메뉴 건너뛰기




Volumn 4, Issue 10, 1998, Pages 2463-2471

Inhibition of human glioblastoma cell adhesion and invasion by 4-(4'- hydroxylphenyl)-amino-6,7-dimethoxyquinazoline (WHI-P131) and 4-(3'-bromo- 4'-hydroxylphenyl)amino-6,7-dimethoxyquinazoline (WHI-P154)

Author keywords

[No Author keywords available]

Indexed keywords

4 (3' BROMO 4' HYDROXYPHENYL)AMINO 6,7 DIMETHOXYQUINAZOLINE; 4 (4 HYDROXYANILINO) 6,7 DIMETHOXYQUINAZOLINE; 4 (4' HYDROXYPHENYL)AMINO 6,7 DIMETHOXYQUINAZOLINE; QUINAZOLINE DERIVATIVE; UNCLASSIFIED DRUG; WHI P 154;

EID: 0031755916     PISSN: 10780432     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (35)

References (45)
  • 1
    • 0000117128 scopus 로고
    • Tumors of central neuroepithelial orisin
    • E. Arnold (ed.), London: Hodder & Stoughton
    • Russel, D. C., and Rubinstein, L. Tumors of central neuroepithelial orisin. In: E. Arnold (ed.), Pathology of Tumors of the Nervous System, Ed. 5., pp. 83-289. London: Hodder & Stoughton, 1989.
    • (1989) Pathology of Tumors of the Nervous System, Ed. 5 , pp. 83-289
    • Russel, D.C.1    Rubinstein, L.2
  • 2
    • 0027520998 scopus 로고
    • Resection, biopsy, and survival in malignant glial neoplasm
    • Devaux, B. C., O'Fallon, J. R., and Kelly, P. J. Resection, biopsy, and survival in malignant glial neoplasm. J. Neurosurg., 78: 767-775, 1993.
    • (1993) J. Neurosurg. , vol.78 , pp. 767-775
    • Devaux, B.C.1    O'Fallon, J.R.2    Kelly, P.J.3
  • 3
    • 0027415401 scopus 로고
    • Surgical resection and radiotherapy versus biopsy and radiation therapy in the treatment of glioblastoma multiforme
    • Kreth, F. W., Warnke, P. C., Scherement, R., Ostertag, C. B. Surgical resection and radiotherapy versus biopsy and radiation therapy in the treatment of glioblastoma multiforme. J. Neurosurg., 78: 762-766, 1993.
    • (1993) J. Neurosurg. , vol.78 , pp. 762-766
    • Kreth, F.W.1    Warnke, P.C.2    Scherement, R.3    Ostertag, C.B.4
  • 4
    • 0026076377 scopus 로고
    • The relationship between survival and the extent of the resection in patients with supratentorial malignant gliomas
    • Quigley, M. R., and Maroon, J. C. The relationship between survival and the extent of the resection in patients with supratentorial malignant gliomas. Neurosurgery, 29: 385-389, 1991.
    • (1991) Neurosurgery , vol.29 , pp. 385-389
    • Quigley, M.R.1    Maroon, J.C.2
  • 7
    • 0038858397 scopus 로고
    • Chemotherapeutic strategies for high grade astrocytoma of childhood
    • R. J. Packer, W. A. Bleyer, and C. Pochedly (eds.), Philadelphia: Harwood Academics
    • Finlay, J. L. Chemotherapeutic strategies for high grade astrocytoma of childhood. In: R. J. Packer, W. A. Bleyer, and C. Pochedly (eds.), Pediatric Neuro-Oncology, pp. 278-297. Philadelphia: Harwood Academics, 1992.
    • (1992) Pediatric Neuro-Oncology , pp. 278-297
    • Finlay, J.L.1
  • 8
    • 0029588683 scopus 로고
    • Adjuvant and neoadjuvant treatments for primary brain tumors in adults
    • Grossman, S. A., and Norris, L. K. Adjuvant and neoadjuvant treatments for primary brain tumors in adults. Semin. Oncol., 22: 530-539, 1995.
    • (1995) Semin. Oncol. , vol.22 , pp. 530-539
    • Grossman, S.A.1    Norris, L.K.2
  • 9
    • 0030817283 scopus 로고    scopus 로고
    • Chemotherapy of brain tumors
    • Pardos, M. D., and Russo, C. Chemotherapy of brain tumors. Semin. Surg. Oncol., 14: 88-95, 1998.
    • (1998) Semin. Surg. Oncol. , vol.14 , pp. 88-95
    • Pardos, M.D.1    Russo, C.2
  • 10
    • 0030477277 scopus 로고    scopus 로고
    • The role of chemotherapy in recurrent malignant gliomas: An overview
    • Brandes, A. A., and Fiorentino, M. V. The role of chemotherapy in recurrent malignant gliomas: an overview. Cancer Invest., 14: 551-559, 1996.
    • (1996) Cancer Invest. , vol.14 , pp. 551-559
    • Brandes, A.A.1    Fiorentino, M.V.2
  • 11
    • 0009496876 scopus 로고    scopus 로고
    • Neoplasms of the central nervous system
    • J. F. Holland, R. C. Bast, Jr., D. L. Morton, E. Frei, III, D. W. Kufe, and R. R. Weichselbaum (eds.), Baltimore: Williams and Wilkins
    • Pardos, M. D., and Wilson, C. B. Neoplasms of the central nervous system. In: J. F. Holland, R. C. Bast, Jr., D. L. Morton, E. Frei, III, D. W. Kufe, and R. R. Weichselbaum (eds.), Cancer Medicine, Vol I, pp. 1471-1514. Baltimore: Williams and Wilkins, 1997.
    • (1997) Cancer Medicine , vol.1 , pp. 1471-1514
    • Pardos, M.D.1    Wilson, C.B.2
  • 12
    • 0031801528 scopus 로고    scopus 로고
    • 4-(3′-Bromo-4′hydroxylphenyl)-amino-6,7-dimethoxyquinazoline (WHI-P154): A novel quinazoline derivative with potent cytotoxic activity against human glioblastoma cells
    • Narla, R. K., Liu, X., Myers, D. E., and Uckun, F. M. 4-(3′-Bromo-4′hydroxylphenyl)-amino-6,7-dimethoxyquinazoline (WHI-P154): a novel quinazoline derivative with potent cytotoxic activity against human glioblastoma cells. Clin. Cancer Res., 4: 1405-1414, 1998.
    • (1998) Clin. Cancer Res. , vol.4 , pp. 1405-1414
    • Narla, R.K.1    Liu, X.2    Myers, D.E.3    Uckun, F.M.4
  • 15
    • 0029939720 scopus 로고    scopus 로고
    • In vitro inhibition, of cell proliferation, viability, and invasiveness in U87MG human glioblastoma cells by estramustine phosphate
    • Yoshida, D., Piepmeier, J. M., and Teramoto, A. In vitro inhibition, of cell proliferation, viability, and invasiveness in U87MG human glioblastoma cells by estramustine phosphate. Neurosurgery, 39: 360-366, 1996.
    • (1996) Neurosurgery , vol.39 , pp. 360-366
    • Yoshida, D.1    Piepmeier, J.M.2    Teramoto, A.3
  • 16
    • 0021217763 scopus 로고
    • The extracellular matrix of the central nervous system
    • Carbonetto, S. The extracellular matrix of the central nervous system. Trends Neurosci., 7: 382-387, 1984.
    • (1984) Trends Neurosci. , vol.7 , pp. 382-387
    • Carbonetto, S.1
  • 17
    • 0023722254 scopus 로고
    • The role of extracellular matrix of the central and peripheral nervous system: Structure and function
    • Rutka, J. T., Apodaca, G., and Stern, R. The role of extracellular matrix of the central and peripheral nervous system: structure and function. J. Neurosurg., 69: 155-170, 1988.
    • (1988) J. Neurosurg. , vol.69 , pp. 155-170
    • Rutka, J.T.1    Apodaca, G.2    Stern, R.3
  • 18
    • 0027325517 scopus 로고
    • Extracellular matrix 2: Role of extracellular matrix molecules and their receptors in the nervous system
    • Venstrom, K. A., and Reichard, L. F. Extracellular matrix 2: role of extracellular matrix molecules and their receptors in the nervous system. FASEB J., 7: 996-1003, 1993.
    • (1993) FASEB J. , vol.7 , pp. 996-1003
    • Venstrom, K.A.1    Reichard, L.F.2
  • 19
    • 0028098829 scopus 로고
    • Stimulation of tyrosine- and serine-phosphorylation of focal adhesion kinase in mouse 3T3 cells by fibronectin and fibroblast growth factor
    • Hatai, M., Hashi, H., Mogi, A., Soga, H., Yokota, J., and Yaoi, Y. Stimulation of tyrosine- and serine-phosphorylation of focal adhesion kinase in mouse 3T3 cells by fibronectin and fibroblast growth factor. FEBS Lett., 350: 113-116, 1994.
    • (1994) FEBS Lett. , vol.350 , pp. 113-116
    • Hatai, M.1    Hashi, H.2    Mogi, A.3    Soga, H.4    Yokota, J.5    Yaoi, Y.6
  • 20
    • 0029819507 scopus 로고    scopus 로고
    • Insulin-induced tyrosine dephosphorylation of paxillin and focal adhesion kinase requires active phosphotyrosine phosphatase 1D
    • Ouwens, D. M., Mikkers, H. M., van der Zon, G. C., Stein Gerlach, M., Ullrich, A., and Maassen, J. A. Insulin-induced tyrosine dephosphorylation of paxillin and focal adhesion kinase requires active phosphotyrosine phosphatase 1D. Biochem. J., 318: 609-614, 1996.
    • (1996) Biochem. J. , vol.318 , pp. 609-614
    • Ouwens, D.M.1    Mikkers, H.M.2    Van Der Zon, G.C.3    Stein Gerlach, M.4    Ullrich, A.5    Maassen, J.A.6
  • 21
    • 0028122650 scopus 로고
    • Focal adhesion kinase and associated proteins
    • Schaller, M. D., and Parsons, J. T. Focal adhesion kinase and associated proteins. Curr. Opin. Cell Biol., 6: 705-710, 1994.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 705-710
    • Schaller, M.D.1    Parsons, J.T.2
  • 23
    • 0029090940 scopus 로고
    • EGF enhances attachment of metastatic rat mammary adenocarcinoma cell clone MTLn3 to fibronectin and collagen
    • Rohde-Schulz, B., and Lichtner, R. B. EGF enhances attachment of metastatic rat mammary adenocarcinoma cell clone MTLn3 to fibronectin and collagen. Invasion Metastasis, 15: 1-10, 1995.
    • (1995) Invasion Metastasis , vol.15 , pp. 1-10
    • Rohde-Schulz, B.1    Lichtner, R.B.2
  • 25
    • 0030271724 scopus 로고    scopus 로고
    • Epidermal growth factor (EGF) increases the in vitro invasion, motility and adhesion interactions of the primary renal carcinoma cell line, A704
    • Price, J. T., Wilson, H. M., and Haites, N. E. Epidermal growth factor (EGF) increases the in vitro invasion, motility and adhesion interactions of the primary renal carcinoma cell line, A704. Eur. J. Cancer, 32: 1977-1982, 1996.
    • (1996) Eur. J. Cancer , vol.32 , pp. 1977-1982
    • Price, J.T.1    Wilson, H.M.2    Haites, N.E.3
  • 26
    • 0031213544 scopus 로고    scopus 로고
    • Differential effects of EGF and amphiregulin on adhesion molecule expression and migration of colon carcinoma cells
    • Solic, N., and Davies, D. E. Differential effects of EGF and amphiregulin on adhesion molecule expression and migration of colon carcinoma cells. Exp. Cell Res., 234: 465-476, 1997.
    • (1997) Exp. Cell Res. , vol.234 , pp. 465-476
    • Solic, N.1    Davies, D.E.2
  • 27
    • 0025785552 scopus 로고
    • Control of actin polymerization in live and permeabilized fibroblasts
    • Symons, M. H., and Mitchison, T. J. Control of actin polymerization in live and permeabilized fibroblasts. J. Cell Biol., 114: 503-513, 1991.
    • (1991) J. Cell Biol. , vol.114 , pp. 503-513
    • Symons, M.H.1    Mitchison, T.J.2
  • 28
    • 0021684768 scopus 로고
    • Reorganization of actin filament bundles in living fibroblasts
    • Wang, Y. L. Reorganization of actin filament bundles in living fibroblasts. J. Cell Biol., 99: 1478-1485, 1984.
    • (1984) J. Cell Biol. , vol.99 , pp. 1478-1485
    • Wang, Y.L.1
  • 29
    • 0030584089 scopus 로고    scopus 로고
    • Getting membrane flow and the cytoskeleton to cooperate in moving cells
    • Bretcher, M. S. Getting membrane flow and the cytoskeleton to cooperate in moving cells. Cell, 87: 601-606, 1996.
    • (1996) Cell , vol.87 , pp. 601-606
    • Bretcher, M.S.1
  • 30
    • 0030756973 scopus 로고    scopus 로고
    • Role of actin polymerization and adhesion to extracellular matrix in Rac- and Rho-induced cytoskeletal reorganization
    • Machesky, L. M., and Hall, A. Role of actin polymerization and adhesion to extracellular matrix in Rac- and Rho-induced cytoskeletal reorganization. J. Cell Biol., 138: 913-926, 1997.
    • (1997) J. Cell Biol. , vol.138 , pp. 913-926
    • Machesky, L.M.1    Hall, A.2
  • 31
    • 0024150623 scopus 로고
    • Focal adhesions: Transmembrane junctions between the extracellular matrix and the cytoskeleton
    • Burridge, K., Path, K., Kelly, G., and Turner, C. Focal adhesions: transmembrane junctions between the extracellular matrix and the cytoskeleton. Annu. Rev. Cell Biol., 4: 487-525, 1988.
    • (1988) Annu. Rev. Cell Biol. , vol.4 , pp. 487-525
    • Burridge, K.1    Path, K.2    Kelly, G.3    Turner, C.4
  • 33
    • 0024651413 scopus 로고
    • Focal contacts: Transmembrane links between the extracellular matrix and cytoskeleton
    • Burridge, K., and Fath, K. Focal contacts: transmembrane links between the extracellular matrix and cytoskeleton. Bioessays. 10: 104-108, 1989.
    • (1989) Bioessays , vol.10 , pp. 104-108
    • Burridge, K.1    Fath, K.2
  • 34
    • 0031148599 scopus 로고    scopus 로고
    • Cell migration: May the force be with you
    • Schwarzbauer, J. E. Cell migration: may the force be with you. Curr. Biol., 7: 292-294, 1997.
    • (1997) Curr. Biol. , vol.7 , pp. 292-294
    • Schwarzbauer, J.E.1
  • 35
    • 0032472411 scopus 로고    scopus 로고
    • The activity of Src is dispensable for translocation to focal adhesions but controls the turnover of these structures during cell motility
    • Finchman, V. J., and Frame, M. C. The activity of Src is dispensable for translocation to focal adhesions but controls the turnover of these structures during cell motility. EMBO J., 17: 81-92, 1998.
    • (1998) EMBO J. , vol.17 , pp. 81-92
    • Finchman, V.J.1    Frame, M.C.2
  • 36
    • 0028173980 scopus 로고
    • Stable association of pp60src and pp59fyn with the focal adhesion-associated protein tyrosine kinase, pp125FAK
    • Cobb, B. S., Schaller, M. D., Leu, T. H., and Parsons, J. T. Stable association of pp60src and pp59fyn with the focal adhesion-associated protein tyrosine kinase, pp125FAK. Mol. Cell. Biol., 14: 147-155, 1994.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 147-155
    • Cobb, B.S.1    Schaller, M.D.2    Leu, T.H.3    Parsons, J.T.4
  • 37
    • 0029994358 scopus 로고    scopus 로고
    • Integrin-mediated activation of MEK and mitogen-activated protein kinase is independent of Ras
    • Chen, Q., Lin, T. H., Der, C. J., and Juliano, R. L. Integrin-mediated activation of MEK and mitogen-activated protein kinase is independent of Ras. J. Biol. Chem., 271: 18122-18127, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18122-18127
    • Chen, Q.1    Lin, T.H.2    Der, C.J.3    Juliano, R.L.4
  • 39
    • 0028940658 scopus 로고
    • Adhesion-induced tyrosine phosphorylation of the p130 src substrate
    • Fetch, L. A., Bockholt, S. M., Bouton, A., Parsons, J. T., and Burridge, K., Adhesion-induced tyrosine phosphorylation of the p130 src substrate. J. Cell Sci., 108: 1371-1379, 1995.
    • (1995) J. Cell Sci. , vol.108 , pp. 1371-1379
    • Fetch, L.A.1    Bockholt, S.M.2    Bouton, A.3    Parsons, J.T.4    Burridge, K.5
  • 40
    • 0029995797 scopus 로고    scopus 로고
    • Rho-stimulated contractility drives the formation of stress fibers and focal adhesions
    • Chrzanowska-Wodnicka, M., and Burridge, K. Rho-stimulated contractility drives the formation of stress fibers and focal adhesions. J. Cell Biol., 133: 1403-1415, 1996.
    • (1996) J. Cell Biol. , vol.133 , pp. 1403-1415
    • Chrzanowska-Wodnicka, M.1    Burridge, K.2
  • 41
    • 0028954797 scopus 로고
    • Synergistic roles for receptor occupancy and aggregation in integrin transmembrane function
    • Washington DC
    • Miyamoto, S., Akiyama, S. K., and Yamada, K. M. Synergistic roles for receptor occupancy and aggregation in integrin transmembrane function. Science (Washington DC), 267: 883-885, 1995.
    • (1995) Science , vol.267 , pp. 883-885
    • Miyamoto, S.1    Akiyama, S.K.2    Yamada, K.M.3
  • 42
    • 0030453194 scopus 로고    scopus 로고
    • Integrins can collaborate with growth factors for phosphorylation of receptor tyrosine kinases and MAP kinase activation: Roles of integrin aggregation and activation of receptors
    • Miyamoto, S., Teramoto, H., Gutkind, J. S., and Yamada, K. M. Integrins can collaborate with growth factors for phosphorylation of receptor tyrosine kinases and MAP kinase activation: roles of integrin aggregation and activation of receptors. J. Cell Biol., 135: 1633-1642, 1996.
    • (1996) J. Cell Biol. , vol.135 , pp. 1633-1642
    • Miyamoto, S.1    Teramoto, H.2    Gutkind, J.S.3    Yamada, K.M.4
  • 45
    • 0030697807 scopus 로고    scopus 로고
    • PD153035, a tyrosine kinase inhibitor, prevents epidermal growth factor receptor activation and inhibits growth of cancer cells in a receptor number-dependent manner
    • Bos, M., Mendelsohn, J., Kim, Y., Albanell, J., Fry, D. W., and Baselga, J. PD153035, a tyrosine kinase inhibitor, prevents epidermal growth factor receptor activation and inhibits growth of cancer cells in a receptor number-dependent manner. Clin. Cancer Res., 3: 2099-2106, 1997.
    • (1997) Clin. Cancer Res. , vol.3 , pp. 2099-2106
    • Bos, M.1    Mendelsohn, J.2    Kim, Y.3    Albanell, J.4    Fry, D.W.5    Baselga, J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.