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Volumn 139, Issue 4, 1997, Pages 963-973

Microtubule stabilization in pressure overload cardiac hypertrophy

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA TUBULIN; MICROTUBULE ASSOCIATED PROTEIN;

EID: 0030697290     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.139.4.963     Document Type: Article
Times cited : (97)

References (55)
  • 1
    • 0025035790 scopus 로고
    • Molecular cloning of a ubiquitously distributed microtubule-associated protein with Mr 190,000
    • Aizawa, H., Y. Emori, H. Murofushi, H. Kawasaki, H. Sakai, and K. Suzuki. 1990. Molecular cloning of a ubiquitously distributed microtubule-associated protein with Mr 190,000. J. Biol. Chem. 265:13849-13855.
    • (1990) J. Biol. Chem. , vol.265 , pp. 13849-13855
    • Aizawa, H.1    Emori, Y.2    Murofushi, H.3    Kawasaki, H.4    Sakai, H.5    Suzuki, K.6
  • 2
    • 0025775640 scopus 로고
    • Functional analysis of the domain structure of microtubule-associated protein-4 (MAP-U)
    • Aizawa, H., Y. Emori, A. Mori, H. Murofushi, H. Sakai, and K. Suzuki. 1991. Functional analysis of the domain structure of microtubule-associated protein-4 (MAP-U). J. Biol. Chem. 266:9841-9846.
    • (1991) J. Biol. Chem. , vol.266 , pp. 9841-9846
    • Aizawa, H.1    Emori, Y.2    Mori, A.3    Murofushi, H.4    Sakai, H.5    Suzuki, K.6
  • 3
    • 0027410644 scopus 로고
    • Tyrosinatable and non-tyrosinatable tubulin subpopulations in rat muscle in comparison with those in brain
    • Alonso, A. del C., Arce, C.A., Barra, H.S. 1993. Tyrosinatable and non-tyrosinatable tubulin subpopulations in rat muscle in comparison with those in brain. Biochim. Biophys. Acta. 1163:26-30.
    • (1993) Biochim. Biophys. Acta , vol.1163 , pp. 26-30
    • Alonso, A.D.C.1    Arce, C.A.2    Barra, H.S.3
  • 4
    • 0028294997 scopus 로고
    • Deconstructing the microtubule-organizing center
    • Archer, J., and F. Solomon. 1994. Deconstructing the microtubule-organizing center. Cell. 76:589-591.
    • (1994) Cell , vol.76 , pp. 589-591
    • Archer, J.1    Solomon, F.2
  • 5
    • 0026758423 scopus 로고
    • γ-tubulin distribution in the neuron: Implications for the origins of neuritic microtubules
    • Baas, P.W., and H.C. Joshi. 1992. γ-tubulin distribution in the neuron: Implications for the origins of neuritic microtubules. J. Cell Biol. 119:171-178.
    • (1992) J. Cell Biol. , vol.119 , pp. 171-178
    • Baas, P.W.1    Joshi, H.C.2
  • 6
    • 0028037828 scopus 로고
    • Stable expression of heterologous microtubule-associated proteins (MAPs) in Chinese hamster ovary cells: Evidence for differing roles of MAPs in microtubule organization
    • Barlow, S., M.L. Gonzalez-Garay, R.R. West, J.B. Olmsted, and F. Cabral. 1994. Stable expression of heterologous microtubule-associated proteins (MAPs) in Chinese hamster ovary cells: evidence for differing roles of MAPs in microtubule organization. J. Cell Biol. 126:1017-1029.
    • (1994) J. Cell Biol. , vol.126 , pp. 1017-1029
    • Barlow, S.1    Gonzalez-Garay, M.L.2    West, R.R.3    Olmsted, J.B.4    Cabral, F.5
  • 8
    • 0016587144 scopus 로고
    • Purification of tubulin and associated high molecular weight proteins from porcine brain and characterization of microtubule assembly in vitro
    • Borisy, G.G., J.M. Marcum, J.B. Olmsted, D.B. Murphy, and K.A. Johnson. 1975. Purification of tubulin and associated high molecular weight proteins from porcine brain and characterization of microtubule assembly in vitro. Ann. NY Acad. Sci. 253:107-132.
    • (1975) Ann. NY Acad. Sci. , vol.253 , pp. 107-132
    • Borisy, G.G.1    Marcum, J.M.2    Olmsted, J.B.3    Murphy, D.B.4    Johnson, K.A.5
  • 9
    • 0013576148 scopus 로고
    • Self-assembly of microtubules in extracts of cultured HeLa cells and identification of HeLa microtubule-associated proteins
    • Bulinski, J.C., and G.G. Borisy. 1979. Self-assembly of microtubules in extracts of cultured HeLa cells and identification of HeLa microtubule-associated proteins. Proc. Natl. Acad. Sci. USA. 76:293-297.
    • (1979) Proc. Natl. Acad. Sci. USA. , vol.76 , pp. 293-297
    • Bulinski, J.C.1    Borisy, G.G.2
  • 10
    • 0019171148 scopus 로고
    • Microtubule-associated proteins from cultured HeLa cells: Analysis of molecular properties and effects on microtubule polymerization
    • Bulinski, J.C., and G.G. Borisy. 1980. Microtubule-associated proteins from cultured HeLa cells: Analysis of molecular properties and effects on microtubule polymerization. J. Biol. Chem. 255:11570-11576.
    • (1980) J. Biol. Chem. , vol.255 , pp. 11570-11576
    • Bulinski, J.C.1    Borisy, G.G.2
  • 11
    • 0026181461 scopus 로고
    • Stabilization of post-translational modification of microtubules during cellular morphogenesis
    • Bulinski, J.C., and G.G. Gundersen. 1991. Stabilization of post-translational modification of microtubules during cellular morphogenesis. Bioessays. 13: 285-293.
    • (1991) Bioessays , vol.13 , pp. 285-293
    • Bulinski, J.C.1    Gundersen, G.G.2
  • 12
    • 0023313208 scopus 로고
    • The multitubulin hypothesis revisited: What have we learned?
    • Cleveland, D.W. 1987. The multitubulin hypothesis revisited: what have we learned? J. Cell Biol. 104:381-383.
    • (1987) J. Cell Biol. , vol.104 , pp. 381-383
    • Cleveland, D.W.1
  • 13
    • 0015581364 scopus 로고
    • Normal myocardial function and energetics in volume overload hypertrophy in the cat
    • Cooper, G., F.J. Puga, K.J. Zujko, C.E. Harrison, and H.N. Coleman. 1973a. Normal myocardial function and energetics in volume overload hypertrophy in the cat. Circ. Res. 32:140-148.
    • (1973) Circ. Res. , vol.32 , pp. 140-148
    • Cooper, G.1    Puga, F.J.2    Zujko, K.J.3    Harrison, C.E.4    Coleman, H.N.5
  • 14
    • 0015693837 scopus 로고
    • Mechanism for the abnormal energetics of pressure-induced hypertrophy of cat myocardium
    • Cooper, G., R.M. Satava, C.E. Harrison, and H.N. Coleman. 1973b. Mechanism for the abnormal energetics of pressure-induced hypertrophy of cat myocardium. Circ. Res. 33:213-223.
    • (1973) Circ. Res. , vol.33 , pp. 213-223
    • Cooper, G.1    Satava, R.M.2    Harrison, C.E.3    Coleman, H.N.4
  • 15
  • 16
    • 0021752265 scopus 로고
    • Distinct populations of microtubules: Tyrosinated and non-tyrosinated α-tubulin are distributed differently in vivo
    • Gundersen, G.G., M.H. Kalnoski, and J.C. Bulinski. 1984. Distinct populations of microtubules: Tyrosinated and non-tyrosinated α-tubulin are distributed differently in vivo. Cell. 38:779-789.
    • (1984) Cell , vol.38 , pp. 779-789
    • Gundersen, G.G.1    Kalnoski, M.H.2    Bulinski, J.C.3
  • 17
    • 0024453421 scopus 로고
    • Generation of a stable, posttranslationally modified microtubule array is an early event in myogenic differentiaiton
    • Gundersen, G.G., S. Khawaja, and J.C. Bulinski. 1989. Generation of a stable, posttranslationally modified microtubule array is an early event in myogenic differentiaiton. J. Cell Biol. 109:2275-2288.
    • (1989) J. Cell Biol. , vol.109 , pp. 2275-2288
    • Gundersen, G.G.1    Khawaja, S.2    Bulinski, J.C.3
  • 18
    • 0020334993 scopus 로고
    • Bioenergetics and kinetics of microtubule and actin filament assembly-disassembly
    • Hill, T.L., and M.W. Kirschner. 1982. Bioenergetics and kinetics of microtubule and actin filament assembly-disassembly. Int. Rev. Cytol. 78:1-125.
    • (1982) Int. Rev. Cytol. , vol.78 , pp. 1-125
    • Hill, T.L.1    Kirschner, M.W.2
  • 19
    • 0022198218 scopus 로고
    • Tension and compression in the cytoskeleton of PC 12 neurites
    • Joshi, H.C., D. Chu, R.E. Buxbaum, and S.R. Heidemann. 1985. Tension and compression in the cytoskeleton of PC 12 neurites. J. Cell Biol. 101:697-705.
    • (1985) J. Cell Biol. , vol.101 , pp. 697-705
    • Joshi, H.C.1    Chu, D.2    Buxbaum, R.E.3    Heidemann, S.R.4
  • 20
    • 0026538817 scopus 로고
    • γ-tubulin is a centrosomal protein required for cell cycle-dependent microtubule nucleation
    • Joshi, H.C., M.J. Palacios, L. McNamara, and D.W. Cleveland. 1992. γ-tubulin is a centrosomal protein required for cell cycle-dependent microtubule nucleation. Nature. 356:80-83.
    • (1992) Nature , vol.356 , pp. 80-83
    • Joshi, H.C.1    Palacios, M.J.2    McNamara, L.3    Cleveland, D.W.4
  • 22
    • 0023896761 scopus 로고
    • Isolation of rat liver microtubule-associated proteins: Evidence for a family of microtubule-associated proteins with molecular mass of around 200,000 which distribute widely among mammalian cells
    • Kotani, S., H. Murofushi, S. Maekawa, H. Aizawa, and H. Sakai. 1988. Isolation of rat liver microtubule-associated proteins: evidence for a family of microtubule-associated proteins with molecular mass of around 200,000 which distribute widely among mammalian cells. J. Biol. Chem. 263:5385-5389.
    • (1988) J. Biol. Chem. , vol.263 , pp. 5385-5389
    • Kotani, S.1    Murofushi, H.2    Maekawa, S.3    Aizawa, H.4    Sakai, H.5
  • 23
    • 0023395003 scopus 로고
    • The microtubule-organizing complex and the Golgi apparatus are co-localized around the entire nuclear envelope of interphase cardiac myocytes
    • Kronebusch, P.J., and S.J. Singer. 1987. The microtubule-organizing complex and the Golgi apparatus are co-localized around the entire nuclear envelope of interphase cardiac myocytes. J. Cell Sci. 88:25-34.
    • (1987) J. Cell Sci. , vol.88 , pp. 25-34
    • Kronebusch, P.J.1    Singer, S.J.2
  • 24
    • 0023662301 scopus 로고
    • Free intermingling of mammalian β-tubulin isotypes among functionally distinct microtubules
    • Lewis, S.A., W. Gu, and N.J. Cowan. 1987. Free intermingling of mammalian β-tubulin isotypes among functionally distinct microtubules. Cell. 49:539-548.
    • (1987) Cell , vol.49 , pp. 539-548
    • Lewis, S.A.1    Gu, W.2    Cowan, N.J.3
  • 25
    • 0027207944 scopus 로고
    • Are tubulin isotypes functionally significant?
    • Ludueña, R.F. 1993. Are tubulin isotypes functionally significant? Mol. Biol. Cell. 4:445-457.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 445-457
    • Ludueña, R.F.1
  • 26
    • 0024041251 scopus 로고
    • Differential interaction of synthetic peptides from the carboxy-terminal regulatory domain of tubulin with microtubule-associated proteins
    • Maccioni, R.B., C.I. Rivas, and J.C. Vera. 1988. Differential interaction of synthetic peptides from the carboxy-terminal regulatory domain of tubulin with microtubule-associated proteins. EMBO (Eur. Mol. Biol. Organ.) J. 7:1957-1963.
    • (1988) EMBO (Eur. Mol. Biol. Organ.) J. , vol.7 , pp. 1957-1963
    • Maccioni, R.B.1    Rivas, C.I.2    Vera, J.C.3
  • 27
    • 0030008156 scopus 로고    scopus 로고
    • A muscle-specific variant of microtubule-associated protein 4 (MAP 4) is required in myogenesis
    • Mangan, M.E., and J.B. Olmsted. 1996. A muscle-specific variant of microtubule-associated protein 4 (MAP 4) is required in myogenesis. Development. 122:771-781.
    • (1996) Development , vol.122 , pp. 771-781
    • Mangan, M.E.1    Olmsted, J.B.2
  • 28
    • 0024409475 scopus 로고
    • Load regulation of the properties of adult feline cardiocytes: Growth induction by cellular deformation
    • Mann, D.L., R.L. Kent, and G. Cooper. 1989. Load regulation of the properties of adult feline cardiocytes: Growth induction by cellular deformation. Circ. Res. 64:1079-1090.
    • (1989) Circ. Res. , vol.64 , pp. 1079-1090
    • Mann, D.L.1    Kent, R.L.2    Cooper, G.3
  • 29
    • 0026035329 scopus 로고
    • Cellular versus myocardial basis for the contractile dysfunction of hypertrophied myocardium
    • Mann, D.L., Y. Urabe, R.L. Kent, S. Vinciguerra, and G. Cooper. 1991. Cellular versus myocardial basis for the contractile dysfunction of hypertrophied myocardium. Circ. Res. 68:402-415.
    • (1991) Circ. Res. , vol.68 , pp. 402-415
    • Mann, D.L.1    Urabe, Y.2    Kent, R.L.3    Vinciguerra, S.4    Cooper, G.5
  • 30
    • 0025760492 scopus 로고
    • Transcriptional regulation of ribosomal RNA synthesis during growth of cardiac myocytes in culture
    • McDermott, P.J., L.L. Carl, K.J. Conner, and S.N. Allo. 1991. Transcriptional regulation of ribosomal RNA synthesis during growth of cardiac myocytes in culture. J. Biol. Chem. 266:4409-4416.
    • (1991) J. Biol. Chem. , vol.266 , pp. 4409-4416
    • McDermott, P.J.1    Carl, L.L.2    Conner, K.J.3    Allo, S.N.4
  • 31
    • 0027424297 scopus 로고
    • Identification of katanin, an ATPase that severs and disassembles stable microtubules
    • McNally, F.J., and R.D. Vale. 1993. Identification of katanin, an ATPase that severs and disassembles stable microtubules. Cell. 75:419-429.
    • (1993) Cell , vol.75 , pp. 419-429
    • McNally, F.J.1    Vale, R.D.2
  • 32
    • 0028140113 scopus 로고
    • Coordinate regulation of tubulin and microtubule-associated protein genes during development of hamster brain
    • Oblinger, M.M., and S.A. Kost. 1994. Coordinate regulation of tubulin and microtubule-associated protein genes during development of hamster brain. Dev. Brain Res. 77:45-54.
    • (1994) Dev. Brain Res. , vol.77 , pp. 45-54
    • Oblinger, M.M.1    Kost, S.A.2
  • 33
    • 0022850973 scopus 로고
    • Microtubule-associated proteins
    • Olmsted, J.B. 1986. Microtubule-associated proteins. Annu. Rev. Cell Biol. 2: 421-457.
    • (1986) Annu. Rev. Cell Biol. , vol.2 , pp. 421-457
    • Olmsted, J.B.1
  • 34
    • 0018362186 scopus 로고
    • Biochemical determination of tubulin-microtubule equilibrium in cultured cells
    • Ostlund, R.E., J.T. Leung, and S.V. Hajek. 1979. Biochemical determination of tubulin-microtubule equilibrium in cultured cells. Anal. Biochem. 96:155-164.
    • (1979) Anal. Biochem. , vol.96 , pp. 155-164
    • Ostlund, R.E.1    Leung, J.T.2    Hajek, S.V.3
  • 36
    • 0024583552 scopus 로고
    • Complete separation of tyrosinated, detyrosinated, and nontyrosinatable brain tubulin subpopulations using affinity chromatography
    • Paturle, L., J. Wehland, R.L. Margolis, and D. Job. 1989. Complete separation of tyrosinated, detyrosinated, and nontyrosinatable brain tubulin subpopulations using affinity chromatography. Biochemistry. 28:2698-2704.
    • (1989) Biochemistry , vol.28 , pp. 2698-2704
    • Paturle, L.1    Wehland, J.2    Margolis, R.L.3    Job, D.4
  • 38
    • 0028283568 scopus 로고
    • Accumulation of Δ2-tubulin, a major tubulin variant that cannot be tyrosinated, in neuronal tissues and in stable microtubule assemblies
    • Paturle-Lafanechère, L., M. Manier, N. Trigault, F. Pirollet, H. Mazarguil, and D. Job. 1994. Accumulation of Δ2-tubulin, a major tubulin variant that cannot be tyrosinated, in neuronal tissues and in stable microtubule assemblies. J. Cell Sci. 107:1529-1543.
    • (1994) J. Cell Sci. , vol.107 , pp. 1529-1543
    • Paturle-Lafanechère, L.1    Manier, M.2    Trigault, N.3    Pirollet, F.4    Mazarguil, H.5    Job, D.6
  • 39
    • 0016760652 scopus 로고
    • An enzyme tyrosylating α-tubulin and its role in microtubule assembly
    • Raybin, D., and M. Flavin. 1975. An enzyme tyrosylating α-tubulin and its role in microtubule assembly. Biochem. Biophphvs. Res. Commun. 65:1088-1095.
    • (1975) Biochem. Biophphvs. Res. Commun. , vol.65 , pp. 1088-1095
    • Raybin, D.1    Flavin, M.2
  • 41
    • 0028328735 scopus 로고
    • Centrin plays an essential role in microtubule severing during flagellar excision in Chlamydomonas reinhardtii
    • Sanders, M.A., and J.L. Salisbury. 1994. Centrin plays an essential role in microtubule severing during flagellar excision in Chlamydomonas reinhardtii. J. Cell Biol. 124:795-805.
    • (1994) J. Cell Biol. , vol.124 , pp. 795-805
    • Sanders, M.A.1    Salisbury, J.L.2
  • 42
    • 0019585912 scopus 로고
    • Stabilization of the cytoplasmic ground substance in detergent-opened cells and a structural and biochemical analysis of its composition
    • Schliwa, M., J. van Blerkom, and K.R. Porter. 1981. Stabilization of the cytoplasmic ground substance in detergent-opened cells and a structural and biochemical analysis of its composition. Proc. Natl. Acad. Sci. USA. 78:4329-4333.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 4329-4333
    • Schliwa, M.1    Van Blerkom, J.2    Porter, K.R.3
  • 43
    • 0023292950 scopus 로고
    • Dynamic and stable populations of microtubules in cells
    • Schulze, E., and M.W. Kirschner. 1987. Dynamic and stable populations of microtubules in cells. J. Cell Biol. 104:277-288.
    • (1987) J. Cell Biol. , vol.104 , pp. 277-288
    • Schulze, E.1    Kirschner, M.W.2
  • 45
    • 0029043037 scopus 로고
    • Microtubule-severing activity in M phase
    • Shiina, N., Y. Gotoh, and E. Nishida. 1995. Microtubule-severing activity in M phase. Trends Cell Biol. 5:283-286.
    • (1995) Trends Cell Biol. , vol.5 , pp. 283-286
    • Shiina, N.1    Gotoh, Y.2    Nishida, E.3
  • 48
    • 0018758372 scopus 로고
    • Intact microtubules are required for rapid turnover of carboxyl-terminal tyrosine of α-tubulin in cell cultures
    • Thompson, W.C., G.G. Deanin, and M.W. Gordon. 1979. Intact microtubules are required for rapid turnover of carboxyl-terminal tyrosine of α-tubulin in cell cultures. Proc. Natl. Acad. Sci. USA. 76:1318-1322.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 1318-1322
    • Thompson, W.C.1    Deanin, G.G.2    Gordon, M.W.3
  • 49
    • 0027196279 scopus 로고
    • Cytoskeletal role in the contractile dysfunction of hypertrophied myocardium
    • Tsutsui, H., K. Ishihara, and G. Cooper. 1993. Cytoskeletal role in the contractile dysfunction of hypertrophied myocardium. Science. 260:682-687.
    • (1993) Science , vol.260 , pp. 682-687
    • Tsutsui, H.1    Ishihara, K.2    Cooper, G.3
  • 51
    • 0011214518 scopus 로고    scopus 로고
    • Removal of MAP 4 from microtubules in vivo produces no observable phenotype at the cellular level
    • Wang, X.M., J.G. Peloquin, Y. Zhai, J.C. Bulinski, and G.G. Borisy. 1996. Removal of MAP 4 from microtubules in vivo produces no observable phenotype at the cellular level. J. Cell Biol. 132:345-357.
    • (1996) J. Cell Biol. , vol.132 , pp. 345-357
    • Wang, X.M.1    Peloquin, J.G.2    Zhai, Y.3    Bulinski, J.C.4    Borisy, G.G.5
  • 52
    • 0025294639 scopus 로고
    • Detyrosination of α-tubulin does not stabilize microtubules in vivo
    • Webster, D.R., J. Wehland, K. Weber, and G.G. Borisy. 1990. Detyrosination of α-tubulin does not stabilize microtubules in vivo. J. Cell Biol. 111:113-122.
    • (1990) J. Cell Biol. , vol.111 , pp. 113-122
    • Webster, D.R.1    Wehland, J.2    Weber, K.3    Borisy, G.G.4
  • 53
    • 0023195188 scopus 로고
    • Tubulin-tyrosine ligase has a binding site on β-tubulin: A two-domain structure of the enzyme
    • Wehland, J., and K. Weber. 1987a. Tubulin-tyrosine ligase has a binding site on β-tubulin: a two-domain structure of the enzyme. J. Cell Biol. 104:1059-1067.
    • (1987) J. Cell Biol. , vol.104 , pp. 1059-1067
    • Wehland, J.1    Weber, K.2
  • 54
    • 0023406178 scopus 로고
    • Turnover of the carboxy-terminal tyrosine of α-tubulin and means of reaching elevated levels of detyrosination in living cells
    • Wehland, J., and K. Weber. 1987b. Turnover of the carboxy-terminal tyrosine of α-tubulin and means of reaching elevated levels of detyrosination in living cells. J. Cell Sci. 88:185-203.
    • (1987) J. Cell Sci. , vol.88 , pp. 185-203
    • Wehland, J.1    Weber, K.2
  • 55
    • 0025837142 scopus 로고
    • A model for microtubule-associated protein 4 structure: Domains defined by comparisons of human, mouse, and bovine sequences
    • West, R.R., K.M. Tenbarge, and J.B. Olmsted. 1991. A model for microtubule-associated protein 4 structure: domains defined by comparisons of human, mouse, and bovine sequences. J. Biol. Chem. 266:21886-21896.
    • (1991) J. Biol. Chem. , vol.266 , pp. 21886-21896
    • West, R.R.1    Tenbarge, K.M.2    Olmsted, J.B.3


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