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Volumn 59, Issue 12, 2002, Pages 2216-2223

Isoforms of soluble α-tubulin in oocytes and brain of the frog (genus Rana): Changes during oocyte maturation

Author keywords

DM1A; Isoelectric focusing; Microtubule; SDS PAGE; Species specificity; Two dimensional electrophoresis

Indexed keywords

ALPHA TUBULIN; MONOCLONAL ANTIBODY; OLIGOMER; PROGESTERONE;

EID: 0036967327     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s000180200021     Document Type: Article
Times cited : (7)

References (39)
  • 1
    • 0026569828 scopus 로고
    • Microtubule functions
    • Avila J. (1991) Microtubule functions. Life Sci. 50: 327-334
    • (1991) Life Sci. , vol.50 , pp. 327-334
    • Avila, J.1
  • 2
    • 0021686169 scopus 로고
    • Dynamic instability of microtubule growth
    • Mitchison T. J. and Kirschner M. W. (1984) Dynamic instability of microtubule growth. Nature 312: 237-242
    • (1984) Nature , vol.312 , pp. 237-242
    • Mitchison, T.J.1    Kirschner, M.W.2
  • 4
    • 0025754855 scopus 로고
    • Functions of tubulin isoforms
    • Murphy D. B. (1991) Functions of tubulin isoforms. Curr. Opin. Cell Biol. 3: 43-51
    • (1991) Curr. Opin. Cell Biol. , vol.3 , pp. 43-51
    • Murphy, D.B.1
  • 5
    • 0027207944 scopus 로고
    • Are tubulin isotypes functionally significant
    • Luduena R. F. (1993) Are tubulin isotypes functionally significant. Mol. Biol. Cell 4: 445-457
    • (1993) Mol. Biol. Cell , vol.4 , pp. 445-457
    • Luduena, R.F.1
  • 6
    • 0022814974 scopus 로고
    • Two functional α-tubulin genes of the yeast Saccharomyces cerevisiae encode divergent proteins
    • Schatz P. J., Pillus L., Grisafi P., Solomon F. and Botstein D. (1986) Two functional α-tubulin genes of the yeast Saccharomyces cerevisiae encode divergent proteins. Mol. Cell Biol. 6: 3711-3721
    • (1986) Mol. Cell Biol. , vol.6 , pp. 3711-3721
    • Schatz, P.J.1    Pillus, L.2    Grisafi, P.3    Solomon, F.4    Botstein, D.5
  • 7
    • 0023425413 scopus 로고
    • In vivo microtubules are copolymers of available β-tubulin isotypes: Localization of each of six vertebrate β-tubulin isotypes using polyclonal antibodies elicited by synthetic peptide antigens
    • Lopata M. A. and Cleveland D. W. (1987) In vivo microtubules are copolymers of available β-tubulin isotypes: localization of each of six vertebrate β-tubulin isotypes using polyclonal antibodies elicited by synthetic peptide antigens. J. Cell Biol. 105: 1707-1720
    • (1987) J. Cell Biol. , vol.105 , pp. 1707-1720
    • Lopata, M.A.1    Cleveland, D.W.2
  • 8
    • 18844475127 scopus 로고
    • Microtubules are acetylated in domains that turn over slowly
    • Webster D. R. and Borisy G. G. (1989) Microtubules are acetylated in domains that turn over slowly. J. Cell Sci. 92: 57-65
    • (1989) J. Cell Sci. , vol.92 , pp. 57-65
    • Webster, D.R.1    Borisy, G.G.2
  • 9
    • 0025153022 scopus 로고
    • Two Drosophila beta tubulin isoforms are not functionally equivalent
    • Hoyle H. D. and Raff E. C. (1990) Two Drosophila beta tubulin isoforms are not functionally equivalent. J. Cell Biol. 111: 1009-1026
    • (1990) J. Cell Biol. , vol.111 , pp. 1009-1026
    • Hoyle, H.D.1    Raff, E.C.2
  • 11
    • 0027753345 scopus 로고
    • Posttranslational modifications and assembly characteristics of goldfish tubulin
    • Lessman C. A., Zhang J. and MacRae T. H. (1993) Posttranslational modifications and assembly characteristics of goldfish tubulin. Biol. Cell 79: 63-70
    • (1993) Biol. Cell , vol.79 , pp. 63-70
    • Lessman, C.A.1    Zhang, J.2    MacRae, T.H.3
  • 12
    • 0030066248 scopus 로고
    • Confocal immunofluorescence microscopy of microtubules, microtubule-associated proteins, and microtubule-organizing centers during amphibian oogenesis and early development
    • Gard D. L., Cha B. J. and Schroeder M. M. (1995) Confocal immunofluorescence microscopy of microtubules, microtubule-associated proteins, and microtubule-organizing centers during amphibian oogenesis and early development. Curr. Top. Dev. Biol. 31: 383-432
    • (1995) Curr. Top. Dev. Biol. , vol.31 , pp. 383-432
    • Gard, D.L.1    Cha, B.J.2    Schroeder, M.M.3
  • 13
    • 0024094432 scopus 로고
    • Dynamic instability of individual microtubules analyzed by video light microscopy: Rate constants and transition frequencies
    • Walker R. A., O'Brien E. T., Pryer N. K., Fagen A. P. and Williams R. C. (1988) Dynamic instability of individual microtubules analyzed by video light microscopy: rate constants and transition frequencies. J. Cell Biol. 107: 1437-1448
    • (1988) J. Cell Biol. , vol.107 , pp. 1437-1448
    • Walker, R.A.1    O'Brien, E.T.2    Pryer, N.K.3    Fagen, A.P.4    Williams, R.C.5
  • 14
    • 0002195603 scopus 로고
    • Microtubule stabilization
    • Hyams J. S. and Lloyd C. W. (eds), Wiley-Liss, New York
    • Margolis R. L. and Job D. (1994) Microtubule stabilization. In: Microtubules, pp. 221-228, Hyams J. S. and Lloyd C. W. (eds), Wiley-Liss, New York
    • (1994) Microtubules , pp. 221-228
    • Margolis, R.L.1    Job, D.2
  • 15
    • 0030060174 scopus 로고    scopus 로고
    • Modulation of microtubule dynamics during the cell cycle
    • McNally F. J. (1996) Modulation of microtubule dynamics during the cell cycle. Curr. Opin. Cell Biol. 8: 23-29
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 23-29
    • McNally, F.J.1
  • 17
    • 0027530407 scopus 로고
    • Taxol induced assembly of brain and testis tubulins, and ovarian follicle tubulin dynamics in the frog (genus Rana), in vitro
    • Lessman C. A. (1993) Taxol induced assembly of brain and testis tubulins, and ovarian follicle tubulin dynamics in the frog (genus Rana), in vitro. Comp. Biochem. Physiol. 104B: 155-162
    • (1993) Comp. Biochem. Physiol. , vol.104 B , pp. 155-162
    • Lessman, C.A.1
  • 18
    • 0031438817 scopus 로고    scopus 로고
    • The major soluble tubulins are found in mega Dalton (MDa) fractions in fully-grown oocytes and eggs but not in brain of the frog, Rana pipiens
    • Wang T. and Lessman C. A. (1997) The major soluble tubulins are found in mega Dalton (MDa) fractions in fully-grown oocytes and eggs but not in brain of the frog, Rana pipiens. Comp. Biochem. Physiol. 118B: 421-430
    • (1997) Comp. Biochem. Physiol. , vol.118 B , pp. 421-430
    • Wang, T.1    Lessman, C.A.2
  • 19
    • 0021230027 scopus 로고
    • Cytoplasmic microtubules of normal and tumor cells of the leopard frog - Temperature effects
    • McKinnell R. C., De Bruyne G. K., Mareel M. M., Tarin D. and Tweedell K. S. (1984) Cytoplasmic microtubules of normal and tumor cells of the leopard frog - temperature effects. Differentiation 26: 231-234
    • (1984) Differentiation , vol.26 , pp. 231-234
    • McKinnell, R.C.1    De Bruyne, G.K.2    Mareel, M.M.3    Tarin, D.4    Tweedell, K.S.5
  • 20
    • 0012842167 scopus 로고
    • Developmental regulation of cold-stable microtubules (MTs) during oogenesis in Rana pipiens
    • Wang T., Lessman C. A. and Gard D. L. (1993) Developmental regulation of cold-stable microtubules (MTs) during oogenesis in Rana pipiens. Mol. Biol. Cell 4: 26a
    • (1993) Mol. Biol. Cell , vol.4
    • Wang, T.1    Lessman, C.A.2    Gard, D.L.3
  • 21
    • 0034897404 scopus 로고    scopus 로고
    • Soluble tubulin complexes in oocytes of the common leopard frog, Rana pipiens, contain γ-tubulin
    • Lessman C. A. and Kim H. (2001) Soluble tubulin complexes in oocytes of the common leopard frog, Rana pipiens, contain γ-tubulin. Mol. Reprod. Dev. 60:128-136
    • (2001) Mol. Reprod. Dev. , vol.60 , pp. 128-136
    • Lessman, C.A.1    Kim, H.2
  • 22
    • 0000171784 scopus 로고    scopus 로고
    • Oogenesis in non-mammalian vertebrates
    • Knobil E. and Neill J. D. (eds), Academic Press, New York
    • Lessman C. A. (1999) Oogenesis in non-mammalian vertebrates. In: Encyclopedia of Reproduction, vol. 3, pp. 498-508, Knobil E. and Neill J. D. (eds), Academic Press, New York
    • (1999) Encyclopedia of Reproduction , vol.3 , pp. 498-508
    • Lessman, C.A.1
  • 23
    • 0033117826 scopus 로고    scopus 로고
    • γ-Tubulin complexes and their interaction with microtubule-organizing centers
    • Wiese C. and Zheng Y. (1999) γ-Tubulin complexes and their interaction with microtubule-organizing centers. Curr. Opin. Struct. Biol. 9: 250-259
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 250-259
    • Wiese, C.1    Zheng, Y.2
  • 24
    • 0023053369 scopus 로고
    • Carboxy-terminal regions on the surface of tubulin and microtubules: Epitope locations of YOL1/34, DM1A and DM1B
    • Breitling F. and Little M. (1986) Carboxy-terminal regions on the surface of tubulin and microtubules: epitope locations of YOL1/34, DM1A and DM1B. J. Mol. Biol. 189: 367-370
    • (1986) J. Mol. Biol. , vol.189 , pp. 367-370
    • Breitling, F.1    Little, M.2
  • 26
    • 0031064639 scopus 로고    scopus 로고
    • Microinjection of anti-α-tubulin antibody (DM1A) inhibits progesterone-induced meiotic maturation and deranges the microtubule array in follicle-enclosed oocytes of the frog, Rana pipiens
    • Lessman C. A., Gard D. L., Wang T. and Woods C. W. (1997) Microinjection of anti-α-tubulin antibody (DM1A) inhibits progesterone-induced meiotic maturation and deranges the microtubule array in follicle-enclosed oocytes of the frog, Rana pipiens. Zygote 5: 83-95
    • (1997) Zygote , vol.5 , pp. 83-95
    • Lessman, C.A.1    Gard, D.L.2    Wang, T.3    Woods, C.W.4
  • 28
    • 0020322766 scopus 로고
    • Role of the surface epithelium and follicle wall in ovulation and progesterone production by frog (Rana pipiens) follicles
    • Schuetz A. W. and Lessman C. A. (1982) Role of the surface epithelium and follicle wall in ovulation and progesterone production by frog (Rana pipiens) follicles. Differentiation 22: 79-84
    • (1982) Differentiation , vol.22 , pp. 79-84
    • Schuetz, A.W.1    Lessman, C.A.2
  • 29
  • 30
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli E. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, E.K.1
  • 31
    • 0003448569 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Harlow E. and Lane D. (1988) Antibodies: A Laboratory Manual, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1988) Antibodies: A Laboratory Manual
    • Harlow, E.1    Lane, D.2
  • 32
    • 0023442001 scopus 로고
    • Microtubule assembly in cytoplasmic extracts of Xenopus oocytes and eggs
    • Gard D. L. and Kirschner M. (1987) Microtubule assembly in cytoplasmic extracts of Xenopus oocytes and eggs. J. Cell Biol. 105: 2191-2201
    • (1987) J. Cell Biol. , vol.105 , pp. 2191-2201
    • Gard, D.L.1    Kirschner, M.2
  • 33
    • 0022994054 scopus 로고
    • Heterogeneity and structure of brain tubulins from cold-adapted antarctic fishes: Comparison to brain tubulins from a temperate fish and a mammal
    • Detrich H. W. III and Overton S. A. (1986) Heterogeneity and structure of brain tubulins from cold-adapted antarctic fishes: comparison to brain tubulins from a temperate fish and a mammal. J. Biol. Chem. 261: 10922-10930
    • (1986) J. Biol. Chem. , vol.261 , pp. 10922-10930
    • Detrich H.W. III1    Overton, S.A.2
  • 35
    • 0026486578 scopus 로고
    • A predominant basic α-tubulin isoform present in prophase Xenopus oocyte decreases during meiotic maturation
    • Thibier C., Denqulet P., Jessus C. and Ozon R. (1992) A predominant basic α-tubulin isoform present in prophase Xenopus oocyte decreases during meiotic maturation. Biol. Cell. 75: 173-180
    • (1992) Biol. Cell , vol.75 , pp. 173-180
    • Thibier, C.1    Denqulet, P.2    Jessus, C.3    Ozon, R.4
  • 36
    • 0026087534 scopus 로고
    • Organization, nucleation, and acetylation of microtubules in Xenopus laevis oocytes: A study by confocal immunofluorescence microscopy
    • Gard D. L. (1991) Organization, nucleation, and acetylation of microtubules in Xenopus laevis oocytes: a study by confocal immunofluorescence microscopy. Dev. Biol. 143: 346-362
    • (1991) Dev. Biol. , vol.143 , pp. 346-362
    • Gard, D.L.1
  • 37
    • 0023582253 scopus 로고
    • Control of microtubule nucleation and stability in Madin-Darby canine kidney cells: The occurrence of noncentrosomal, stable detyrosinated microtubules
    • Bré M. H., Kreis T. E. and Karsenti E. (1987) Control of microtubule nucleation and stability in Madin-Darby canine kidney cells: the occurrence of noncentrosomal, stable detyrosinated microtubules. J. Cell Biol. 105: 1283-1296
    • (1987) J. Cell Biol. , vol.105 , pp. 1283-1296
    • Bré, M.H.1    Kreis, T.E.2    Karsenti, E.3
  • 38
    • 0029558318 scopus 로고
    • Microtubule organization and the distribution of γ-tubulin in spermatogenesis of a beetle, Tenebrio molitor (Tenebrionidae, Coleoptera, Insecta)
    • Wolf K. W. and Joshi H. C. (1995) Microtubule organization and the distribution of γ-tubulin in spermatogenesis of a beetle, Tenebrio molitor (Tenebrionidae, Coleoptera, Insecta) J. Cell Sci. 108: 3855-3865
    • (1995) J. Cell Sci. , vol.108 , pp. 3855-3865
    • Wolf, K.W.1    Joshi, H.C.2
  • 39
    • 0028948469 scopus 로고
    • Cold-stable and cold-adapted microtubules
    • Wallin M. and Stromberg E. (1995) Cold-stable and cold-adapted microtubules. Int. Rev. Cytol. 157: 1-31
    • (1995) Int. Rev. Cytol. , vol.157 , pp. 1-31
    • Wallin, M.1    Stromberg, E.2


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