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Volumn 36, Issue 3, 1997, Pages 179-187

Redistribution of DNA topoisomerase II β after in vitro stabilization of human erythroleukemic nuclei by heat or Cu++ revealed by confocal microscopy

Author keywords

3 D reconstruction; confocal microscopy; nuclear matrix; topoisomerase

Indexed keywords

CONFOCAL MICROSCOPY; DNA; FLUORESCENCE; IMAGE RECONSTRUCTION; MONOCLONAL ANTIBODIES; SCAFFOLDS; SCAFFOLDS (BIOLOGY); VOLUMETRIC ANALYSIS;

EID: 0030980556     PISSN: 1059910X     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0029(19970201)36:3<179::AID-JEMT6>3.0.CO;2-K     Document Type: Article
Times cited : (16)

References (43)
  • 1
    • 0027383759 scopus 로고
    • Nuclear organization of splicing snRNPs during differentiation of murine erythroleukemia cells in vitro
    • Antoniou, M., Carmo-Fonseca, M., Ferreira, J., and Lamond, A.I. (1993) Nuclear organization of splicing snRNPs during differentiation of murine erythroleukemia cells in vitro. J. Cell Biol., 123:1055-1068.
    • (1993) J. Cell Biol. , vol.123 , pp. 1055-1068
    • Antoniou, M.1    Carmo-Fonseca, M.2    Ferreira, J.3    Lamond, A.I.4
  • 2
    • 0027299710 scopus 로고
    • Treatment with a polyamine analog alters DNA-matrix association in HeLa cell nuclei: A nucleoid halo assay
    • Basu, H.S., Wright, W.D., Deen, D.F., Roti-Roti, J., and Marton, L.J. (1993) Treatment with a polyamine analog alters DNA-matrix association in HeLa cell nuclei: A nucleoid halo assay. Biochemistry, 32:4073-4076.
    • (1993) Biochemistry , vol.32 , pp. 4073-4076
    • Basu, H.S.1    Wright, W.D.2    Deen, D.F.3    Roti-Roti, J.4    Marton, L.J.5
  • 3
    • 0026071401 scopus 로고
    • A comprehensive study on the isolation and characterization of the HeLa S3 nuclear matrix
    • Belgrader, P., Siegel, A.J., and Berezney, R. (1991) A comprehensive study on the isolation and characterization of the HeLa S3 nuclear matrix. J. Cell Sci., 98:281-291.
    • (1991) J. Cell Sci. , vol.98 , pp. 281-291
    • Belgrader, P.1    Siegel, A.J.2    Berezney, R.3
  • 4
    • 0001532085 scopus 로고
    • Organization and functions of the nuclear matrix
    • L.S. Hnilica, ed. CRC Press, Boca Raton, FL
    • Berezney, R. (1984) Organization and functions of the nuclear matrix. In: Chromosomal Nonhistone Proteins, Vol. IV. L.S. Hnilica, ed. CRC Press, Boca Raton, FL, pp. 119-180.
    • (1984) Chromosomal Nonhistone Proteins , vol.4 , pp. 119-180
    • Berezney, R.1
  • 5
    • 0025939613 scopus 로고
    • The nuclear matrix: A heuristic model for investigating genomic organization and function in the cell nucleus
    • Berezney, R. (1991) The nuclear matrix: A heuristic model for investigating genomic organization and function in the cell nucleus. J. Cell. Biochem., 47:109-123.
    • (1991) J. Cell. Biochem. , vol.47 , pp. 109-123
    • Berezney, R.1
  • 6
    • 0024094652 scopus 로고
    • Thermal stabilization of putative karyoskeletal protein-enriched fractions from Saccharomyces cerevisiae
    • Berrios, S., and Fisher, P.A. (1988) Thermal stabilization of putative karyoskeletal protein-enriched fractions from Saccharomyces cerevisiae. Mol. Cell. Biol., 8:4573-4575.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 4573-4575
    • Berrios, S.1    Fisher, P.A.2
  • 7
    • 0029048816 scopus 로고
    • Colocalization of a high molecular mass phosphoprotein of the nuclear matrix (p255) with spliceosomes
    • Bisotto, S., Lauriault, P., Duval, M., and Vincent, M. (1995) Colocalization of a high molecular mass phosphoprotein of the nuclear matrix (p255) with spliceosomes. J. Cell Sci., 108:1873-1882.
    • (1995) J. Cell Sci. , vol.108 , pp. 1873-1882
    • Bisotto, S.1    Lauriault, P.2    Duval, M.3    Vincent, M.4
  • 8
    • 0025895781 scopus 로고
    • The influence of specimen refractive index, detector signal integration and non-uniform scan speed on the imaging properties in confocal microscopy
    • Carlsson, K. (1991) The influence of specimen refractive index, detector signal integration and non-uniform scan speed on the imaging properties in confocal microscopy. J. Microsc., 163:167-178.
    • (1991) J. Microsc. , vol.163 , pp. 167-178
    • Carlsson, K.1
  • 9
    • 0002638476 scopus 로고
    • The nucleoskeleton: Artifact, passive framework or active site?
    • Cook, P.R. (1988) The nucleoskeleton: artifact, passive framework or active site? J. Cell Sci., 90:1-6.
    • (1988) J. Cell Sci. , vol.90 , pp. 1-6
    • Cook, P.R.1
  • 10
    • 0025863420 scopus 로고
    • The nucleoskeleton and the topology of DNA replication
    • Cook, P.R. (1991) The nucleoskeleton and the topology of DNA replication. Cell, 66:627-635.
    • (1991) Cell , vol.66 , pp. 627-635
    • Cook, P.R.1
  • 11
    • 0022342630 scopus 로고
    • c-myc as a member of a discrete subset of nuclear proteins
    • c-myc as a member of a discrete subset of nuclear proteins. Cell, 43:253-261.
    • (1985) Cell , vol.43 , pp. 253-261
    • Evan, G.I.1    Hancock, D.C.2
  • 12
    • 0023684923 scopus 로고
    • The nuclear matrix protein, numatrin (B23), is associated with growth factor-induced mitogenesis in Swiss 3T3 fibroblasts and with T lymphocyte proliferation stimulated by lectins and anti-T cell receptor antibody
    • Feuerstein, N., Spiegel, S., and Mond, J.J. (1988) The nuclear matrix protein, numatrin (B23), is associated with growth factor-induced mitogenesis in Swiss 3T3 fibroblasts and with T lymphocyte proliferation stimulated by lectins and anti-T cell receptor antibody. J. Cell Biol., 107:1629-1642.
    • (1988) J. Cell Biol. , vol.107 , pp. 1629-1642
    • Feuerstein, N.1    Spiegel, S.2    Mond, J.J.3
  • 13
    • 0023395457 scopus 로고
    • Endogenous polyamines are intimately associated with highly condensed chromatin in vivo. A fluorescence cytochemical and immunocytochemical study of spermine and spermidine during the cell cycle and in reactivated nuclei
    • Hougaard, D.M., Bolund, L., Fujiwara, K., and Larsson, L.I. (1987) Endogenous polyamines are intimately associated with highly condensed chromatin in vivo. A fluorescence cytochemical and immunocytochemical study of spermine and spermidine during the cell cycle and in reactivated nuclei. Eur. J. Cell Biol., 44:151-155.
    • (1987) Eur. J. Cell Biol. , vol.44 , pp. 151-155
    • Hougaard, D.M.1    Bolund, L.2    Fujiwara, K.3    Larsson, L.I.4
  • 14
    • 0023892071 scopus 로고
    • Interaction of DNA with nuclear scaffold in vitro
    • Izuarralde, E., Mirkovitch, J., and Laemmli, U.K. (1988) Interaction of DNA with nuclear scaffold in vitro. J. Mol. Biol., 200:111-125.
    • (1988) J. Mol. Biol. , vol.200 , pp. 111-125
    • Izuarralde, E.1    Mirkovitch, J.2    Laemmli, U.K.3
  • 15
    • 0027499230 scopus 로고
    • Visualization of focal sites of transcription within human nuclei
    • Jackson, D.A., Hassan, B.A., Errington, R.J., and Cook, P.A. (1993) Visualization of focal sites of transcription within human nuclei. EMBO J., 12:1059-1065.
    • (1993) EMBO J. , vol.12 , pp. 1059-1065
    • Jackson, D.A.1    Hassan, B.A.2    Errington, R.J.3    Cook, P.A.4
  • 16
    • 0028308290 scopus 로고
    • Sites in human nuclei where DNA damaged by ultraviolet light is repaired: Visualization and localization relative to the nucleoskeleton
    • Jackson, D.A., Baljee, A.S., Mullenders, L., and Cook, P.R. (1994) Sites in human nuclei where DNA damaged by ultraviolet light is repaired: Visualization and localization relative to the nucleoskeleton. J. Cell Sci., 107:1745-1752.
    • (1994) J. Cell Sci. , vol.107 , pp. 1745-1752
    • Jackson, D.A.1    Baljee, A.S.2    Mullenders, L.3    Cook, P.R.4
  • 17
    • 0025995437 scopus 로고
    • A 210 kDa nuclear matrix protein is a functional part of the mitotic spindle; a microinjection study using SPN monoclonal antibodies
    • Kallajoki, M., Weber, K., and Osborn, M. (1991) A 210 kDa nuclear matrix protein is a functional part of the mitotic spindle; a microinjection study using SPN monoclonal antibodies. EMBO J., 10:3351-3362.
    • (1991) EMBO J. , vol.10 , pp. 3351-3362
    • Kallajoki, M.1    Weber, K.2    Osborn, M.3
  • 18
    • 0021691674 scopus 로고
    • A subset of non-histone nuclear proteins reversibly stabilized by the sulfhydryl cross-linking reagent tetrathionate. Polypeptides of the nuclear matrix
    • Kaufmann, S.H., and Shaper, J.H. (1984) A subset of non-histone nuclear proteins reversibly stabilized by the sulfhydryl cross-linking reagent tetrathionate. Polypeptides of the nuclear matrix. Exp Cell Res., 155:477-495.
    • (1984) Exp Cell Res. , vol.155 , pp. 477-495
    • Kaufmann, S.H.1    Shaper, J.H.2
  • 19
    • 0015583252 scopus 로고
    • Synthetic activity of isolated rat liver nuclei. I. Ultrastructural activity study at various steps of isolation
    • Laval, M., and Bouteille, M. (1973) Synthetic activity of isolated rat liver nuclei. I. Ultrastructural activity study at various steps of isolation. Exp. Cell Res., 76:337-348.
    • (1973) Exp. Cell Res. , vol.76 , pp. 337-348
    • Laval, M.1    Bouteille, M.2
  • 20
    • 20244389811 scopus 로고
    • Characterization of a heat shock-induced insoluble complex in the nuclei of cells
    • Littlewood, T.D., Hancok, B.C., and Evan, G.I. (1987) Characterization of a heat shock-induced insoluble complex in the nuclei of cells. J. Cell Sci., 88:65-72.
    • (1987) J. Cell Sci. , vol.88 , pp. 65-72
    • Littlewood, T.D.1    Hancok, B.C.2    Evan, G.I.3
  • 22
    • 0022539918 scopus 로고
    • Morphometric analysis and topological organization of nuclear matrix in freeze-fractured electron microscopy
    • Maraldi, N.M., Marinelli, F., Cocco, L., Papa, S., Santi, P., and Manzoli, F.A. (1986) Morphometric analysis and topological organization of nuclear matrix in freeze-fractured electron microscopy. Exp. Cell Res., 163:349-362.
    • (1986) Exp. Cell Res. , vol.163 , pp. 349-362
    • Maraldi, N.M.1    Marinelli, F.2    Cocco, L.3    Papa, S.4    Santi, P.5    Manzoli, F.A.6
  • 23
    • 0028179445 scopus 로고
    • 6-iodoacetamidofluorescein labelling to assess the state of sulfhhydryl groups after thermal stabilization of isolated nuclei
    • Martelli, A.M., Neri, L.M., Zamai, L., Bareggi, R., Manzoli, L., and Cocco, L. (1994a) 6-iodoacetamidofluorescein labelling to assess the state of sulfhhydryl groups after thermal stabilization of isolated nuclei. Histochem. J., 26:179-188.
    • (1994) Histochem. J. , vol.26 , pp. 179-188
    • Martelli, A.M.1    Neri, L.M.2    Zamai, L.3    Bareggi, R.4    Manzoli, L.5    Cocco, L.6
  • 24
    • 0028363516 scopus 로고
    • The effect of in vitro heating on the distribution of nuclear matrix polypeptides in HeLa cells
    • Martelli, A.M., Bareggi, R., Riederer, B.M., Marugg, R.A., and Narducci, P. (1994b) The effect of in vitro heating on the distribution of nuclear matrix polypeptides in HeLa cells. Cell Biol. Int., 18:151-158.
    • (1994) Cell Biol. Int. , vol.18 , pp. 151-158
    • Martelli, A.M.1    Bareggi, R.2    Riederer, B.M.3    Marugg, R.A.4    Narducci, P.5
  • 25
    • 0021675784 scopus 로고
    • Organization of the higher-order chromatin loop: Specific DNA attachment sites on nuclear scaffold
    • Mirkovitch, J., Mirault, M.-E., and Laemmli, U.K. (1984) Organization of the higher-order chromatin loop: Specific DNA attachment sites on nuclear scaffold. Cell, 39:223-232.
    • (1984) Cell , vol.39 , pp. 223-232
    • Mirkovitch, J.1    Mirault, M.-E.2    Laemmli, U.K.3
  • 26
    • 0024526184 scopus 로고
    • Mapping replicational sites in the eucaryotic cell nucleus
    • Nakasayu, H., and Berezney, R. (1989) Mapping replicational sites in the eucaryotic cell nucleus. J. Cell Biol., 108:1-11.
    • (1989) J. Cell Biol. , vol.108 , pp. 1-11
    • Nakasayu, H.1    Berezney, R.2
  • 27
    • 0025790440 scopus 로고
    • Identification of the major nuclear matrix proteins
    • Nakasayu, H., and Berezney, R. (1991) Identification of the major nuclear matrix proteins. Proc. Natl. Acad. Sci. U.S.A., 88:10312-10316.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 10312-10316
    • Nakasayu, H.1    Berezney, R.2
  • 28
    • 0026625669 scopus 로고
    • Monoclonal antibodies to human DNA topoisomerase I and the two isoforms of DNA topoisomerase II: 170- and 180-kDa isozymes
    • Negri, C., Chiesa, R., Cerino, A., Bestagno, M., Sala, C., Zini, N., Maraldi, N.M., and Astaldi-Ricotti, G.C.B. (1992) Monoclonal antibodies to human DNA topoisomerase I and the two isoforms of DNA topoisomerase II: 170- and 180-kDa isozymes. Exp. Cell Res., 200:452-459.
    • (1992) Exp. Cell Res. , vol.200 , pp. 452-459
    • Negri, C.1    Chiesa, R.2    Cerino, A.3    Bestagno, M.4    Sala, C.5    Zini, N.6    Maraldi, N.M.7    Astaldi-Ricotti, G.C.B.8
  • 29
    • 0026698242 scopus 로고
    • From two dimensional to three dimensional analysis by confocal microscopy
    • Neri, L.M., Martelli, A.M., Previati, M., Valmori, A., and Capitani, S. (1992) From two dimensional to three dimensional analysis by confocal microscopy. Liver, 12:268-279.
    • (1992) Liver , vol.12 , pp. 268-279
    • Neri, L.M.1    Martelli, A.M.2    Previati, M.3    Valmori, A.4    Capitani, S.5
  • 30
    • 0028360875 scopus 로고
    • In vitro heat exposure induces a redistribution of nuclear matrix proteins in human K562 erythroleukemia cells
    • Neri, L.M., Santi, S., Marugg, R.A., Riederer, B.M., Capitani, S., Cataldi, A., and Martelli, A.M. (1994) In vitro heat exposure induces a redistribution of nuclear matrix proteins in human K562 erythroleukemia cells. Exp. Cell Res., 213:275-285.
    • (1994) Exp. Cell Res. , vol.213 , pp. 275-285
    • Neri, L.M.1    Santi, S.2    Marugg, R.A.3    Riederer, B.M.4    Capitani, S.5    Cataldi, A.6    Martelli, A.M.7
  • 31
    • 0028981064 scopus 로고
    • The effect of sodium tetrathionate stabilization on the distribution of three nuclear matrix proteins in human K562 erythroleukemia cells
    • Neri, L.M., Riederer, B.M., Marugg, R.A., Capitani, S., and Martelli, A.M. (1995) The effect of sodium tetrathionate stabilization on the distribution of three nuclear matrix proteins in human K562 erythroleukemia cells. Histochem. Cell Biol., 104:29-36.
    • (1995) Histochem. Cell Biol. , vol.104 , pp. 29-36
    • Neri, L.M.1    Riederer, B.M.2    Marugg, R.A.3    Capitani, S.4    Martelli, A.M.5
  • 32
    • 0026537584 scopus 로고
    • A normally masked nuclear matrix antigen that appears at mitosis on cytoskeleton filaments adjoining chromosomes, centrioles and midbodies
    • Nickerson, J.A., Krockmalnic, G., Wan, K.M., Turner, C.D., and Penman, S. (1992) A normally masked nuclear matrix antigen that appears at mitosis on cytoskeleton filaments adjoining chromosomes, centrioles and midbodies. J. Cell Biol., 116:977-987.
    • (1992) J. Cell Biol. , vol.116 , pp. 977-987
    • Nickerson, J.A.1    Krockmalnic, G.2    Wan, K.M.3    Turner, C.D.4    Penman, S.5
  • 33
    • 0026672117 scopus 로고
    • Depletion in nuclear spermine during spermatogenesis, a natural process of cell differentiation
    • Quemener, V., Blanchard, Y., Lescoat, D., Havouis, R., and Moulinoux, J.P. (1992) Depletion in nuclear spermine during spermatogenesis, a natural process of cell differentiation. Am. J. Physiol., 263:343-347.
    • (1992) Am. J. Physiol. , vol.263 , pp. 343-347
    • Quemener, V.1    Blanchard, Y.2    Lescoat, D.3    Havouis, R.4    Moulinoux, J.P.5
  • 34
    • 0027397110 scopus 로고
    • Three-dimensional organization of the ribosomal genes and Ag-NOR proteins during interphase and mitosis in PtK cells studied by confocal microscopy
    • Robert-Fortel, I., Junéra, H.R., Géraud, G., and Hernandez-Verdun, D. (1993) Three-dimensional organization of the ribosomal genes and Ag-NOR proteins during interphase and mitosis in PtK cells studied by confocal microscopy. Chromosoma, 102:146-157.
    • (1993) Chromosoma , vol.102 , pp. 146-157
    • Robert-Fortel, I.1    Junéra, H.R.2    Géraud, G.3    Hernandez-Verdun, D.4
  • 35
    • 0022531432 scopus 로고
    • Condensation of chromatin: Role of multivalent cations
    • Sen, D., and Crothers, D.M. (1986) Condensation of chromatin: Role of multivalent cations. Biochemistry, 25:1495-1503.
    • (1986) Biochemistry , vol.25 , pp. 1495-1503
    • Sen, D.1    Crothers, D.M.2
  • 36
    • 0025936626 scopus 로고
    • Associations between distinct pre-mRNA splicing components and the cell nucleus
    • Spector, D.L., Fu, X.-D., and Maniatis, T. (1991) Associations between distinct pre-mRNA splicing components and the cell nucleus. EMBO J., 10:3467-3481.
    • (1991) EMBO J. , vol.10 , pp. 3467-3481
    • Spector, D.L.1    Fu, X.-D.2    Maniatis, T.3
  • 37
    • 0021235767 scopus 로고
    • Preparation of nuclear matrices from cultured cells: Subfractionation of nuclei in situ
    • Staufenbiel, M., and Deppert, W. (1984) Preparation of nuclear matrices from cultured cells: Subfractionation of nuclei in situ. J. Cell Biol., 98:1886-1894.
    • (1984) J. Cell Biol. , vol.98 , pp. 1886-1894
    • Staufenbiel, M.1    Deppert, W.2
  • 39
    • 0028137793 scopus 로고
    • The B1C8 protein is in the dense assemblies of the nuclear matrix and relocates to the spindle and pericentriolar filaments at mitosis
    • Wan, K.M., Nickerson, J.A., Krockmalnic, G., and Penman, S. (1994) The B1C8 protein is in the dense assemblies of the nuclear matrix and relocates to the spindle and pericentriolar filaments at mitosis. Proc. Natl. Acad. Sci. U.S.A., 91:594-598.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 594-598
    • Wan, K.M.1    Nickerson, J.A.2    Krockmalnic, G.3    Penman, S.4
  • 40
    • 0028243081 scopus 로고
    • RNA polymerase II transcription is concentrated outside replication domains throughout S-phase
    • Wansink, D.G., Manders, E.E.M., van der Kraan, I., Aten, J.A., van Driel, R., and de Jong, L. (1994) RNA polymerase II transcription is concentrated outside replication domains throughout S-phase. J. Cell Sci., 107:1449-1456.
    • (1994) J. Cell Sci. , vol.107 , pp. 1449-1456
    • Wansink, D.G.1    Manders, E.E.M.2    Van Der Kraan, I.3    Aten, J.A.4    Van Driel, R.5    De Jong, L.6
  • 41
    • 0028600629 scopus 로고
    • Localization of pre-mRNA splicing in mammalian nuclei
    • Zhang, G., Taneja, K.L., Siger, R.H., and Green, M.R. (1994) Localization of pre-mRNA splicing in mammalian nuclei. Nature, 372:809-812.
    • (1994) Nature , vol.372 , pp. 809-812
    • Zhang, G.1    Taneja, K.L.2    Siger, R.H.3    Green, M.R.4
  • 42
    • 0026694667 scopus 로고
    • The 180-kDa isoform of topoisomerase II is localized in the nucleolus and belongs to the structural elements of the nucleolar remnant
    • Zini, N., Martelli, A.M., Sabatelli, P., Santi, S., Negri, C., Astaldi-Ricotti, G.C.B., and Maraldi, N.M. (1992) The 180-kDa isoform of topoisomerase II is localized in the nucleolus and belongs to the structural elements of the nucleolar remnant. Exp. Cell Res., 200:460-466.
    • (1992) Exp. Cell Res. , vol.200 , pp. 460-466
    • Zini, N.1    Martelli, A.M.2    Sabatelli, P.3    Santi, S.4    Negri, C.5    Astaldi-Ricotti, G.C.B.6    Maraldi, N.M.7


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