications. J.Struct. Biol. 2008, 161:359-371.
    • (2008) J.Struct. Biol. , vol.161 , pp. 359-371
    • Sosinsky, G.E.1    Crum, J.2    Jones, Y.Z.3    Lanman, J.4    Smarr, B.5    Terada, M.6    Martone, M.E.7    Deerinck, T.J.8    Johnson, J.E.9    Ellisman, M.H.10
  • 35
    • 0022384765 scopus 로고
    • Recrystallization and ice-crystal growth in a biological specimen, as shown by a simple freeze substitution method
    • Steinbrecht R.A. Recrystallization and ice-crystal growth in a biological specimen, as shown by a simple freeze substitution method. J.Microsc-Oxford 1985, 140:41-46.
    • (1985) J.Microsc-Oxford , vol.140 , pp. 41-46
    • Steinbrecht, R.A.1
  • 36
    • 0001131615 scopus 로고
    • High-pressure freezing of soybean nodules leads to an improved preservation of ultrastructure
    • Studer D., Hennecke H., Muller M. High-pressure freezing of soybean nodules leads to an improved preservation of ultrastructure. Planta 1992, 188:155-163.
    • (1992) Planta , vol.188 , pp. 155-163
    • Studer, D.1    Hennecke, H.2    Muller, M.3
  • 37
    • 54049097431 scopus 로고    scopus 로고
    • Electron microscopy of high pressure frozen samples: bridging the gap between cellular ultrastructure and atomic resolution
    • Studer D., Humbel B.M., Chiquet M. Electron microscopy of high pressure frozen samples: bridging the gap between cellular ultrastructure and atomic resolution. Histochem. Cell. Biol. 2008, 130:877-889.
    • (2008) Histochem. Cell. Biol. , vol.130 , pp. 877-889
    • Studer, D.1    Humbel, B.M.2    Chiquet, M.3
  • 38
    • 0035462162 scopus 로고    scopus 로고
    • Anew approach for cryofixation by high-pressure freezing
    • Studer D., Graber W., Al-Amoudi A., Eggli P. Anew approach for cryofixation by high-pressure freezing. J.Microsc. 2001, 203:285-294.
    • (2001) J.Microsc. , vol.203 , pp. 285-294
    • Studer, D.1    Graber, W.2    Al-Amoudi, A.3    Eggli, P.4
  • 40
    • 14644393078 scopus 로고    scopus 로고
    • Hair cell regeneration in sensory epithelia from the inner ear of a urodele amphibian
    • Taylor R.R., Forge A. Hair cell regeneration in sensory epithelia from the inner ear of a urodele amphibian. J.Comp. Neurol. 2005, 484:105-120.
    • (2005) J.Comp. Neurol. , vol.484 , pp. 105-120
    • Taylor, R.R.1    Forge, A.2
  • 41
    • 0032487531 scopus 로고    scopus 로고
    • Why are two different cross-linkers necessary for actin bundle formation invivo and what does each cross-link contribute?
    • Tilney L.G., Connelly P.S., Vranich K.A., Shaw M.K., Guild G.M. Why are two different cross-linkers necessary for actin bundle formation invivo and what does each cross-link contribute?. J.Cell. Biol. 1998, 143:121-133.
    • (1998) J.Cell. Biol. , vol.143 , pp. 121-133
    • Tilney, L.G.1    Connelly, P.S.2    Vranich, K.A.3    Shaw, M.K.4    Guild, G.M.5
  • 42
    • 0017135770 scopus 로고
    • Chemical nature of osmium tetroxide fixation and staining of membranes by X-Ray photoelectron-spectroscopy
    • White D.L., Andrews S.B., Faller J.W., Barrnett R.J. Chemical nature of osmium tetroxide fixation and staining of membranes by X-Ray photoelectron-spectroscopy. Biochim. Biophys. Acta 1976, 436:577-592.
    • (1976) Biochim. Biophys. Acta , vol.436 , pp. 577-592
    • White, D.L.1    Andrews, S.B.2    Faller, J.W.3    Barrnett, R.J.4


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