메뉴 건너뛰기




Volumn 34, Issue 31, 2015, Pages 4078-4088

Neutralizing the EGF receptor in glioblastoma cells stimulates cell migration by activating uPAR-initiated cell signaling

Author keywords

[No Author keywords available]

Indexed keywords

CRK ASSOCIATED SUBSTRATE PROTEIN; DASATINIB; EPIDERMAL GROWTH FACTOR RECEPTOR; GEFITINIB; RNA; UROKINASE RECEPTOR; VASCULOTROPIN RECEPTOR; EPIDERMAL GROWTH FACTOR RECEPTOR VIII; PROTEIN TYROSINE KINASE; QUINAZOLINE DERIVATIVE; SMALL INTERFERING RNA;

EID: 84938551652     PISSN: 09509232     EISSN: 14765594     Source Type: Journal    
DOI: 10.1038/onc.2014.336     Document Type: Article
Times cited : (18)

References (67)
  • 1
    • 21344470873 scopus 로고    scopus 로고
    • Lyn kinase activity is the predominant cellular SRC kinase activity in glioblastoma tumor cells
    • Stettner MR, Wang W, Nabors LB, Bharara S, Flynn DC, Grammer JR et al. Lyn kinase activity is the predominant cellular SRC kinase activity in glioblastoma tumor cells. Cancer Res 2005; 65: 5535-5543.
    • (2005) Cancer Res , vol.65 , pp. 5535-5543
    • Stettner, M.R.1    Wang, W.2    Nabors, L.B.3    Bharara, S.4    Flynn, D.C.5    Grammer, J.R.6
  • 2
    • 60149089005 scopus 로고    scopus 로고
    • Bead-based profiling of tyrosine kinase phosphorylation identifies SRC as a potential target for glioblastoma therapy
    • Du J, Bernasconi P, Clauser KR, Mani DR, Finn SP, Beroukhim R et al. Bead-based profiling of tyrosine kinase phosphorylation identifies SRC as a potential target for glioblastoma therapy. Nat Biotechnol 2009; 27: 77-83.
    • (2009) Nat Biotechnol , vol.27 , pp. 77-83
    • Du, J.1    Bernasconi, P.2    Clauser, K.R.3    Mani, D.R.4    Finn, S.P.5    Beroukhim, R.6
  • 3
    • 70149112112 scopus 로고    scopus 로고
    • Fyn and src are effectors of oncogenic epidermal growth factor receptor signaling in glioblastoma patients
    • Lu KV, Zhu S, Cvrljevic A, Huang TT, Sarkaria S, Ahkavan D et al. Fyn and Src are effectors of oncogenic epidermal growth factor receptor signaling in glioblastoma patients. Cancer Res 2009; 69: 6889-6898.
    • (2009) Cancer Res , vol.69 , pp. 6889-6898
    • Lu, K.V.1    Zhu, S.2    Cvrljevic, A.3    Huang, T.T.4    Sarkaria, S.5    Ahkavan, D.6
  • 4
    • 77957937844 scopus 로고    scopus 로고
    • Targeting src in glioblastoma tumors and brain metastases: Rationale and preclinical studies
    • Ahluwalia MS, de Groot J, Liu WM, Gladson CL. Targeting Src in glioblastoma tumors and brain metastases: rationale and preclinical studies. Cancer Lett 2010; 298: 139-149.
    • (2010) Cancer Lett , vol.298 , pp. 139-149
    • Ahluwalia, M.S.1    De Groot, J.2    Liu, W.M.3    Gladson, C.L.4
  • 5
    • 2942618768 scopus 로고    scopus 로고
    • A renaissance for SRC
    • Yeatman TJ. A renaissance for SRC. Nat Rev Cancer 2004; 4: 470-480.
    • (2004) Nat Rev Cancer , vol.4 , pp. 470-480
    • Yeatman, T.J.1
  • 6
    • 15544389207 scopus 로고    scopus 로고
    • Novel insights into c-src
    • Alper O, Bowden ET. Novel insights into c-Src. Curr Pharm Des 2005; 11: 1119-1130.
    • (2005) Curr Pharm des , vol.11 , pp. 1119-1130
    • Alper, O.1    Bowden, E.T.2
  • 7
    • 0033522510 scopus 로고    scopus 로고
    • Src family kinases are required for integrin but not PDGFR signal transduction
    • Klinghoffer RA, Sachsenmaier C, Cooper JA, Soriano P. Src family kinases are required for integrin but not PDGFR signal transduction. EMBO J 1999; 18: 2459-2471.
    • (1999) EMBO J , vol.18 , pp. 2459-2471
    • Klinghoffer, R.A.1    Sachsenmaier, C.2    Cooper, J.A.3    Soriano, P.4
  • 8
    • 0033175564 scopus 로고    scopus 로고
    • Selective regulation of integrin-cytoskeleton interactions by the tyrosine kinase src
    • Felsenfeld DP, Schwartzberg PL, Venegas A, Tse R, Sheetz MP. Selective regulation of integrin-cytoskeleton interactions by the tyrosine kinase Src. Nat Cell Biol 1999; 1: 200-206.
    • (1999) Nat Cell Biol , vol.1 , pp. 200-206
    • Felsenfeld, D.P.1    Schwartzberg, P.L.2    Venegas, A.3    Tse, R.4    Sheetz, M.P.5
  • 9
    • 0034268796 scopus 로고    scopus 로고
    • Src tyrosine kinase is a novel directeffector of G proteins
    • Ma YC, Huang J, Ali S, Lowry W, Huang XY. Src tyrosine kinase is a novel directeffector of G proteins. Cell 2000; 102: 635-646.
    • (2000) Cell , vol.102 , pp. 635-646
    • Ma, Y.C.1    Huang, J.2    Ali, S.3    Lowry, W.4    Huang, X.Y.5
  • 10
    • 0035887309 scopus 로고    scopus 로고
    • Src transduces erythropoietin-induced differentiation signals through phosphatidylinositol 3-kinase
    • Kubota Y, Tanaka T, Kitanaka A, Ohnishi H, Okutani Y, Waki M et al. Src transduces erythropoietin-induced differentiation signals through phosphatidylinositol 3-kinase. EMBO J 2001; 20: 5666-5677.
    • (2001) EMBO J , vol.20 , pp. 5666-5677
    • Kubota, Y.1    Tanaka, T.2    Kitanaka, A.3    Ohnishi, H.4    Okutani, Y.5    Waki, M.6
  • 11
    • 0141668894 scopus 로고    scopus 로고
    • Rac1 function is required for src-induced transformation. Evidence of a role for tiam1 and vav2 in rac activation by src
    • Servitja JM, Marinissen MJ, Sodhi A, Bustelo XR, Gutkind JS. Rac1 function is required for Src-induced transformation. Evidence of a role for Tiam1 and Vav2 in Rac activation by Src. J Biol Chem 2003; 278: 34339-34346.
    • (2003) J Biol Chem , vol.278 , pp. 34339-34346
    • Servitja, J.M.1    Marinissen, M.J.2    Sodhi, A.3    Bustelo, X.R.4    Gutkind, J.S.5
  • 12
    • 0033573921 scopus 로고    scopus 로고
    • Mechanism of biological synergy between cellular src and epidermal growth factor receptor
    • Tice DA, Biscardi JS, Nickles AL, Parsons SJ. Mechanism of biological synergy between cellular Src and epidermal growth factor receptor. Proc Natl Acad Sci USA 1999; 96: 1415-1420.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 1415-1420
    • Tice, D.A.1    Biscardi, J.S.2    Nickles, A.L.3    Parsons, S.J.4
  • 14
    • 34247340196 scopus 로고    scopus 로고
    • Urokinase receptor primes cells to proliferate in response to epidermal growth factor
    • Jo M, Thomas K, Takimoto S, Gaultier A, Hsieh E, Lester R et al. Urokinase receptor primes cells to proliferate in response to epidermal growth factor. Oncogene 2007; 26: 2585-2594.
    • (2007) Oncogene , vol.26 , pp. 2585-2594
    • Jo, M.1    Thomas, K.2    Takimoto, S.3    Gaultier, A.4    Hsieh, E.5    Lester, R.6
  • 15
    • 80053135166 scopus 로고    scopus 로고
    • Crosstalk between the urokinase-type plasminogen activator receptor and EGF receptor variant III supports survival and growth of glioblastoma cells
    • Hu J, Jo M, Cavenee WK, Furnari F, Vanden Berg SR, Gonias SL. Crosstalk between the urokinase-type plasminogen activator receptor and EGF receptor variant III supports survival and growth of glioblastoma cells. Proc Natl Acad Sci USA 2011; 108: 15984-15989.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 15984-15989
    • Hu, J.1    Jo, M.2    Cavenee, W.K.3    Furnari, F.4    Vanden Berg, S.R.5    Gonias, S.L.6
  • 16
    • 79952386422 scopus 로고    scopus 로고
    • Analysis of phosphotyrosine signaling in glioblastoma identifies STAT5 as a novel downstream target of delta EGFR
    • Chumbalkar V, Latha K, Hwang Y, Maywald R, Hawley L, Sawaya R et al. Analysis of phosphotyrosine signaling in glioblastoma identifies STAT5 as a novel downstream target of Delta EGFR. J Proteome Res 2011; 10: 1343-1352.
    • (2011) J Proteome Res , vol.10 , pp. 1343-1352
    • Chumbalkar, V.1    Latha, K.2    Hwang, Y.3    Maywald, R.4    Hawley, L.5    Sawaya, R.6
  • 17
    • 3543025709 scopus 로고    scopus 로고
    • Phosphorylation of Y845 on the epidermal growth factor receptor mediates binding to the mitochondrial protein cytochrome c oxidase subunit II
    • Boerner JL, Demory ML, Silva C, Parsons SJ. Phosphorylation of Y845 on the epidermal growth factor receptor mediates binding to the mitochondrial protein cytochrome c oxidase subunit II. Mol Cell Biol 2004; 24: 7059-7071.
    • (2004) Mol Cell Biol , vol.24 , pp. 7059-7071
    • Boerner, J.L.1    Demory, M.L.2    Silva, C.3    Parsons, S.J.4
  • 18
    • 0021932240 scopus 로고
    • Amplification, enhanced expression and possible rearrangement of EGF receptor gene in primary human brain tumours of glial origin
    • Libermann TA, Nusbaum HR, Razon N, Kris R, Lax I, Soreq H et al. Amplification, enhanced expression and possible rearrangement of EGF receptor gene in primary human brain tumours of glial origin. Nature 1985; 313: 144-147.
    • (1985) Nature , vol.313 , pp. 144-147
    • Libermann, T.A.1    Nusbaum, H.R.2    Razon, N.3    Kris, R.4    Lax, I.5    Soreq, H.6
  • 19
    • 0028641258 scopus 로고
    • Amplification and differential expression of members of the erbB-gene family in human glioblastoma
    • Schlegel J, Stumm G, Brandle K, Merdes A, Mechtersheimer G, Hynes NE et al. Amplification and differential expression of members of the erbB-gene family in human glioblastoma. J Neurooncol 1994; 22: 201-207.
    • (1994) J Neurooncol , vol.22 , pp. 201-207
    • Schlegel, J.1    Stumm, G.2    Brandle, K.3    Merdes, A.4    Mechtersheimer, G.5    Hynes, N.E.6
  • 20
    • 0028097815 scopus 로고
    • Amplification of the epidermal-growth-factor-receptor gene correlates with different growth behaviour in human glioblastoma
    • Schlegel J, Merdes A, Stumm G, Albert FK, Forsting M, Hynes N et al. Amplification of the epidermal-growth-factor-receptor gene correlates with different growth behaviour in human glioblastoma. Int J Cancer 1994; 56: 72-77.
    • (1994) Int J Cancer , vol.56 , pp. 72-77
    • Schlegel, J.1    Merdes, A.2    Stumm, G.3    Albert, F.K.4    Forsting, M.5    Hynes, N.6
  • 21
    • 0025114687 scopus 로고
    • Identical splicing of aberrant epidermal growth factor receptor transcripts from amplified rearranged genes in human glioblastomas
    • Sugawa N, Ekstrand AJ, James CD, Collins VP. Identical splicing of aberrant epidermal growth factor receptor transcripts from amplified rearranged genes in human glioblastomas. Proc Natl Acad Sci USA 1990; 87: 8602-8606.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 8602-8606
    • Sugawa, N.1    Ekstrand, A.J.2    James, C.D.3    Collins, V.P.4
  • 22
    • 14444288522 scopus 로고    scopus 로고
    • The enhanced tumorigenic activity of a mutant epidermal growth factor receptor common in human cancers is mediated by threshold levels of constitutive tyrosine phosphorylation and unattenuated signaling
    • Huang HS, Nagane M, Klingbeil CK, Lin H, Nishikawa R, Ji XD et al. The enhanced tumorigenic activity of a mutant epidermal growth factor receptor common in human cancers is mediated by threshold levels of constitutive tyrosine phosphorylation and unattenuated signaling. J Biol Chem 1997; 272: 2927-2935.
    • (1997) J Biol Chem , vol.272 , pp. 2927-2935
    • Huang, H.S.1    Nagane, M.2    Klingbeil, C.K.3    Lin, H.4    Nishikawa, R.5    Ji, X.D.6
  • 23
    • 0036906177 scopus 로고    scopus 로고
    • UPAR: A versatile signalling orchestrator
    • Blasi F, Carmeliet P. uPAR: a versatile signalling orchestrator. Nat Rev Mol Cell Biol 2002; 3: 932-943.
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 932-943
    • Blasi, F.1    Carmeliet, P.2
  • 24
    • 0036596352 scopus 로고    scopus 로고
    • EGFR is a transducer of the urokinase receptor initiated signal that is required for in vivo growth of a human carcinoma
    • Liu D, Aguirre Ghiso J, Estrada Y, Ossowski L. EGFR is a transducer of the urokinase receptor initiated signal that is required for in vivo growth of a human carcinoma. Cancer Cell 2002; 1: 445-457.
    • (2002) Cancer Cell , vol.1 , pp. 445-457
    • Liu, D.1    Aguirre Ghiso, J.2    Estrada, Y.3    Ossowski, L.4
  • 25
    • 0028925552 scopus 로고
    • Urokinase plasminogen activator receptor, beta 2-integrins, and src-kinases within a single receptor complex of human monocytes
    • Bohuslav J, Horejsi V, Hansmann C, Stockl J, Weidle UH, Majdic O et al. Urokinase plasminogen activator receptor, beta 2-integrins, and Src-kinases within a single receptor complex of human monocytes. J Exp Med 1995; 181: 1381-1390.
    • (1995) J Exp Med , vol.181 , pp. 1381-1390
    • Bohuslav, J.1    Horejsi, V.2    Hansmann, C.3    Stockl, J.4    Weidle, U.H.5    Majdic, O.6
  • 26
    • 0033566354 scopus 로고    scopus 로고
    • Src-dependence and pertussis-toxin sensitivity of urokinase receptor-dependent chemotaxis and cytoskeleton reorganization in rat smooth muscle cells
    • Degryse B, Resnati M, Rabbani SA, Villa A, Fazioli F, Blasi F. Src-dependence and pertussis-toxin sensitivity of urokinase receptor-dependent chemotaxis and cytoskeleton reorganization in rat smooth muscle cells. Blood 1999; 94: 649-662.
    • (1999) Blood , vol.94 , pp. 649-662
    • Degryse, B.1    Resnati, M.2    Rabbani, S.A.3    Villa, A.4    Fazioli, F.5    Blasi, F.6
  • 27
    • 0034705424 scopus 로고    scopus 로고
    • Urokinase-type plasminogen activator stimulates the ras/Extracellular signalregulated kinase (ERK) signaling pathway and MCF-7 cell migration by a mechanism that requires focal adhesion kinase, src, and shc. Rapid dissociation of GRB2/Sos-shc complex is associated with the transient phosphorylation of ERK in urokinase-treated cells
    • Nguyen DH, Webb DJ, Catling AD, Song Q, Dhakephalkar A, Weber MJ et al. Urokinase-type plasminogen activator stimulates the Ras/Extracellular signalregulated kinase (ERK) signaling pathway and MCF-7 cell migration by a mechanism that requires focal adhesion kinase, Src, and Shc. Rapid dissociation of GRB2/Sos-Shc complex is associated with the transient phosphorylation of ERK in urokinase-treated cells. J Biol Chem 2000; 275: 19382-19388.
    • (2000) J Biol Chem , vol.275 , pp. 19382-19388
    • Nguyen, D.H.1    Webb, D.J.2    Catling, A.D.3    Song, Q.4    Dhakephalkar, A.5    Weber, M.J.6
  • 28
    • 50249145697 scopus 로고    scopus 로고
    • UPAR promotes formation of the p130Cas-crk complex to activate rac through DOCK180
    • Smith HW, Marra P, Marshall CJ. uPAR promotes formation of the p130Cas-Crk complex to activate Rac through DOCK180. J Cell Biol 2008; 182: 777-790.
    • (2008) J Cell Biol , vol.182 , pp. 777-790
    • Smith, H.W.1    Marra, P.2    Marshall, C.J.3
  • 29
    • 84870449601 scopus 로고    scopus 로고
    • Urinary-type plasminogen activator receptor (uPAR) modulates oral cancer cell behavior with alteration in p130cas
    • Shi Z, Liu Y, Johnson JJ, Stack MS. Urinary-type plasminogen activator receptor (uPAR) modulates oral cancer cell behavior with alteration in p130cas. Mol Cel Biochem 2011; 357: 151-161.
    • (2011) Mol Cel Biochem , vol.357 , pp. 151-161
    • Shi, Z.1    Liu, Y.2    Johnson, J.J.3    Stack, M.S.4
  • 30
    • 0028171075 scopus 로고
    • Epidermal-growth-factor-dependent activation of the srcfamily kinases
    • Osherov N, Levitzki A. Epidermal-growth-factor-dependent activation of the srcfamily kinases. European Journal of Biochemistry/FEBS 1994; 225: 1047-1053.
    • (1994) European Journal of Biochemistry/FEBS , vol.225 , pp. 1047-1053
    • Osherov, N.1    Levitzki, A.2
  • 31
    • 0033525759 scopus 로고    scopus 로고
    • EGF receptor signaling stimulates src kinase phosphorylation of clathrin, influencing clathrin redistribution and EGF uptake
    • Wilde A, Beattie EC, Lem L, Riethof DA, Liu SH, Mobley WC et al. EGF receptor signaling stimulates Src kinase phosphorylation of clathrin, influencing clathrin redistribution and EGF uptake. Cell 1999; 96: 677-687.
    • (1999) Cell , vol.96 , pp. 677-687
    • Wilde, A.1    Beattie, E.C.2    Lem, L.3    Riethof, D.A.4    Liu, S.H.5    Mobley, W.C.6
  • 32
    • 0141544141 scopus 로고
    • Potential positive and negative autoregulation of p60c-src by intermolecular autophosphorylation
    • Cooper JA, MacAuley A. Potential positive and negative autoregulation of p60c-src by intermolecular autophosphorylation. Proc Natl Acad Sci USA 1988; 85: 4232-4236.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 4232-4236
    • Cooper, J.A.1    MacAuley, A.2
  • 34
    • 34247218483 scopus 로고    scopus 로고
    • Gefitinib in patients with progressive high-grade gliomas: A multicentre phase II study by gruppo Italiano cooperativo di neuro-oncologia (GICNO)
    • Franceschi E, Cavallo G, Lonardi S, Magrini E, Tosoni A, Grosso D et al. Gefitinib in patients with progressive high-grade gliomas: a multicentre phase II study by Gruppo Italiano Cooperativo di Neuro-Oncologia (GICNO). Br J Cancer 2007; 96: 1047-1051.
    • (2007) Br J Cancer , vol.96 , pp. 1047-1051
    • Franceschi, E.1    Cavallo, G.2    Lonardi, S.3    Magrini, E.4    Tosoni, A.5    Grosso, D.6
  • 37
  • 38
    • 84878172399 scopus 로고    scopus 로고
    • Cellular functions regulated by phosphorylation of EGFR on tyr845
    • Sato K. Cellular functions regulated by phosphorylation of EGFR on Tyr845. Int J Mol Sci 2013; 14: 10761-10790.
    • (2013) Int J Mol Sci , vol.14 , pp. 10761-10790
    • Sato, K.1
  • 39
    • 0023649622 scopus 로고
    • Tyrosine phosphorylation regulates the biochemical and biological properties of pp60c-src
    • Piwnica-Worms H, Saunders KB, Roberts TM, Smith AE, Cheng SH. Tyrosine phosphorylation regulates the biochemical and biological properties of pp60c-src. Cell 1987; 49: 75-82.
    • (1987) Cell , vol.49 , pp. 75-82
    • Piwnica-Worms, H.1    Saunders, K.B.2    Roberts, T.M.3    Smith, A.E.4    Cheng, S.H.5
  • 40
    • 34147184365 scopus 로고    scopus 로고
    • Identification of molecular characteristics correlated with glioblastoma sensitivity to EGFR kinase inhibition through use of an intracranial xenograft test panel
    • Sarkaria JN, Yang L, Grogan PT, Kitange GJ, Carlson BL, Schroeder MA et al. Identification of molecular characteristics correlated with glioblastoma sensitivity to EGFR kinase inhibition through use of an intracranial xenograft test panel. Mol Cancer Ther 2007; 6: 1167-1174.
    • (2007) Mol Cancer Ther , vol.6 , pp. 1167-1174
    • Sarkaria, J.N.1    Yang, L.2    Grogan, P.T.3    Kitange, G.J.4    Carlson, B.L.5    Schroeder, M.A.6
  • 41
    • 0032566763 scopus 로고    scopus 로고
    • Quantum dot bioconjugates for ultrasensitive nonisotopic detection
    • Chan WC, Nie S. Quantum dot bioconjugates for ultrasensitive nonisotopic detection. Science 1998; 281: 2016-2018.
    • (1998) Science , vol.281 , pp. 2016-2018
    • Chan, W.C.1    Nie, S.2
  • 42
    • 77249101567 scopus 로고    scopus 로고
    • Mutant EGFR is required for maintenance of glioma growth in vivo, and its ablation leads to escape from receptor dependence
    • Mukasa A, Wykosky J, Ligon KL, Chin L, Cavenee WK, Furnari F. Mutant EGFR is required for maintenance of glioma growth in vivo, and its ablation leads to escape from receptor dependence. Proc Natl Acad Sci USA 2010; 107: 2616-2621.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 2616-2621
    • Mukasa, A.1    Wykosky, J.2    Ligon, K.L.3    Chin, L.4    Cavenee, W.K.5    Furnari, F.6
  • 43
    • 0033549558 scopus 로고    scopus 로고
    • Myosin light chain kinase functions downstream of ras/ERK to promote migration of urokinase-type plasminogen activator-stimulated cells in an integrinselective manner
    • Nguyen D, Catling A, Webb D, Sankovic M, Walker L, Somlyo A et al. Myosin light chain kinase functions downstream of Ras/ERK to promote migration of urokinase-type plasminogen activator-stimulated cells in an integrinselective manner. J Cell Biol 1999; 146: 149-164.
    • (1999) J Cell Biol , vol.146 , pp. 149-164
    • Nguyen, D.1    Catling, A.2    Webb, D.3    Sankovic, M.4    Walker, L.5    Somlyo, A.6
  • 44
    • 0035911966 scopus 로고    scopus 로고
    • Rac mediates cytoskeletal rearrangements and increased cell motility induced by urokinase-type plasminogen activator receptor binding to vitronectin
    • Kjoller L, Hall A. Rac mediates cytoskeletal rearrangements and increased cell motility induced by urokinase-type plasminogen activator receptor binding to vitronectin. J Cell Biol 2001; 152: 1145-1157.
    • (2001) J Cell Biol , vol.152 , pp. 1145-1157
    • Kjoller, L.1    Hall, A.2
  • 45
    • 0037164811 scopus 로고    scopus 로고
    • Regulation of rac1 activation by the low density lipoprotein receptor-related protein
    • Ma Z, Thomas KS, Webb DJ, Moravec R, Salicioni AM, Mars WM et al. Regulation of Rac1 activation by the low density lipoprotein receptor-related protein. J Cell Biol 2002; 159: 1061-1070.
    • (2002) J Cell Biol , vol.159 , pp. 1061-1070
    • Ma, Z.1    Thomas, K.S.2    Webb, D.J.3    Moravec, R.4    Salicioni, A.M.5    Mars, W.M.6
  • 46
    • 67649910151 scopus 로고    scopus 로고
    • The urokinase receptor promotes cancer metastasis independently of urokinase-type plasminogen activator in mice
    • Jo M, Takimoto S, Montel V, Gonias S. The urokinase receptor promotes cancer metastasis independently of urokinase-type plasminogen activator in mice. Amer J Pathol 2009; 175: 190-200.
    • (2009) Amer J Pathol , vol.175 , pp. 190-200
    • Jo, M.1    Takimoto, S.2    Montel, V.3    Gonias, S.4
  • 47
    • 84862650960 scopus 로고    scopus 로고
    • A transformation in the mechanism by which the urokinase receptor signals provides a selection advantage for estrogen receptor-expressing breast cancer cells in the absence of estrogen
    • Eastman BM, Jo M, Webb DL, Takimoto S, Gonias SL. A transformation in the mechanism by which the urokinase receptor signals provides a selection advantage for estrogen receptor-expressing breast cancer cells in the absence of estrogen. Cell Signal 2012; 24: 1847-1855.
    • (2012) Cell Signal , vol.24 , pp. 1847-1855
    • Eastman, B.M.1    Jo, M.2    Webb, D.L.3    Takimoto, S.4    Gonias, S.L.5
  • 49
    • 0029961912 scopus 로고    scopus 로고
    • A common mutant epidermal growth factor receptor confers enhanced tumorigenicity on human glioblastoma cells by increasing proliferation and reducing apoptosis
    • Nagane M, Coufal F, Lin H, Bogler O, Cavenee WK, Huang HJ. A common mutant epidermal growth factor receptor confers enhanced tumorigenicity on human glioblastoma cells by increasing proliferation and reducing apoptosis. Cancer Res 1996; 56: 5079-5086.
    • (1996) Cancer Res , vol.56 , pp. 5079-5086
    • Nagane, M.1    Coufal, F.2    Lin, H.3    Bogler, O.4    Cavenee, W.K.5    Huang, H.J.6
  • 50
    • 0030027206 scopus 로고    scopus 로고
    • A common region of loss of heterozygosity in wilms' tumor and embryonal rhabdomyosarcoma distal to the D11S988 locus on chromosome 11p15.5
    • Besnard-Guerin C, Newsham I, Winqvist R, Cavenee WK. A common region of loss of heterozygosity in Wilms' tumor and embryonal rhabdomyosarcoma distal to the D11S988 locus on chromosome 11p15.5. Hum Genet 1996; 97: 163-170.
    • (1996) Hum Genet , vol.97 , pp. 163-170
    • Besnard-Guerin, C.1    Newsham, I.2    Winqvist, R.3    Cavenee, W.K.4
  • 51
    • 77955911497 scopus 로고    scopus 로고
    • Tumor heterogeneity is an active process maintained by a mutant EGFR-induced cytokine circuit in glioblastoma
    • Inda M, Bonavia R, Mukasa A, Narita Y, Sah D, Vandenberg S et al. Tumor heterogeneity is an active process maintained by a mutant EGFR-induced cytokine circuit in glioblastoma. Genes Dev 2010; 24: 1731-1745.
    • (2010) Genes Dev , vol.24 , pp. 1731-1745
    • Inda, M.1    Bonavia, R.2    Mukasa, A.3    Narita, Y.4    Sah, D.5    Vandenberg, S.6
  • 52
    • 77953573187 scopus 로고    scopus 로고
    • Escape from targeted inhibition: The dark side of kinase inhibitor therapy
    • Wykosky J, Mukasa A, Furnari F, Cavenee WK. Escape from targeted inhibition: the dark side of kinase inhibitor therapy. Cell Cycle 2010; 9: 1661-1662.
    • (2010) Cell Cycle , vol.9 , pp. 1661-1662
    • Wykosky, J.1    Mukasa, A.2    Furnari, F.3    Cavenee, W.K.4
  • 53
    • 20444478292 scopus 로고    scopus 로고
    • Dynamic assembly of the urokinase-type plasminogen activator signaling receptor complex determines the mitogenic activity of urokinase-type plasminogen activator
    • Jo M, Thomas K, Marozkina N, Amin T, Silva C, Parsons S et al. Dynamic assembly of the urokinase-type plasminogen activator signaling receptor complex determines the mitogenic activity of urokinase-type plasminogen activator. J Biol Chem 2005; 280: 17449-17457.
    • (2005) J Biol Chem , vol.280 , pp. 17449-17457
    • Jo, M.1    Thomas, K.2    Marozkina, N.3    Amin, T.4    Silva, C.5    Parsons, S.6
  • 54
    • 0037461901 scopus 로고    scopus 로고
    • Downregulation of uPA inhibits migration and PI3k/Akt signaling in glioblastoma cells
    • Chandrasekar N, Mohanam S, Gujrati M, Olivero WC, Dinh DH, Rao JS. Downregulation of uPA inhibits migration and PI3k/Akt signaling in glioblastoma cells. Oncogene 2003; 22: 392-400.
    • (2003) Oncogene , vol.22 , pp. 392-400
    • Chandrasekar, N.1    Mohanam, S.2    Gujrati, M.3    Olivero, W.C.4    Dinh, D.H.5    Rao, J.S.6
  • 55
    • 84857916018 scopus 로고    scopus 로고
    • Targeting src family kinases in anti-cancer therapies: Turning promise into triumph
    • Zhang S, Yu D. Targeting Src family kinases in anti-cancer therapies: turning promise into triumph. Trends Pharmacol Sci 2012; 33: 122-128.
    • (2012) Trends Pharmacol Sci , vol.33 , pp. 122-128
    • Zhang, S.1    Yu, D.2
  • 56
    • 0002460807 scopus 로고    scopus 로고
    • Tumor dormancy induced by downregulation of urokinase receptor in human carcinoma involves integrin and MAPK signaling
    • Aguirre Ghiso JA, Kovalski K, Ossowski L. Tumor dormancy induced by downregulation of urokinase receptor in human carcinoma involves integrin and MAPK signaling. J Cell Biol 1999; 147: 89-104.
    • (1999) J Cell Biol , vol.147 , pp. 89-104
    • Aguirre Ghiso, J.A.1    Kovalski, K.2    Ossowski, L.3
  • 57
    • 80051703869 scopus 로고    scopus 로고
    • Regulation of cell migration and invasion by specific modules of uPA: Mechanistic insights and specific inhibitors
    • Carriero MV, Franco P, Votta G, Longanesi-Cattani I, Vento MT, Masucci MT et al. Regulation of cell migration and invasion by specific modules of uPA: mechanistic insights and specific inhibitors. Curr Drug Targets 2011; 12: 1761-1771.
    • (2011) Curr Drug Targets , vol.12 , pp. 1761-1771
    • Carriero, M.V.1    Franco, P.2    Votta, G.3    Longanesi-Cattani, I.4    Vento, M.T.5    Masucci, M.T.6
  • 58
    • 84873278736 scopus 로고    scopus 로고
    • UPAR regulates pericellular proteolysis through a mechanism involving integrins and fMLFreceptors
    • Montuori N, Cosimato V, Rinaldi L, Rea VE, Alfano D, Ragno P. uPAR regulates pericellular proteolysis through a mechanism involving integrins and fMLFreceptors. Thromb Haemost 2013; 109: 309-318.
    • (2013) Thromb Haemost , vol.109 , pp. 309-318
    • Montuori, N.1    Cosimato, V.2    Rinaldi, L.3    Rea, V.E.4    Alfano, D.5    Ragno, P.6
  • 59
    • 0032698213 scopus 로고    scopus 로고
    • Urokinase receptor interacts with alpha(v)beta5 vitronectin receptor, promoting urokinase-dependent cell migration in breast cancer
    • Carriero MV, Del Vecchio S, Capozzoli M, Franco P, Fontana L, Zannetti A et al. Urokinase receptor interacts with alpha(v)beta5 vitronectin receptor, promoting urokinase-dependent cell migration in breast cancer. Cancer Res 1999; 59: 5307-5314.
    • (1999) Cancer Res , vol.59 , pp. 5307-5314
    • Carriero, M.V.1    Del Vecchio, S.2    Capozzoli, M.3    Franco, P.4    Fontana, L.5    Zannetti, A.6
  • 60
    • 0030956119 scopus 로고    scopus 로고
    • Reduction in surface urokinase receptor forces malignant cells into a protracted state of dormancy
    • Yu W, Kim J, Ossowski L. Reduction in surface urokinase receptor forces malignant cells into a protracted state of dormancy. J Cell Biol 1997; 137: 767-777.
    • (1997) J Cell Biol , vol.137 , pp. 767-777
    • Yu, W.1    Kim, J.2    Ossowski, L.3
  • 61
    • 0034782160 scopus 로고    scopus 로고
    • Endogenously produced urokinase-type plasminogen activator is a major determinant of the basal level of activated ERK/MAP kinase and prevents apoptosis in MDA-MB-231 breast cancer cells
    • Ma Z, Webb D, Jo M, Gonias S. Endogenously produced urokinase-type plasminogen activator is a major determinant of the basal level of activated ERK/MAP kinase and prevents apoptosis in MDA-MB-231 breast cancer cells. J Cell Sci 2001; 114: 3387-3396.
    • (2001) J Cell Sci , vol.114 , pp. 3387-3396
    • Ma, Z.1    Webb, D.2    Jo, M.3    Gonias, S.4
  • 62
    • 13844256438 scopus 로고    scopus 로고
    • The urokinase plasminogen activator and its receptor: Role in cell growth and apoptosis
    • Alfano D, Franco P, Vocca I, Gambi N, Pisa V, Mancini A et al. The urokinase plasminogen activator and its receptor: role in cell growth and apoptosis. Thromb Haemost 2005; 93: 205-211.
    • (2005) Thromb Haemost , vol.93 , pp. 205-211
    • Alfano, D.1    Franco, P.2    Vocca, I.3    Gambi, N.4    Pisa, V.5    Mancini, A.6
  • 63
    • 33745841867 scopus 로고    scopus 로고
    • Urokinase signaling through its receptor protects against anoikis by increasing BCL-xL expression levels
    • Alfano D, Iaccarino I, Stoppelli M. Urokinase signaling through its receptor protects against anoikis by increasing BCL-xL expression levels. J Biol Chem 2006; 281: 17758-17767.
    • (2006) J Biol Chem , vol.281 , pp. 17758-17767
    • Alfano, D.1    Iaccarino, I.2    Stoppelli, M.3
  • 64
    • 0027426213 scopus 로고
    • Cellular receptor for urokinase-type plasminogen activator: Function in cell-surface proteolysis
    • Ellis V, Behrendt N, Dano K. Cellular receptor for urokinase-type plasminogen activator: function in cell-surface proteolysis. Methods Enzymol 1993; 223: 223-233.
    • (1993) Methods Enzymol , vol.223 , pp. 223-233
    • Ellis, V.1    Behrendt, N.2    Dano, K.3
  • 65
  • 66
    • 80051697374 scopus 로고    scopus 로고
    • Development of novel therapeutics targeting the urokinase plasminogen activator receptor (uPAR) and their translation toward the clinic
    • Mazar AP, Ahn RW, O'Halloran TV. Development of novel therapeutics targeting the urokinase plasminogen activator receptor (uPAR) and their translation toward the clinic. Curr Pharm Des 2011; 17: 1970-1978.
    • (2011) Curr Pharm des , vol.17 , pp. 1970-1978
    • Mazar, A.P.1    Ahn, R.W.2    O'Halloran, T.V.3
  • 67
    • 69249111313 scopus 로고    scopus 로고
    • Reversibility of epithelial-mesenchymal transition (EMT) induced in breast cancer cells by activation of urokinase receptor-dependent cell signaling
    • Jo M, Lester R, Montel V, Eastman B, Takimoto S, Gonias S. Reversibility of epithelial-mesenchymal transition (EMT) induced in breast cancer cells by activation of urokinase receptor-dependent cell signaling. J Biol Chem 2009; 284: 22825-22833.
    • (2009) J Biol Chem , vol.284 , pp. 22825-22833
    • Jo, M.1    Lester, R.2    Montel, V.3    Eastman, B.4    Takimoto, S.5    Gonias, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.