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Volumn 45, Issue 3, 2006, Pages 899-906

Understanding the mechanism of the antimitogenic activity of suramin

Author keywords

[No Author keywords available]

Indexed keywords

CALORIMETRY; ISOTHERMS; SIZE EXCLUSION CHROMATOGRAPHY; STOICHIOMETRY; TITRATION; TUMORS;

EID: 31044435080     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi051389b     Document Type: Article
Times cited : (27)

References (34)
  • 1
    • 1242340428 scopus 로고    scopus 로고
    • Antiangiogenic cancer therapy
    • Cao, Y. (2004) Antiangiogenic cancer therapy, Semin. Cancer Biol. 14, 139-145.
    • (2004) Semin. Cancer Biol. , vol.14 , pp. 139-145
    • Cao, Y.1
  • 2
    • 0024339705 scopus 로고
    • The heparin-binding (fibroblast) growth factor family of proteins
    • Burgess, W. H., and Maciag, T. (1989) The heparin-binding (fibroblast) growth factor family of proteins, Annu. Rev. Biochem. 58, 575-606.
    • (1989) Annu. Rev. Biochem. , vol.58 , pp. 575-606
    • Burgess, W.H.1    Maciag, T.2
  • 3
    • 0023157363 scopus 로고
    • Angiogenic factors
    • Folkman, J., and Klagsburn, M. (1987) Angiogenic factors, Science 235, 442-447.
    • (1987) Science , vol.235 , pp. 442-447
    • Folkman, J.1    Klagsburn, M.2
  • 4
    • 0033662360 scopus 로고    scopus 로고
    • Fibroblast growth factors and their inhibitors
    • Manetti, F., Corelli, F., and Botta, M. (2000) Fibroblast growth factors and their inhibitors, Curr. Pharm. Des. 6, 1897-1924.
    • (2000) Curr. Pharm. Des. , vol.6 , pp. 1897-1924
    • Manetti, F.1    Corelli, F.2    Botta, M.3
  • 6
    • 0036229960 scopus 로고    scopus 로고
    • Nature of interaction between basic fibroblast growth factor and the antiangiogenic drug 7,7-(carbonyl-bis[imino-N-methyl-4,2-pyrrolecarbonylimino[N- methyl-4,2-pyrrole]-carbonylimino])-bis-(1,3-naphthalene disulfonate). II. Removal of polar interactions affects protein folding
    • Zamai, M., Hariharan, C., Pines, D., Safran, M., Yayon, A., Caiolfa, V. R., Cohen-Luria, R., Pines, E., and Parola, A. H. (2002) Nature of interaction between basic fibroblast growth factor and the antiangiogenic drug 7,7-(carbonyl-bis[imino-N-methyl-4,2-pyrrolecarbonylimino[N-methyl-4,2-pyrrole] -carbonylimino])-bis-(1,3-naphthalene disulfonate). II. Removal of polar interactions affects protein folding, Biophys. J. 82, 2652-2664.
    • (2002) Biophys. J. , vol.82 , pp. 2652-2664
    • Zamai, M.1    Hariharan, C.2    Pines, D.3    Safran, M.4    Yayon, A.5    Caiolfa, V.R.6    Cohen-Luria, R.7    Pines, E.8    Parola, A.H.9
  • 7
    • 12944272151 scopus 로고    scopus 로고
    • Fibroblast growth factors: An epigenetic mechanism of broad spectrum resistance to anticancer drugs
    • Song, S., Wientjes, M. G., Gan, Y., and Au, J. L. S. (2000) Fibroblast growth factors: An epigenetic mechanism of broad spectrum resistance to anticancer drugs, Proc. Natl. Acad. Sci. U.S.A. 97, 8658-8663.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 8658-8663
    • Song, S.1    Wientjes, M.G.2    Gan, Y.3    Au, J.L.S.4
  • 9
    • 0032483474 scopus 로고    scopus 로고
    • Solution structure of acidic fibroblast growth factor bound to 1,3,6-naphthalenetrisulfonate: A minimal model for the anti-tumoral action of suramins and suradistas
    • Lozano, R. M., Jimenez, M. A., Santora, J., Rico, M., and Gallego, G. G. (1998) Solution structure of acidic fibroblast growth factor bound to 1,3,6-naphthalenetrisulfonate: A minimal model for the anti-tumoral action of suramins and suradistas, J. Mol. Biol. 281, 899-915.
    • (1998) J. Mol. Biol. , vol.281 , pp. 899-915
    • Lozano, R.M.1    Jimenez, M.A.2    Santora, J.3    Rico, M.4    Gallego, G.G.5
  • 11
    • 0037168468 scopus 로고    scopus 로고
    • Investigation of the structural stability of the human acidic fibroblast growth factor by hydrogen-deuterium exchange
    • Chi, Y. H., Kumar, T. K. S., Kathir, K. M., Lin, D. H., Zhu, G., Chiu, I. M., and Yu, C. (2002) Investigation of the structural stability of the human acidic fibroblast growth factor by hydrogen-deuterium exchange, Biochemistry 41, 15350-15339.
    • (2002) Biochemistry , vol.41 , pp. 15350-115339
    • Chi, Y.H.1    Kumar, T.K.S.2    Kathir, K.M.3    Lin, D.H.4    Zhu, G.5    Chiu, I.M.6    Yu, C.7
  • 14
    • 9444287030 scopus 로고    scopus 로고
    • Common and distinct elements in cellular signaling via EGF and FGF receptors
    • Schlessinger, J. (2004) Common and distinct elements in cellular signaling via EGF and FGF receptors, Science 306, 1506-1507.
    • (2004) Science , vol.306 , pp. 1506-1507
    • Schlessinger, J.1
  • 15
    • 0034640103 scopus 로고    scopus 로고
    • Crystal structures of two FGF-FGFR complexes reveal the determinants of ligand-receptor specificity
    • Plotnikov, A. N., Hubbard, S. R., Schlessinger, J., and Mohammadi, M. (2000) Crystal structures of two FGF-FGFR complexes reveal the determinants of ligand-receptor specificity, Cell 101, 413-424.
    • (2000) Cell , vol.101 , pp. 413-424
    • Plotnikov, A.N.1    Hubbard, S.R.2    Schlessinger, J.3    Mohammadi, M.4
  • 16
    • 0035443744 scopus 로고    scopus 로고
    • Role of heparan sulfate in fibroblast growth factor signalling: A structural view
    • Pellegrini, L. (2001) Role of heparan sulfate in fibroblast growth factor signalling: A structural view, Curr. Opin. Struct. Biol. 11, 629-634.
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 629-634
    • Pellegrini, L.1
  • 17
    • 1642422312 scopus 로고    scopus 로고
    • Molecular cloning, overexpression, and characterization of the ligand-binding D2 domain of fibroblast growth factor receptor
    • Hung, K. W., Kumar, T. K., Chi, Y. H., Chiu, I. M., and Yu, C. (2004) Molecular cloning, overexpression, and characterization of the ligand-binding D2 domain of fibroblast growth factor receptor, Biochem. Biophys. Res. Commun. 317, 253-258.
    • (2004) Biochem. Biophys. Res. Commun. , vol.317 , pp. 253-258
    • Hung, K.W.1    Kumar, T.K.2    Chi, Y.H.3    Chiu, I.M.4    Yu, C.5
  • 20
    • 0027989479 scopus 로고
    • Multivalent ligand-receptor binding interactions in the fibroblast growth factor system produce a cooperative growth factor and heparin mechanism for receptor dimerization
    • Pantoliano, M. W., Horlick, R. A., Springer, B. A., Van Dyk, D. E., Tobery, T., Wetmore, D. R., Lear, J. D., Nahapetian, A. T., Bradley, J. D., and Sisk, W. P. (1994) Multivalent ligand-receptor binding interactions in the fibroblast growth factor system produce a cooperative growth factor and heparin mechanism for receptor dimerization, Biochemistry 33, 10229-10248.
    • (1994) Biochemistry , vol.33 , pp. 10229-10248
    • Pantoliano, M.W.1    Horlick, R.A.2    Springer, B.A.3    Van Dyk, D.E.4    Tobery, T.5    Wetmore, D.R.6    Lear, J.D.7    Nahapetian, A.T.8    Bradley, J.D.9    Sisk, W.P.10
  • 21
    • 4944241352 scopus 로고    scopus 로고
    • Antitumor activities of a novel indolin-2-ketone compound, Z24: More potent inhibition on bFGF-induced angiogenesis and bcl-2 over-expressing cancer cells
    • Wang, L., Li, J. J., Zheng, Z. B., Liu, H. X., Du, G. J., and Li, S. (2004) Antitumor activities of a novel indolin-2-ketone compound, Z24: More potent inhibition on bFGF-induced angiogenesis and bcl-2 over-expressing cancer cells, Eur. J. Pharmacol. 502, 1-10.
    • (2004) Eur. J. Pharmacol. , vol.502 , pp. 1-10
    • Wang, L.1    Li, J.J.2    Zheng, Z.B.3    Liu, H.X.4    Du, G.J.5    Li, S.6
  • 22
    • 9744254768 scopus 로고    scopus 로고
    • Evaluation of combination chemotherapy: Integration of nonlinear regression, curve shift, isobologram, and combination index analyses
    • Zhao, L., Wientjes, M. G., and Au, A. L. (2004) Evaluation of combination chemotherapy: Integration of nonlinear regression, curve shift, isobologram, and combination index analyses, Clin. Cancer Res. 10, 7994-8004.
    • (2004) Clin. Cancer Res. , vol.10 , pp. 7994-8004
    • Zhao, L.1    Wientjes, M.G.2    Au, A.L.3
  • 23
    • 4644265735 scopus 로고    scopus 로고
    • Low-dose suramin enhanced paclitaxel activity in chemotherapy-naïve and paclitaxel-retreated human breast xenograft tumors
    • Song, S., Yu, B., Wei, Y., Wientjes, M. G., and Au, J. L. (2004) Low-Dose Suramin Enhanced Paclitaxel Activity in Chemotherapy-Naïve and Paclitaxel-retreated Human Breast Xenograft Tumors, Clin. Cancer Res. 10, 6058-6065.
    • (2004) Clin. Cancer Res. , vol.10 , pp. 6058-6065
    • Song, S.1    Yu, B.2    Wei, Y.3    Wientjes, M.G.4    Au, J.L.5
  • 24
    • 14344255691 scopus 로고    scopus 로고
    • Use of inding enthalpy to drive an allosteric transition
    • Brown, P. H., and Beckett, D. (2005) Use of inding enthalpy to drive an allosteric transition, Biochemistry 44, 3112-3121.
    • (2005) Biochemistry , vol.44 , pp. 3112-3121
    • Brown, P.H.1    Beckett, D.2
  • 25
    • 12344326693 scopus 로고    scopus 로고
    • Sulfonamide drugs binding to the colchicine site of tubulin: Thermodynamic analysis of the drug-tubulin interactions by isothermal titration calorimetry
    • Banerjee, M., Poddar, A., Mitra, G., Surolea, A., Owa, T., and Battacharyya, B. (2005) Sulfonamide drugs binding to the colchicine site of tubulin: Thermodynamic analysis of the drug-tubulin interactions by isothermal titration calorimetry, J. Med. Chem. 48, 547-555.
    • (2005) J. Med. Chem. , vol.48 , pp. 547-555
    • Banerjee, M.1    Poddar, A.2    Mitra, G.3    Surolea, A.4    Owa, T.5    Battacharyya, B.6
  • 26
    • 14644415912 scopus 로고    scopus 로고
    • The interaction of human tryptase-β with small molecule inhibitors provides new insights into the unusual functional instability and quaternary structure of the protease
    • Selwood, T., Smolensky, H., McCaslin, D. R., and Schechter, N. M. (2005) The interaction of human tryptase-β with small molecule inhibitors provides new insights into the unusual functional instability and quaternary structure of the protease, Biochemistry 44, 3580-3590.
    • (2005) Biochemistry , vol.44 , pp. 3580-3590
    • Selwood, T.1    Smolensky, H.2    McCaslin, D.R.3    Schechter, N.M.4
  • 27
    • 4644229651 scopus 로고    scopus 로고
    • Partial proteolysis of simian virus 40 T antigen reveals intramolecular contacts between domains and conformation changes upon hexamer assembly
    • Weisshart, K., Friedl, S., Taneja, P., Nasheuer, H. P., Schlott, B., Grosse, F., and Fanning, E. (2004) Partial Proteolysis of Simian Virus 40 T Antigen Reveals Intramolecular Contacts between Domains and Conformation Changes upon Hexamer Assembly, J. Biol. Chem. 279, 38943-38951.
    • (2004) J. Biol. Chem. , vol.279 , pp. 38943-38951
    • Weisshart, K.1    Friedl, S.2    Taneja, P.3    Nasheuer, H.P.4    Schlott, B.5    Grosse, F.6    Fanning, E.7
  • 29
    • 0037448895 scopus 로고    scopus 로고
    • Discovery of aminoglycoside mimetics by NMR-based screening of Escherichia coli A-site RNA
    • Yu, L., Oost, T. K., Schkerjantz, J. M., Yang, J., Janowick, D., and Fesik, S. W. (2003) Discovery of aminoglycoside mimetics by NMR-based screening of Escherichia coli A-site RNA, J. Am. Chem. Soc. 125, 4444-4450.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 4444-4450
    • Yu, L.1    Oost, T.K.2    Schkerjantz, J.M.3    Yang, J.4    Janowick, D.5    Fesik, S.W.6
  • 30
    • 0037039335 scopus 로고    scopus 로고
    • Mapping protein-protein interactions in solution by NMR spectroscopy
    • Zuiderweg, E. R. (2002) Mapping protein-protein interactions in solution by NMR spectroscopy, Biochemistry 41, 1-7.
    • (2002) Biochemistry , vol.41 , pp. 1-7
    • Zuiderweg, E.R.1
  • 31
    • 0034718796 scopus 로고    scopus 로고
    • Crystal structure of fibroblast growth factor receptor ectodomain bound to ligand and heparin
    • Pellegrini, L., Burke, D. F., von Delft, F., Mulloy, B., and Blundell, T. L. (2000) Crystal structure of fibroblast growth factor receptor ectodomain bound to ligand and heparin, Nature 407, 1029-1034.
    • (2000) Nature , vol.407 , pp. 1029-1034
    • Pellegrini, L.1    Burke, D.F.2    Von Delft, F.3    Mulloy, B.4    Blundell, T.L.5
  • 33
    • 0037484261 scopus 로고    scopus 로고
    • Leads for development of new naphthalenesulfonate derivatives with enhanced antiangiogenic activity: Crystal structure of acidic fibroblast growth factor in complex with 5-amino-2-naphthalene sulfonate
    • Fernandez-Tornero, C., Lozano, R. M., Redondo-Horcajo, M., Gomez, A. M., Lopez, J. C., Quesada, E., Uriel, C., Valverde, S., Cuevas, P., Romero, A., and Gimenez-Gallego, G. (2003) Leads for development of new naphthalenesulfonate derivatives with enhanced antiangiogenic activity: Crystal structure of acidic fibroblast growth factor in complex with 5-amino-2-naphthalene sulfonate, J. Biol. Chem. 278, 21774-21781.
    • (2003) J. Biol. Chem. , vol.278 , pp. 21774-21781
    • Fernandez-Tornero, C.1    Lozano, R.M.2    Redondo-Horcajo, M.3    Gomez, A.M.4    Lopez, J.C.5    Quesada, E.6    Uriel, C.7    Valverde, S.8    Cuevas, P.9    Romero, A.10    Gimenez-Gallego, G.11
  • 34
    • 0031694297 scopus 로고    scopus 로고
    • Synthesis and binding mode of heterocyclic analogues of suramin inhibiting the human basic fibroblast growth factor
    • Manetti, F., Cappello, V., Botta, M., Corelli, F., Mongelli, N., Biasoli, G., Borgia, A. L., and Ciomei, M. (1998) Synthesis and binding mode of heterocyclic analogues of suramin inhibiting the human basic fibroblast growth factor, Bioorg. Med. Chem. 6, 947-958.
    • (1998) Bioorg. Med. Chem. , vol.6 , pp. 947-958
    • Manetti, F.1    Cappello, V.2    Botta, M.3    Corelli, F.4    Mongelli, N.5    Biasoli, G.6    Borgia, A.L.7    Ciomei, M.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.