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Volumn 58, Issue 6, 1999, Pages 959-971

Differential in vitro association of vinca alkaloid-induced tubulin spiral filaments into aggregated spirals

Author keywords

Microtubule associated proteins; Paracrystals; Spirals; Tubulin; Turbidity; Vinca alkaloids

Indexed keywords

ANHYDROVINBLASTINE; MICROTUBULE ASSOCIATED PROTEIN; MICROTUBULE ASSOCIATED PROTEIN 2; MICROTUBULE ASSOCIATED PROTEIN 5; NAVELBINE; PHOSPHORAMIDIC ACID; S 12128; S 12129; S 12155; S 12156; S 12165; S 12334; S 12335; S 12362; S 12363; TAU PROTEIN; TUBULIN; UNCLASSIFIED DRUG; VINBLASTINE; VINCA ALKALOID; VINCRISTINE; VINDESINE;

EID: 0032793783     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-2952(99)00190-2     Document Type: Article
Times cited : (19)

References (41)
  • 1
    • 0017736254 scopus 로고
    • Correlation of biologic data with physico-chemical properties among the vinca alkaloids and their congeners
    • Owellen R.J., Donigian D.W., Hartke C.A., Hains F.O. Correlation of biologic data with physico-chemical properties among the vinca alkaloids and their congeners. Biochem Pharmacol. 26:1977;1213-1219.
    • (1977) Biochem Pharmacol , vol.26 , pp. 1213-1219
    • Owellen, R.J.1    Donigian, D.W.2    Hartke, C.A.3    Hains, F.O.4
  • 2
    • 0026327465 scopus 로고
    • Interactions of the Catharanthus (vinca) alkaloids with tubulin and microtubules
    • Himes R.H. Interactions of the Catharanthus (vinca) alkaloids with tubulin and microtubules. Pharmacol Ther. 51:1991;257-267.
    • (1991) Pharmacol Ther , vol.51 , pp. 257-267
    • Himes, R.H.1
  • 3
    • 0026356972 scopus 로고
    • Physical and spectroscopic methods for the evaluation of the interactions of antimitotic agents with tubulin
    • Timasheff S.N., Andreu J.M., Na G.C. Physical and spectroscopic methods for the evaluation of the interactions of antimitotic agents with tubulin. Pharmacol Ther. 52:1991;191-210.
    • (1991) Pharmacol Ther , vol.52 , pp. 191-210
    • Timasheff, S.N.1    Andreu, J.M.2    Na, G.C.3
  • 4
    • 0026643589 scopus 로고
    • Effects of vinblastine, podophyllotoxin and nocodazole on mitotic spindles: Implications for the role of microtubule dynamics in mitosis
    • Jordan M.A., Thrower D., Wilson L. Effects of vinblastine, podophyllotoxin and nocodazole on mitotic spindles Implications for the role of microtubule dynamics in mitosis . J Cell Sci. 102:1992;401-416.
    • (1992) J Cell Sci , vol.102 , pp. 401-416
    • Jordan, M.A.1    Thrower, D.2    Wilson, L.3
  • 5
    • 0027461876 scopus 로고
    • Kinetic stabilization of microtubule dynamic instability in vitro by vinblastine
    • Toso R.J., Jordan M.A., Farrell K.W., Matsumoto B., Wilson L. Kinetic stabilization of microtubule dynamic instability in vitro by vinblastine. Biochemistry. 32:1993;1285-1293.
    • (1993) Biochemistry , vol.32 , pp. 1285-1293
    • Toso, R.J.1    Jordan, M.A.2    Farrell, K.W.3    Matsumoto, B.4    Wilson, L.5
  • 6
    • 0026345003 scopus 로고
    • The clinical pharmacology and use of antimicrotubule agents in cancer chemotherapeutics
    • Rowinsky E.K., Donehower R.C. The clinical pharmacology and use of antimicrotubule agents in cancer chemotherapeutics. Pharmacol Ther. 52:1991;35-84.
    • (1991) Pharmacol Ther , vol.52 , pp. 35-84
    • Rowinsky, E.K.1    Donehower, R.C.2
  • 7
    • 0030008570 scopus 로고    scopus 로고
    • Interaction of vinca alkaloids with tubulin: A comparison of vinblastine, vincristine, and vinorelbine
    • Lobert S., Vulevic B., Correia J.J. Interaction of vinca alkaloids with tubulin A comparison of vinblastine, vincristine, and vinorelbine . Biochemistry. 35:1996;6806-6814.
    • (1996) Biochemistry , vol.35 , pp. 6806-6814
    • Lobert, S.1    Vulevic, B.2    Correia, J.J.3
  • 8
    • 85063514735 scopus 로고
    • Interaction of tubulin with small ligands
    • J. Avila. Boca Raton FL: CRC Press
    • Hamel E. Interaction of tubulin with small ligands. Avila J. Microtubule Proteins. 1990;89-191 CRC Press, Boca Raton FL.
    • (1990) Microtubule Proteins , pp. 89-191
    • Hamel, E.1
  • 9
    • 0022542990 scopus 로고
    • Vinblastine-induced aggregation of brine shrimp (Artemia) tubulin
    • Mackinlay S.A., Ludueña R.F., MacRae T.H. Vinblastine-induced aggregation of brine shrimp (Artemia) tubulin. Biochim Biophys Acta. 882:1986;419-426.
    • (1986) Biochim Biophys Acta , vol.882 , pp. 419-426
    • MacKinlay, S.A.1    Ludueña, R.F.2    MacRae, T.H.3
  • 10
    • 0025610485 scopus 로고
    • Instability of pleomorphic tubulin paracrystals artificially induced by vinca alkaloids in tissue-cultured cells
    • Takanari H., Yosida T., Morita J., Isutzu K., Ito T. Instability of pleomorphic tubulin paracrystals artificially induced by vinca alkaloids in tissue-cultured cells. Biol Cell. 70:1990;83-90.
    • (1990) Biol Cell , vol.70 , pp. 83-90
    • Takanari, H.1    Yosida, T.2    Morita, J.3    Isutzu, K.4    Ito, T.5
  • 11
    • 0017086604 scopus 로고
    • Action of the Vinca alkaloids vincristine, vinblastine and desacetyl vinblastine amide (vindesine) on microtubules in vitro
    • Himes R.H., Kersey R.N., Heller-Bettinger I., Samson F.E. Action of the Vinca alkaloids vincristine, vinblastine and desacetyl vinblastine amide (vindesine) on microtubules in vitro. Cancer Res. 36:1976;3798-3802.
    • (1976) Cancer Res , vol.36 , pp. 3798-3802
    • Himes, R.H.1    Kersey, R.N.2    Heller-Bettinger, I.3    Samson, F.E.4
  • 13
    • 0021723101 scopus 로고
    • Contrasting roles of tau and microtubule-associated protein 2 in the vinblastine-induced aggregation of brain tubulin
    • Ludueña R.F., Fellous A., McManus L., Jordan M.A., Nunez J. Contrasting roles of tau and microtubule-associated protein 2 in the vinblastine-induced aggregation of brain tubulin. J Biol Chem. 259:1984;12890-12898.
    • (1984) J Biol Chem , vol.259 , pp. 12890-12898
    • Ludueña, R.F.1    Fellous, A.2    McManus, L.3    Jordan, M.A.4    Nunez, J.5
  • 14
    • 0024583029 scopus 로고
    • Specific alterations in the biological activities of C-20′-modified vinblastine congeners
    • Borman L., Kuehne M.E. Specific alterations in the biological activities of C-20′-modified vinblastine congeners. Biochem Pharmacol. 38:1989;715-724.
    • (1989) Biochem Pharmacol , vol.38 , pp. 715-724
    • Borman, L.1    Kuehne, M.E.2
  • 15
    • 0026542731 scopus 로고
    • Cellular uptake and tubulin binding properties of four vinca alkaloids
    • Singer W.D., Himes R.H. Cellular uptake and tubulin binding properties of four vinca alkaloids. Biochem Pharmacol. 43:1992;545-551.
    • (1992) Biochem Pharmacol , vol.43 , pp. 545-551
    • Singer, W.D.1    Himes, R.H.2
  • 16
    • 0025341864 scopus 로고
    • Use of snail neurons in developing quantitative ultrastructural parameters for neurotoxic side effects of Vinca antitumor agents
    • Müller L.J., Moorer-van Delft C.M., Zijl R., Roubos E.W. Use of snail neurons in developing quantitative ultrastructural parameters for neurotoxic side effects of Vinca antitumor agents. Cancer Res. 50:1990;1924-1928.
    • (1990) Cancer Res , vol.50 , pp. 1924-1928
    • Müller, L.J.1    Moorer-Van Delft, C.M.2    Zijl, R.3    Roubos, E.W.4
  • 19
  • 20
  • 22
    • 0025008784 scopus 로고
    • Selective purification of microtubule-associated proteins 1 and 2 from rat brain using poly(l-aspartic acid)
    • Fujii T., Nakamura A., Ogoma Y., Kondo Y., Arai T. Selective purification of microtubule-associated proteins 1 and 2 from rat brain using poly(l-aspartic acid). Anal Biochem. 184:1990;268-273.
    • (1990) Anal Biochem , vol.184 , pp. 268-273
    • Fujii, T.1    Nakamura, A.2    Ogoma, Y.3    Kondo, Y.4    Arai, T.5
  • 23
    • 0000146079 scopus 로고
    • Identification of a major component of the neuronal cytoskeleton
    • Bloom G.S., Lucas F.C., Vallee R.B. Identification of a major component of the neuronal cytoskeleton. Proc Natl Acad Sci USA. 82:1985;5404-5408.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 5404-5408
    • Bloom, G.S.1    Lucas, F.C.2    Vallee, R.B.3
  • 24
    • 0018269898 scopus 로고
    • Interaction of vinblastine analogues with tubulin
    • Zavala F., Guénard D., Potier P. Interaction of vinblastine analogues with tubulin. Experientia. 34:1978;1497-1499.
    • (1978) Experientia , vol.34 , pp. 1497-1499
    • Zavala, F.1    Guénard, D.2    Potier, P.3
  • 25
    • 0015507486 scopus 로고
    • Vinblastine sulfate: Its reversible thermal aggregation and interaction with hydrophobic groups
    • Nimni M.E. Vinblastine sulfate Its reversible thermal aggregation and interaction with hydrophobic groups . Biochem Pharmacol. 21:1972;485-493.
    • (1972) Biochem Pharmacol , vol.21 , pp. 485-493
    • Nimni, M.E.1
  • 26
    • 0016838962 scopus 로고
    • Some features of the vinblastine-induced assembly of porcine tubulin
    • Ventilla M., Cantor C.R., Shelanski M.L. Some features of the vinblastine-induced assembly of porcine tubulin. Arch Biochem Biophys. 171:1975;154-162.
    • (1975) Arch Biochem Biophys , vol.171 , pp. 154-162
    • Ventilla, M.1    Cantor, C.R.2    Shelanski, M.L.3
  • 27
    • 0023898531 scopus 로고
    • Effect of solution variables on the binding of vinblastine to tubulin
    • Singer W.D., Hersh R.T., Himes R.H. Effect of solution variables on the binding of vinblastine to tubulin. Biochem Pharmacol. 37:1988;2691-2696.
    • (1988) Biochem Pharmacol , vol.37 , pp. 2691-2696
    • Singer, W.D.1    Hersh, R.T.2    Himes, R.H.3
  • 28
    • 0031037726 scopus 로고    scopus 로고
    • Divalent cation and ionic strength on Vinca alkaloid-induced tubulin self-association
    • Lobert S., Boyd C.A., Correia J.J. Divalent cation and ionic strength on Vinca alkaloid-induced tubulin self-association. Biophys J. 72:1997;416-427.
    • (1997) Biophys J , vol.72 , pp. 416-427
    • Lobert, S.1    Boyd, C.A.2    Correia, J.J.3
  • 29
    • 0029615473 scopus 로고
    • The effect of temperature on the structure of vinblastine-induced polymers of purified tubulin: Detection of a reversible conformational change
    • Nogales E., Medrano F.J., Diakun G.P., Mant G.R., Towns-Andrews E., Bordas J. The effect of temperature on the structure of vinblastine-induced polymers of purified tubulin Detection of a reversible conformational change . J Mol Biol. 254:1995;416-430.
    • (1995) J Mol Biol , vol.254 , pp. 416-430
    • Nogales, E.1    Medrano, F.J.2    Diakun, G.P.3    Mant, G.R.4    Towns-Andrews, E.5    Bordas, J.6
  • 30
    • 0029020164 scopus 로고
    • Binding of vinblastine to phosphocellulose-purified and αβ-class III tubulin: The role of nucleotides and β-tubulin isotypes
    • Lobert S., Frankfurter A., Correia J.J. Binding of vinblastine to phosphocellulose-purified and αβ-class III tubulin The role of nucleotides and β-tubulin isotypes . Biochemistry. 34:1995;8050-8060.
    • (1995) Biochemistry , vol.34 , pp. 8050-8060
    • Lobert, S.1    Frankfurter, A.2    Correia, J.J.3
  • 31
    • 0018570883 scopus 로고
    • Effect of antimitotic drugs on tubulin GTPase activity and self-assembly
    • David-Pfeuty T., Simon C., Pantaloni D. Effect of antimitotic drugs on tubulin GTPase activity and self-assembly. J Biol Chem. 254:1979;11696-11702.
    • (1979) J Biol Chem , vol.254 , pp. 11696-11702
    • David-Pfeuty, T.1    Simon, C.2    Pantaloni, D.3
  • 32
    • 0031453820 scopus 로고    scopus 로고
    • Vinblastine-induced formation of tubulin polymers is electrostatically regulated and nucleated
    • Rai S.S., Wolff J. Vinblastine-induced formation of tubulin polymers is electrostatically regulated and nucleated. Eur J Biochem. 250:1997;427-431.
    • (1997) Eur J Biochem , vol.250 , pp. 427-431
    • Rai, S.S.1    Wolff, J.2
  • 33
    • 0015493817 scopus 로고
    • Definition of three classes of binding sites in isolated microtubule crystals
    • Bryan J. Definition of three classes of binding sites in isolated microtubule crystals. Biochemistry. 11:1972;2611-2616.
    • (1972) Biochemistry , vol.11 , pp. 2611-2616
    • Bryan, J.1
  • 34
    • 0018197941 scopus 로고
    • 3H-labeled vinblastine binding to vinblastine-tubulin crystals
    • 3H-labeled vinblastine binding to vinblastine-tubulin crystals. J Mol Biol. 121:1978;255-268.
    • (1978) J Mol Biol , vol.121 , pp. 255-268
    • Wilson, L.1    Morse, A.N.C.2    Bryan, J.3
  • 35
    • 0027058327 scopus 로고
    • X-ray solution scattering studies on vinblastine-induced polymers of microtubule protein: Structural characterisation and effects of temperature
    • Hodgkinson J.L., Hutton T., Medrano F.J., Bordas J. X-ray solution scattering studies on vinblastine-induced polymers of microtubule protein Structural characterisation and effects of temperature . J Struct Biol. 109:1992;28-38.
    • (1992) J Struct Biol , vol.109 , pp. 28-38
    • Hodgkinson, J.L.1    Hutton, T.2    Medrano, F.J.3    Bordas, J.4
  • 36
    • 0021591122 scopus 로고
    • Arrangement of protofilaments in two forms of tubulin crystal induced by vinblastine
    • Amos L.A., Jubb J.S., Henderson R., Vigers G. Arrangement of protofilaments in two forms of tubulin crystal induced by vinblastine. J Mol Biol. 178:1984;711-729.
    • (1984) J Mol Biol , vol.178 , pp. 711-729
    • Amos, L.A.1    Jubb, J.S.2    Henderson, R.3    Vigers, G.4
  • 37
    • 0018760635 scopus 로고
    • Effect of microtubule-associated proteins on the interaction of vincristine with microtubule and tubulin
    • Donoso J.A., Haskins K.M., Himes R.H. Effect of microtubule-associated proteins on the interaction of vincristine with microtubule and tubulin. Cancer Res. 39:1979;1604-1610.
    • (1979) Cancer Res , vol.39 , pp. 1604-1610
    • Donoso, J.A.1    Haskins, K.M.2    Himes, R.H.3
  • 38
    • 0032516066 scopus 로고    scopus 로고
    • The C terminus of β-tubulin regulates vinblastine-induced tubulin polymerization
    • Rai S.S., Wolff J. The C terminus of β-tubulin regulates vinblastine-induced tubulin polymerization. Proc Natl Acad Sci USA. 95:1998;4253-4257.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 4253-4257
    • Rai, S.S.1    Wolff, J.2
  • 39
    • 0029190887 scopus 로고
    • Structure and function in the tubulin dimer and the role of the acidic carbonyl terminus
    • B.B. Biswas, Siddhartha R. New York: Plenum Press
    • Sackett D.L. Structure and function in the tubulin dimer and the role of the acidic carbonyl terminus. Biswas B.B., Siddhartha R. Subcellular Biochemistry. Vol. 24:1995;255-302 Plenum Press, New York.
    • (1995) Subcellular Biochemistry , vol.24 , pp. 255-302
    • Sackett, D.L.1
  • 40
    • 0030723169 scopus 로고    scopus 로고
    • Dissociation of tubulin assembly-inhibiting and aggregation-promoting activities by a vinblastine derivative
    • Rai S.S., Wolff J. Dissociation of tubulin assembly-inhibiting and aggregation-promoting activities by a vinblastine derivative. FEBS Lett. 416:1997;251-253.
    • (1997) FEBS Lett , vol.416 , pp. 251-253
    • Rai, S.S.1    Wolff, J.2
  • 41
    • 0032495513 scopus 로고    scopus 로고
    • Structure of the αβ tubulin dimer by electron crystallography
    • Nogales E., Wolf S.G., Downing K.H. Structure of the αβ tubulin dimer by electron crystallography. Nature. 391:1998;199-202.
    • (1998) Nature , vol.391 , pp. 199-202
    • Nogales, E.1    Wolf, S.G.2    Downing, K.H.3


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