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Volumn 263, Issue 1, 2008, Pages 114-121

Molecular mechanism of the inhibitory effect of KS-5 on bFGF-induced angiogenesis in vitro and in vivo

Author keywords

Acridone derivatives; Angiogenesis; Endothelial cells

Indexed keywords

1,7 DIHYDROXY 3 METHOXYACRIDONE; ACRIDONE DERIVATIVE; BASIC FIBROBLAST GROWTH FACTOR; BROXURIDINE; INITIATION FACTOR 4E; KS 5; LACTATE DEHYDROGENASE; MAMMALIAN TARGET OF RAPAMYCIN INHIBITOR; MATRIGEL; MITOGEN ACTIVATED PROTEIN KINASE; PROTEIN KINASE B; S6 KINASE; UNCLASSIFIED DRUG;

EID: 41049106522     PISSN: 03043835     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.canlet.2007.12.028     Document Type: Article
Times cited : (10)

References (32)
  • 1
    • 33947732977 scopus 로고    scopus 로고
    • Angiogenesis: an organizing principle for drug discovery?
    • Folkman J. Angiogenesis: an organizing principle for drug discovery?. Nat. Rev. Drug Discov. 6 (2007) 273-286
    • (2007) Nat. Rev. Drug Discov. , vol.6 , pp. 273-286
    • Folkman, J.1
  • 2
    • 33749615193 scopus 로고    scopus 로고
    • Angiogenesis: health and disease
    • Bikfalvi A. Angiogenesis: health and disease. Ann. Oncol. 17 (2006) x65-x70
    • (2006) Ann. Oncol. , vol.17
    • Bikfalvi, A.1
  • 3
    • 0034772620 scopus 로고    scopus 로고
    • Endogenous inhibitors of angiogenesis
    • Ruhrberg C. Endogenous inhibitors of angiogenesis. J. Cell Sci. 114 (2001) 3215-3216
    • (2001) J. Cell Sci. , vol.114 , pp. 3215-3216
    • Ruhrberg, C.1
  • 5
    • 0034644525 scopus 로고    scopus 로고
    • TOR, a central controller of cell growth
    • Schmelzle T., and Hall M.N. TOR, a central controller of cell growth. Cell 103 (2000) 253-262
    • (2000) Cell , vol.103 , pp. 253-262
    • Schmelzle, T.1    Hall, M.N.2
  • 6
    • 0037097863 scopus 로고    scopus 로고
    • Mammalian cell size is controlled by mTOR and its downstream targets S6K1 and 4EBP1/eIF4E
    • Fingar D.C., Salama S., Tsou C., Harlow E., and Blenis J. Mammalian cell size is controlled by mTOR and its downstream targets S6K1 and 4EBP1/eIF4E. Genes Dev. 16 (2002) 1472-1487
    • (2002) Genes Dev. , vol.16 , pp. 1472-1487
    • Fingar, D.C.1    Salama, S.2    Tsou, C.3    Harlow, E.4    Blenis, J.5
  • 7
    • 0345732640 scopus 로고    scopus 로고
    • mTOR controls cell cycle progression through its cell growth effectors S6K1 and 4E-BP1/eukaryotic translation initiation factor 4E
    • Fingar D.C., Richardson C.J., Tee A.R., Cheatham L., Tsou C., and Blenis J. mTOR controls cell cycle progression through its cell growth effectors S6K1 and 4E-BP1/eukaryotic translation initiation factor 4E. Mol. Cell. Biol. 24 (2004) 200-216
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 200-216
    • Fingar, D.C.1    Richardson, C.J.2    Tee, A.R.3    Cheatham, L.4    Tsou, C.5    Blenis, J.6
  • 8
    • 0033006919 scopus 로고    scopus 로고
    • eIF4E activity is regulated at multiple levels
    • Raught B., and Gingras A.-C. eIF4E activity is regulated at multiple levels. Int. J. Biochem. Cell Biol. 31 (1999) 43-57
    • (1999) Int. J. Biochem. Cell Biol. , vol.31 , pp. 43-57
    • Raught, B.1    Gingras, A.-C.2
  • 9
    • 0033152072 scopus 로고    scopus 로고
    • Cap-dependent translation initiation in eukaryotes is regulated by a molecular mimic of eIF4G
    • Marcotrigiano J., Gingras A.-C., Sonenberg N., and Burley S.K. Cap-dependent translation initiation in eukaryotes is regulated by a molecular mimic of eIF4G. Mol. Cell 3 (1999) 707-716
    • (1999) Mol. Cell , vol.3 , pp. 707-716
    • Marcotrigiano, J.1    Gingras, A.-C.2    Sonenberg, N.3    Burley, S.K.4
  • 11
    • 15044340650 scopus 로고    scopus 로고
    • Distinct signaling events downstream of mTOR cooperate to mediate the effects of amino acids and insulin on initiation factor 4E-binding proteins
    • Wang X., Beugnet A., Murakami M., Yamanaka S., and Proud C.G. Distinct signaling events downstream of mTOR cooperate to mediate the effects of amino acids and insulin on initiation factor 4E-binding proteins. Mol. Cell. Biol. 25 (2005) 2558-2572
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 2558-2572
    • Wang, X.1    Beugnet, A.2    Murakami, M.3    Yamanaka, S.4    Proud, C.G.5
  • 12
    • 33947149528 scopus 로고    scopus 로고
    • Acridine and acridone derivatives, anticancer properties and synthetic methods: Where are we now?
    • Belmont P., Bosson J., Godet T., and Tiano M. Acridine and acridone derivatives, anticancer properties and synthetic methods: Where are we now?. Anti-Cancer Agents Med. Chem. 7 (2007) 139-169
    • (2007) Anti-Cancer Agents Med. Chem. , vol.7 , pp. 139-169
    • Belmont, P.1    Bosson, J.2    Godet, T.3    Tiano, M.4
  • 13
    • 0041631012 scopus 로고    scopus 로고
    • Cell culture replication of herpes simplex virus and or human cytomegalovirus is inhibited by 3,7-dialkoxylated, 1-hydroxyacridone derivatives
    • Lowden C.T., and Bastow K.F. Cell culture replication of herpes simplex virus and or human cytomegalovirus is inhibited by 3,7-dialkoxylated, 1-hydroxyacridone derivatives. Antiviral Res. 59 (2003) 143-154
    • (2003) Antiviral Res. , vol.59 , pp. 143-154
    • Lowden, C.T.1    Bastow, K.F.2
  • 14
    • 8844254694 scopus 로고    scopus 로고
    • New acridone inhibitors of human herpes virus replication
    • Bastow K.F. New acridone inhibitors of human herpes virus replication. Curr. Drug Targets Infect. Disord. 4 (2004) 323-330
    • (2004) Curr. Drug Targets Infect. Disord. , vol.4 , pp. 323-330
    • Bastow, K.F.1
  • 15
    • 0015822275 scopus 로고
    • Culture of human endothelial cells derived from umbilical veins. Identification by morphologic and immunologic criteria
    • Jaffe E.A., Nachman R.L., Becker C.G., and Minick C.R. Culture of human endothelial cells derived from umbilical veins. Identification by morphologic and immunologic criteria. J. Clin. Invest. 52 (1973) 2745-2756
    • (1973) J. Clin. Invest. , vol.52 , pp. 2745-2756
    • Jaffe, E.A.1    Nachman, R.L.2    Becker, C.G.3    Minick, C.R.4
  • 16
    • 0029552290 scopus 로고
    • Protein serine/threonine kinases of the MAPK cascade
    • Graves J.D., Campbell J.S., and Krebs E.G. Protein serine/threonine kinases of the MAPK cascade. Ann. NY Acad. Sci. 766 (1995) 320-343
    • (1995) Ann. NY Acad. Sci. , vol.766 , pp. 320-343
    • Graves, J.D.1    Campbell, J.S.2    Krebs, E.G.3
  • 17
    • 2142759556 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase signalling pathways in tumor progression, invasion and angiogenesis
    • Brader S., and Eccles S.A. Phosphoinositide 3-kinase signalling pathways in tumor progression, invasion and angiogenesis. Tumori. 90 (2004) 2-8
    • (2004) Tumori. , vol.90 , pp. 2-8
    • Brader, S.1    Eccles, S.A.2
  • 18
    • 0030576517 scopus 로고    scopus 로고
    • Patterns and emerging mechanisms of the angiogenic switch during tumorigenesis
    • Hanahan D., and Folkman J. Patterns and emerging mechanisms of the angiogenic switch during tumorigenesis. Cell 86 (1996) 353-364
    • (1996) Cell , vol.86 , pp. 353-364
    • Hanahan, D.1    Folkman, J.2
  • 19
    • 0032815701 scopus 로고    scopus 로고
    • Roles of extracellular signal-regulated kinase 1/2 and p38 mitogen-activated protein kinase in the signal transduction of basic fibroblast growth factor in endothelial cells during angiogenesis
    • Tanaka K., Abe M., and Sato Y. Roles of extracellular signal-regulated kinase 1/2 and p38 mitogen-activated protein kinase in the signal transduction of basic fibroblast growth factor in endothelial cells during angiogenesis. Jpn. J. Cancer Res. 90 (1999) 647-654
    • (1999) Jpn. J. Cancer Res. , vol.90 , pp. 647-654
    • Tanaka, K.1    Abe, M.2    Sato, Y.3
  • 20
    • 0035313488 scopus 로고    scopus 로고
    • FGF and VEGF function in angiogenesis: signalling pathways, biological responses and therapeutic inhibition
    • Cross M.J., and Claesson-Welsh L. FGF and VEGF function in angiogenesis: signalling pathways, biological responses and therapeutic inhibition. Trends Pharmacol. Sci. 22 (2001) 201-207
    • (2001) Trends Pharmacol. Sci. , vol.22 , pp. 201-207
    • Cross, M.J.1    Claesson-Welsh, L.2
  • 23
    • 0034652115 scopus 로고    scopus 로고
    • Survival function of ERK1/2 as an IL-3 activated, staurosporine-resistant Bcl2 kinases
    • Deng X., Ruvolo P., Carr B., and May Jr. W.S. Survival function of ERK1/2 as an IL-3 activated, staurosporine-resistant Bcl2 kinases. Proc. Natl. Acad. USA 97 (2000) 1578-1583
    • (2000) Proc. Natl. Acad. USA , vol.97 , pp. 1578-1583
    • Deng, X.1    Ruvolo, P.2    Carr, B.3    May Jr., W.S.4
  • 24
    • 1842739136 scopus 로고    scopus 로고
    • Regulation of Bcl2 phosphorylation and potential significance for leukemic cell chemoresistance
    • Deng X., Kornblau S.M., Ruvulo P.P., and May Jr. W.S. Regulation of Bcl2 phosphorylation and potential significance for leukemic cell chemoresistance. J. Natl. Cancer Inst. Monogr. 28 (2001) 30-37
    • (2001) J. Natl. Cancer Inst. Monogr. , vol.28 , pp. 30-37
    • Deng, X.1    Kornblau, S.M.2    Ruvulo, P.P.3    May Jr., W.S.4
  • 25
    • 2442466927 scopus 로고    scopus 로고
    • Cap-dependent and cap-independent translation in eukaryotic systems
    • Merrick W.C. Cap-dependent and cap-independent translation in eukaryotic systems. Gene 332 (2004) 1-11
    • (2004) Gene , vol.332 , pp. 1-11
    • Merrick, W.C.1
  • 26
    • 33750044299 scopus 로고    scopus 로고
    • When translation meets transformation: the mTOR story
    • Averous J., and Proud C.G. When translation meets transformation: the mTOR story. Oncogene 25 (2006) 6423-6435
    • (2006) Oncogene , vol.25 , pp. 6423-6435
    • Averous, J.1    Proud, C.G.2
  • 27
    • 2342489456 scopus 로고    scopus 로고
    • eIF-4E expression and its role in malignancies and metastases
    • De Benedetti A., and Graff J.R. eIF-4E expression and its role in malignancies and metastases. Oncogene 23 (2004) 3189-3199
    • (2004) Oncogene , vol.23 , pp. 3189-3199
    • De Benedetti, A.1    Graff, J.R.2
  • 28
    • 0027969060 scopus 로고
    • Chromatographic resolution of in vivo phosphorylated and nonphosphorylated eukaryotic translation initiation factor eIF-4E: increased cap affinity of the phosphorylated form
    • Minich W.B., Balasta M.L., Goss D.J., and Rhoads R.E. Chromatographic resolution of in vivo phosphorylated and nonphosphorylated eukaryotic translation initiation factor eIF-4E: increased cap affinity of the phosphorylated form. Proc. Natl. Acad. USA 91 (1994) 7668-7672
    • (1994) Proc. Natl. Acad. USA , vol.91 , pp. 7668-7672
    • Minich, W.B.1    Balasta, M.L.2    Goss, D.J.3    Rhoads, R.E.4
  • 29
    • 0037373346 scopus 로고    scopus 로고
    • The C terminus of initiation factor 4E-binding protein 1 contains multiple regulatory features that influence its function and phosphorylation
    • Wang X., Li W., Parra J.L., Beugnet A., and Proud C.G. The C terminus of initiation factor 4E-binding protein 1 contains multiple regulatory features that influence its function and phosphorylation. Mol. Cell. Biol. 23 (2003) 1546-1557
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 1546-1557
    • Wang, X.1    Li, W.2    Parra, J.L.3    Beugnet, A.4    Proud, C.G.5
  • 31
    • 0041440927 scopus 로고    scopus 로고
    • Fibroblast growth factor-2 (FGF-2) induces vascular endothelial growth factor (VEGF) expression in the endothelial cells of forming capillaries: An autocrine mechanism contributing to angiogenesis
    • Seghezzi G., Patel S., Ren C.J., Gualandris A., Pintucci G., Robbins E.S., Shapiro R.L., Galloway A.C., Rifkin D.B., and Mignatti P. Fibroblast growth factor-2 (FGF-2) induces vascular endothelial growth factor (VEGF) expression in the endothelial cells of forming capillaries: An autocrine mechanism contributing to angiogenesis. J. Cell Biol. 141 (1998) 1659-1673
    • (1998) J. Cell Biol. , vol.141 , pp. 1659-1673
    • Seghezzi, G.1    Patel, S.2    Ren, C.J.3    Gualandris, A.4    Pintucci, G.5    Robbins, E.S.6    Shapiro, R.L.7    Galloway, A.C.8    Rifkin, D.B.9    Mignatti, P.10
  • 32
    • 0032911084 scopus 로고    scopus 로고
    • Basic fibroblast growth factor induces expression of VEGF receptor KDR through a protein kinase C and p44/p42 mitogen-activated protein kinase-dependent pathway
    • Hata Y., Rook S.L., and Aiello L.P. Basic fibroblast growth factor induces expression of VEGF receptor KDR through a protein kinase C and p44/p42 mitogen-activated protein kinase-dependent pathway. Diabetes 48 (1999) 1145-1155
    • (1999) Diabetes , vol.48 , pp. 1145-1155
    • Hata, Y.1    Rook, S.L.2    Aiello, L.P.3


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