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Volumn 119, Issue 3, 1997, Pages 260-272

Electron tomography of neuronal mitochondria: Three-dimensional structure and organization of cristae and membrane contacts

Author keywords

[No Author keywords available]

Indexed keywords

ANIMAL TISSUE; ARTICLE; CELL ULTRASTRUCTURE; CEREBELLUM; CHICKEN; ELECTRON MICROSCOPY; IMAGE RECONSTRUCTION; MITOCHONDRIAL MEMBRANE; NERVE CELL; NONHUMAN; PRIORITY JOURNAL; RAT; THREE DIMENSIONAL IMAGING;

EID: 0030794236     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1006/jsbi.1997.3885     Document Type: Article
Times cited : (306)

References (58)
  • 2
    • 0026008425 scopus 로고
    • Mitochondrial proteins essential for viability mediate protein import into yeast mitochondria
    • Baker K. P., Schatz G. Mitochondrial proteins essential for viability mediate protein import into yeast mitochondria. Nature. 349:1991;205-208.
    • (1991) Nature , vol.349 , pp. 205-208
    • Baker, K.P.1    Schatz, G.2
  • 3
    • 0027336964 scopus 로고
    • Increased extracellular calcium concentrations in the isolated rat heart: Effects on mitochondrial contact site formation
    • Bakker A., De Bie M., Bernaert I., Ravingerova T., Ziegelhoffer A., Van Belle H., Jacob W. Increased extracellular calcium concentrations in the isolated rat heart: Effects on mitochondrial contact site formation. Eur. J. Morphol. 31:1993;46-50.
    • (1993) Eur. J. Morphol. , vol.31 , pp. 46-50
    • Bakker, A.1    De Bie, M.2    Bernaert, I.3    Ravingerova, T.4    Ziegelhoffer, A.5    Van Belle, H.6    Jacob, W.7
  • 4
    • 0025036216 scopus 로고
    • Behavior of mitochondria in the living cell
    • Bereiter-Hahn J. Behavior of mitochondria in the living cell. Int. Rev. Cytol. 122:1990;1-63.
    • (1990) Int. Rev. Cytol. , vol.122 , pp. 1-63
    • Bereiter-Hahn, J.1
  • 5
    • 0029070886 scopus 로고
    • The MIM complex mediates preprotein translocation across the mitochondrial inner membrane and couples it to the mt-Hsp70/ATP driving system
    • Berthold J., Bauer M. F., Schneider H.-C., Klaus C., Dietmeier K., Neupert W., Brunner M. The MIM complex mediates preprotein translocation across the mitochondrial inner membrane and couples it to the mt-Hsp70/ATP driving system. Cell. 81:1995;1085-1093.
    • (1995) Cell , vol.81 , pp. 1085-1093
    • Berthold, J.1    Bauer, M.F.2    Schneider, H.-C.3    Klaus, C.4    Dietmeier, K.5    Neupert, W.6    Brunner, M.7
  • 6
    • 0025714322 scopus 로고
    • Contact sites between inner and outer mitochondrial membranes: A dynamic microcompartment for creatine kinase activity
    • Biermans W., Bakker A., Jacob W. Contact sites between inner and outer mitochondrial membranes: A dynamic microcompartment for creatine kinase activity. Biochim. Biophys. Acta. 1018:1990;225-228.
    • (1990) Biochim. Biophys. Acta , vol.1018 , pp. 225-228
    • Biermans, W.1    Bakker, A.2    Jacob, W.3
  • 9
    • 0026079408 scopus 로고
    • Contact sites between mitochondrial envelope membranes: Structure and function in energy- And protein-transfer
    • Brdiczka D. Contact sites between mitochondrial envelope membranes: Structure and function in energy- and protein-transfer. Biochim. Biophys. Acta. 1071:1991;291-312.
    • (1991) Biochim. Biophys. Acta , vol.1071 , pp. 291-312
    • Brdiczka, D.1
  • 10
    • 0029909729 scopus 로고    scopus 로고
    • The irreversibility of inner mitochondrial membrane permeabilization by Ca2+ plus prooxidants is determined by the extent of membrane protein thiol cross-linking
    • Castilho R. F., Kowaltowski A. J., Vercesi A. E. The irreversibility of inner mitochondrial membrane permeabilization by Ca2+ plus prooxidants is determined by the extent of membrane protein thiol cross-linking. J. Bioenerg. Biomembr. 28:1996;523-529.
    • (1996) J. Bioenerg. Biomembr. , vol.28 , pp. 523-529
    • Castilho, R.F.1    Kowaltowski, A.J.2    Vercesi, A.E.3
  • 11
    • 0013943219 scopus 로고
    • Shape and attachment of the cristae mitochondriales in mouse hepatic cell mitochondria
    • Daems W. T., Wisse E. Shape and attachment of the cristae mitochondriales in mouse hepatic cell mitochondria. J. Ultrastruct. Res. 16:1966;123-140.
    • (1966) J. Ultrastruct. Res. , vol.16 , pp. 123-140
    • Daems, W.T.1    Wisse, E.2
  • 12
    • 0026519544 scopus 로고
    • Transmembrane arrangement of mitochondrial porin or voltage-dependent anion channel (VDAC)
    • De Pinto V. D., Palmieri F. Transmembrane arrangement of mitochondrial porin or voltage-dependent anion channel (VDAC). J. Bioenerg. Biomembr. 24:1992;21-26.
    • (1992) J. Bioenerg. Biomembr. , vol.24 , pp. 21-26
    • De Pinto, V.D.1    Palmieri, F.2
  • 14
    • 0029026737 scopus 로고
    • Approaches to large-scale structures
    • Frank J. Approaches to large-scale structures. Curr. Opin. Struct. Biol. 5:1995;194-201.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 194-201
    • Frank, J.1
  • 15
    • 0024644887 scopus 로고
    • Three-dimensional reconstructions from incomplete data: Interpretability of density maps at "atomic" resolution
    • Glaeser R. M., Tong L., Kim S. H. Three-dimensional reconstructions from incomplete data: Interpretability of density maps at "atomic" resolution. Ultramicroscopy. 27:1989;307-318.
    • (1989) Ultramicroscopy , vol.27 , pp. 307-318
    • Glaeser, R.M.1    Tong, L.2    Kim, S.H.3
  • 18
    • 0013936320 scopus 로고
    • Ultrastructural bases for metabolically linked mechanical activity in mitochondria. I. Reversible ultrastructural changes with change in metabolic steady state in isolated liver mitochondria
    • Hackenbrock C. R. Ultrastructural bases for metabolically linked mechanical activity in mitochondria. I. Reversible ultrastructural changes with change in metabolic steady state in isolated liver mitochondria. J. Cell Biol. 30:1966;269-297.
    • (1966) J. Cell Biol. , vol.30 , pp. 269-297
    • Hackenbrock, C.R.1
  • 19
    • 0014347959 scopus 로고
    • Chemical and physical fixation of isolated mitochondria in low-energy and high-energy states
    • Hackenbrock C. R. Chemical and physical fixation of isolated mitochondria in low-energy and high-energy states. Proc. Natl. Acad. Sci. USA. 61:1968;598-605.
    • (1968) Proc. Natl. Acad. Sci. USA , vol.61 , pp. 598-605
    • Hackenbrock, C.R.1
  • 20
    • 0028316039 scopus 로고
    • A crucial role of the mitochondrial protein import receptor MOM19 for the biogenesis of mitochondria
    • Harkness T. A., Nargang F. E., van der Klei I., Neupert W., Lill R. A crucial role of the mitochondrial protein import receptor MOM19 for the biogenesis of mitochondria. J. Cell Biol. 124:1994;637-648.
    • (1994) J. Cell Biol. , vol.124 , pp. 637-648
    • Harkness, T.A.1    Nargang, F.E.2    Van Der Klei, I.3    Neupert, W.4    Lill, R.5
  • 21
    • 0019464219 scopus 로고
    • Ultrastructure of hepatic mitochondria in a child with hyperornithinemia, hyperammonemia and homocitrullinuria
    • Haust M. D., Gatfield P. D., Gordon B. A. Ultrastructure of hepatic mitochondria in a child with hyperornithinemia, hyperammonemia and homocitrullinuria. Hum. Pathol. 12:1981;212-222.
    • (1981) Hum. Pathol. , vol.12 , pp. 212-222
    • Haust, M.D.1    Gatfield, P.D.2    Gordon, B.A.3
  • 23
    • 0028981464 scopus 로고
    • Alterations of Ca2+/calmodulin-dependent protein kinase II and its messenger RNA in the rat hippocampus following normo- And hypothermic ischemia
    • Hu B.-R., Kamme F., Wieloch T. Alterations of Ca2+/calmodulin-dependent protein kinase II and its messenger RNA in the rat hippocampus following normo- and hypothermic ischemia. Neurosci. 68:1995;1003-1016.
    • (1995) Neurosci. , vol.68 , pp. 1003-1016
    • Hu, B.-R.1    Kamme, F.2    Wieloch, T.3
  • 24
    • 0028326451 scopus 로고
    • Mitochondrial matrix granules: Their behavior during changing metabolic situations and their relationship to contact sites between inner and outer mitochondrial membranes
    • Jacob W., Bakker A., Hertsens R. C., Biermans W. Mitochondrial matrix granules: Their behavior during changing metabolic situations and their relationship to contact sites between inner and outer mitochondrial membranes. Microsc. Res. Tech. 27:1994;307-318.
    • (1994) Microsc. Res. Tech. , vol.27 , pp. 307-318
    • Jacob, W.1    Bakker, A.2    Hertsens, R.C.3    Biermans, W.4
  • 25
    • 0026078742 scopus 로고
    • Alignment of tomographic projections using an incomplete set of fiducial markers
    • Jing Z., Sachs F. Alignment of tomographic projections using an incomplete set of fiducial markers. Ultramicroscopy. 35:1991;37-43.
    • (1991) Ultramicroscopy , vol.35 , pp. 37-43
    • Jing, Z.1    Sachs, F.2
  • 26
    • 0010599332 scopus 로고
    • Three-dimensional reconstruction of a dictyosome using serial sections
    • Kristen U., Lockhausen J., Robinson D. G. Three-dimensional reconstruction of a dictyosome using serial sections. J. Exp. Bot. 35:1984;1113-1118.
    • (1984) J. Exp. Bot. , vol.35 , pp. 1113-1118
    • Kristen, U.1    Lockhausen, J.2    Robinson, D.G.3
  • 27
    • 0028212585 scopus 로고
    • Variations in mitochondrial ultrastructure and dynamics observed by high resolution scanning electron microscopy (HRSEM)
    • Lea P. J., Temkin R. J., Freeman K. B., Mitchell G. A., Robinson B. H. Variations in mitochondrial ultrastructure and dynamics observed by high resolution scanning electron microscopy (HRSEM). Microsc. Res. Tech. 27:1994;269-277.
    • (1994) Microsc. Res. Tech. , vol.27 , pp. 269-277
    • Lea, P.J.1    Temkin, R.J.2    Freeman, K.B.3    Mitchell, G.A.4    Robinson, B.H.5
  • 28
    • 0022401384 scopus 로고
    • The neuronal endomembrane system: III. The origins of the axoplasmic reticulum and discrete axonal cisternae at the axon hillock
    • Lindsey J. D., Ellisman M. H. The neuronal endomembrane system: III. The origins of the axoplasmic reticulum and discrete axonal cisternae at the axon hillock. J. Neurosci. 5:1985;3135-3144.
    • (1985) J. Neurosci. , vol.5 , pp. 3135-3144
    • Lindsey, J.D.1    Ellisman, M.H.2
  • 30
    • 0002042418 scopus 로고
    • Sample shrinkage and radiation damage
    • New York: Plenum. p. 39-60
    • Luther P. Sample shrinkage and radiation damage. Electron Tomography. 1992;Plenum, New York. p. 39-60.
    • (1992) Electron Tomography
    • Luther, P.1
  • 31
    • 0026538575 scopus 로고
    • Toward the molecular structure of the mitochondrial channel, VDAC
    • Mannella C. A., Forte M., Colombini M. Toward the molecular structure of the mitochondrial channel, VDAC. J. Bioenerg. Biomembr. 24:1992;7-19.
    • (1992) J. Bioenerg. Biomembr. , vol.24 , pp. 7-19
    • Mannella, C.A.1    Forte, M.2    Colombini, M.3
  • 32
    • 0028211292 scopus 로고
    • The internal compartmentation of rat-liver mitochondria: Tomographic study using the high-voltage transmission electron microscope
    • Mannella C. A., Marko M., Penczek P., Barnard D., Frank J. The internal compartmentation of rat-liver mitochondria: Tomographic study using the high-voltage transmission electron microscope. Microsc. Res. Tech. 27:1994;278-283.
    • (1994) Microsc. Res. Tech. , vol.27 , pp. 278-283
    • Mannella, C.A.1    Marko, M.2    Penczek, P.3    Barnard, D.4    Frank, J.5
  • 33
    • 0027363117 scopus 로고
    • Three-dimensional visualization of the smooth endoplasmic reticulum in Purkinje cell dendrites
    • Martone M. E., Zhang Y., Simpliciano V. M., Carragher B. O., Ellisman M. H. Three-dimensional visualization of the smooth endoplasmic reticulum in Purkinje cell dendrites. J. Neurosci. 13:1993;4636-4646.
    • (1993) J. Neurosci. , vol.13 , pp. 4636-4646
    • Martone, M.E.1    Zhang, Y.2    Simpliciano, V.M.3    Carragher, B.O.4    Ellisman, M.H.5
  • 34
    • 0021740822 scopus 로고
    • Ultrastructural changes in fibroblast mitochondria of a patient with HHH-syndrome
    • Metoki K., Hommes F. A., Dyken P., Kelloes C., Trefz J. Ultrastructural changes in fibroblast mitochondria of a patient with HHH-syndrome. J. Inherit. Metab. Dis. 7:1984;147-150.
    • (1984) J. Inherit. Metab. Dis. , vol.7 , pp. 147-150
    • Metoki, K.1    Hommes, F.A.2    Dyken, P.3    Kelloes, C.4    Trefz, J.5
  • 35
    • 0001001129 scopus 로고
    • The fine structure of mitochondria
    • Palade G. The fine structure of mitochondria. Anat. Rec. 114:1952;427-451.
    • (1952) Anat. Rec. , vol.114 , pp. 427-451
    • Palade, G.1
  • 36
    • 0027508994 scopus 로고
    • Modulation of the mitochondrial cyclosporin A-sensitive permeability transition pore II. The minimal requirements for pore induction underscore a key role for transmembrane electrical potential, matrix pH, and matrix Ca2+
    • Petronilli V., Cola C., Bernardi P. Modulation of the mitochondrial cyclosporin A-sensitive permeability transition pore II. The minimal requirements for pore induction underscore a key role for transmembrane electrical potential, matrix pH, and matrix Ca2+. J. Biol. Chem. 268:1993;1011-1016.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1011-1016
    • Petronilli, V.1    Cola, C.2    Bernardi, P.3
  • 37
    • 0025360581 scopus 로고
    • The mitochondrial protein import apparatus
    • Pfanner N., Neupert W. The mitochondrial protein import apparatus. Annu. Rev. Biochem. 59:1990;331-353.
    • (1990) Annu. Rev. Biochem. , vol.59 , pp. 331-353
    • Pfanner, N.1    Neupert, W.2
  • 38
    • 0026553323 scopus 로고
    • A dynamic model of the mitochondrial import machinery
    • Pfanner N., Rassow J., van der Klei I. J., Neupert W. A dynamic model of the mitochondrial import machinery. Cell. 68:1992;999-1002.
    • (1992) Cell , vol.68 , pp. 999-1002
    • Pfanner, N.1    Rassow, J.2    Van Der Klei, I.J.3    Neupert, W.4
  • 39
    • 0001339881 scopus 로고
    • Three-dimensional reconstruction of single particles from random and nonrandom tilt series
    • Radermacher M. Three-dimensional reconstruction of single particles from random and nonrandom tilt series. J. Electron Microsc. Tech. 9:1988;359-394.
    • (1988) J. Electron Microsc. Tech. , vol.9 , pp. 359-394
    • Radermacher, M.1
  • 41
    • 0024454311 scopus 로고
    • Translocation arrest by reversible folding of a precursor protein imported into mitochondria. A means to quantitate translocation contact sites
    • Rassow J., Guiard B., Wienues U., Herzog V., Hartl F.-U., Neupert W. Translocation arrest by reversible folding of a precursor protein imported into mitochondria. A means to quantitate translocation contact sites. J. Cell Biol. 109:1989;1421-1428.
    • (1989) J. Cell Biol. , vol.109 , pp. 1421-1428
    • Rassow, J.1    Guiard, B.2    Wienues, U.3    Herzog, V.4    Hartl, F.-U.5    Neupert, W.6
  • 42
    • 0024999562 scopus 로고
    • Polypeptides traverse the mitochondrial envelope in an extended state
    • Rassow J., Hartl F. U., Guiard B., Pfanner N., Neupert W. Polypeptides traverse the mitochondrial envelope in an extended state. FEBS Lett. 275:1990;190-194.
    • (1990) FEBS Lett. , vol.275 , pp. 190-194
    • Rassow, J.1    Hartl, F.U.2    Guiard, B.3    Pfanner, N.4    Neupert, W.5
  • 43
    • 0026040249 scopus 로고
    • Mitochondrial preproteins en route from the outer membrane to the inner membrane are exposed to the intermembrane spaces
    • Rassow J., Pfanner N. Mitochondrial preproteins en route from the outer membrane to the inner membrane are exposed to the intermembrane spaces. FEBS Lett. 293:1991;85-88.
    • (1991) FEBS Lett. , vol.293 , pp. 85-88
    • Rassow, J.1    Pfanner, N.2
  • 44
    • 0026124864 scopus 로고
    • A software system for interactive and quantitative visualization of multidimensional biomedical images
    • Robb R. A., Hanson D. P. A software system for interactive and quantitative visualization of multidimensional biomedical images. Aust. Phys. Eng. Sci. Med. 14:1991;9-30.
    • (1991) Aust. Phys. Eng. Sci. Med. , vol.14 , pp. 9-30
    • Robb, R.A.1    Hanson, D.P.2
  • 45
    • 0001580678 scopus 로고
    • A modified method for lead staining
    • Sato T. A modified method for lead staining. J. Electron Microsc. 16:1967;133-141.
    • (1967) J. Electron Microsc. , vol.16 , pp. 133-141
    • Sato, T.1
  • 46
    • 0029979607 scopus 로고    scopus 로고
    • Common principles of protein translocation across membranes
    • Schatz G., Dobberstein B. Common principles of protein translocation across membranes. Science. 271:1996;1519-1526.
    • (1996) Science , vol.271 , pp. 1519-1526
    • Schatz, G.1    Dobberstein, B.2
  • 47
    • 0023779363 scopus 로고
    • Native mitochondrial creatine kinase forms octameric structures. II. Characterization of dimers and octamers by ultracentrifugation, direct mass measurements by scanning transmission electron microscopy, and image analysis of single mitochondrial creatine kinase octamers
    • Schnyder T., Engel A., Lustig A., Wallimann T. Native mitochondrial creatine kinase forms octameric structures. II. Characterization of dimers and octamers by ultracentrifugation, direct mass measurements by scanning transmission electron microscopy, and image analysis of single mitochondrial creatine kinase octamers. J. Biol. Chem. 263:1988;16954-16962.
    • (1988) J. Biol. Chem. , vol.263 , pp. 16954-16962
    • Schnyder, T.1    Engel, A.2    Lustig, A.3    Wallimann, T.4
  • 48
    • 0029928871 scopus 로고    scopus 로고
    • SUPRIM: Easily modified image processing software
    • Schroeter J. P., Bretaudiere J.-P. SUPRIM: Easily modified image processing software. J. Struct. Biol. 116:1996;131-137.
    • (1996) J. Struct. Biol. , vol.116 , pp. 131-137
    • Schroeter, J.P.1    Bretaudiere, J.-P.2
  • 49
    • 0029055754 scopus 로고
    • Evidence that phosphatidylserine is imported into mitochondria via a mitochondria-associated membrane and that the majority of mitochondrial phosphatidylethanolamine is derived from decarboxylation of phosphatidylserine
    • Shiao Y.-J., Lupo G., Vance J. E. Evidence that phosphatidylserine is imported into mitochondria via a mitochondria-associated membrane and that the majority of mitochondrial phosphatidylethanolamine is derived from decarboxylation of phosphatidylserine. J. Biol. Chem. 270:1995;11190-11198.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11190-11198
    • Shiao, Y.-J.1    Lupo, G.2    Vance, J.E.3
  • 50
    • 34250691686 scopus 로고
    • Electron microscopy of mitochondria and cytoplasmic double membranes
    • Sjostrand F. S. Electron microscopy of mitochondria and cytoplasmic double membranes. Nature. 171:1953;30-31.
    • (1953) Nature , vol.171 , pp. 30-31
    • Sjostrand, F.S.1
  • 52
    • 0019225889 scopus 로고
    • Relationships between mitochondrial outer membranes and agranular reticulum in nervous tissue: Ultrastructural observations and a new interpretation
    • Spacek J., Lieberman A. R. Relationships between mitochondrial outer membranes and agranular reticulum in nervous tissue: ultrastructural observations and a new interpretation. J. Cell Sci. 46:1980;129-147.
    • (1980) J. Cell Sci. , vol.46 , pp. 129-147
    • Spacek, J.1    Lieberman, A.R.2
  • 54
    • 0030059122 scopus 로고    scopus 로고
    • Intracellular trafficking of phospholipids: Import of phosphatidylserine into mitochondria
    • Vance J. E., Shiao Y. J. Intracellular trafficking of phospholipids: Import of phosphatidylserine into mitochondria. Anticancer Res. 16:1996;1333-1339.
    • (1996) Anticancer Res. , vol.16 , pp. 1333-1339
    • Vance, J.E.1    Shiao, Y.J.2
  • 55
    • 0020489067 scopus 로고
    • Possible role of non-bilayer lipids in the structure of mitochondria: A freeze-fracture electron microscopy study
    • van Venetie R., Verkleij A. J. Possible role of non-bilayer lipids in the structure of mitochondria: A freeze-fracture electron microscopy study. Biochim. Biophys. Acta. 692:1982;397-405.
    • (1982) Biochim. Biophys. Acta , vol.692 , pp. 397-405
    • Van Venetie, R.1    Verkleij, A.J.2
  • 56
    • 0025805164 scopus 로고
    • Resolution limit of serial sections for 3D reconstruction of tubular cristae in rat liver mitochondria
    • Winslow J. L., Hollenberg M. J., Lea P. J. Resolution limit of serial sections for 3D reconstruction of tubular cristae in rat liver mitochondria. J. Electron Microsc. Tech. 18:1991;241-248.
    • (1991) J. Electron Microsc. Tech. , vol.18 , pp. 241-248
    • Winslow, J.L.1    Hollenberg, M.J.2    Lea, P.J.3
  • 58
    • 0005943239 scopus 로고
    • The organization of chromosomes and chromatin
    • J. Frank. New York: Plenum
    • Woodcock C. L. The organization of chromosomes and chromatin. Frank J. Electron Tomography. 1992;313-337 Plenum, New York.
    • (1992) Electron Tomography , pp. 313-337
    • Woodcock, C.L.1


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