메뉴 건너뛰기




Volumn 4, Issue 5, 2013, Pages 383-390

Plasma fibronectin promotes tumor cell survival and invasion through regulation of Tie2

Author keywords

Fibrin; Metastasis; Plasma fibronectin; Tie2

Indexed keywords

ANGIOPOIETIN RECEPTOR; FIBRIN; FIBRONECTIN; TUMOR NECROSIS FACTOR ALPHA;

EID: 84883041631     PISSN: None     EISSN: 18379664     Source Type: Journal    
DOI: 10.7150/jca.6545     Document Type: Article
Times cited : (8)

References (47)
  • 1
    • 79953147370 scopus 로고    scopus 로고
    • A perspective on cancer cell metastasis
    • Chaffer CL, Weinberg RA. A perspective on cancer cell metastasis. Science. 2011;331:1559-64.
    • (2011) Science , vol.331 , pp. 1559-64
    • Chaffer, C.L.1    Weinberg, R.A.2
  • 2
    • 77953153938 scopus 로고    scopus 로고
    • Plasma fibronectin promotes lung metastasis by contributions to fibrin clots and tumor cell invasion
    • Malik G, Knowles LM, Dhir R, Xu S, Yang S, Ruoslahti E, et al. Plasma fibronectin promotes lung metastasis by contributions to fibrin clots and tumor cell invasion. Cancer Res. 2010;70:4327-34.
    • (2010) Cancer Res. , vol.70 , pp. 4327-34
    • Malik, G.1    Knowles, L.M.2    Dhir, R.3    Xu, S.4    Yang, S.5    Ruoslahti, E.6
  • 3
    • 0021342790 scopus 로고
    • Role of NK cells in the antimetastatic effect of anticoagulant drugs
    • Gorelik E, Bere WW, Herberman RB. Role of NK cells in the antimetastatic effect of anticoagulant drugs. Int J Cancer. 1984;33:87-94.
    • (1984) Int J Cancer , vol.33 , pp. 87-94
    • Gorelik, E.1    Bere, W.W.2    Herberman, R.B.3
  • 4
    • 0025938196 scopus 로고
    • Inhibition of murine melanoma experimental metastasis by recombinant desulfatohirudin, a highly specific thrombin inhibitor
    • Esumi N, Fan D, Fidler IJ. Inhibition of murine melanoma experimental metastasis by recombinant desulfatohirudin, a highly specific thrombin inhibitor. Cancer research. 1991;51:4549-56.
    • (1991) Cancer research , vol.51 , pp. 4549-56
    • Esumi, N.1    Fan, D.2    Fidler, I.J.3
  • 5
    • 42149137285 scopus 로고    scopus 로고
    • Factor XIII transglutaminase supports hematogenous tumor cell metastasis through a mechanism dependent on natural killer cell function
    • Palumbo JS, Barney KA, Blevins EA, Shaw MA, Mishra A, Flick MJ, et al. Factor XIII transglutaminase supports hematogenous tumor cell metastasis through a mechanism dependent on natural killer cell function. J Thromb Haemost. 2008;6:812-9.
    • (2008) J Thromb Haemost , vol.6 , pp. 812-9
    • Palumbo, J.S.1    Barney, K.A.2    Blevins, E.A.3    Shaw, M.A.4    Mishra, A.5    Flick, M.J.6
  • 6
    • 0034669975 scopus 로고    scopus 로고
    • Fibrinogen is an important determinant of the metastatic potential of circulating tumor cells
    • Palumbo JS, Kombrinck KW, Drew AF, Grimes TS, Kiser JH, Degen JL, et al. Fibrinogen is an important determinant of the metastatic potential of circulating tumor cells. Blood. 2000;96:3302-9.
    • (2000) Blood , vol.96 , pp. 3302-3309
    • Palumbo, J.S.1    Kombrinck, K.W.2    Drew, A.F.3    Grimes, T.S.4    Kiser, J.H.5    Degen, J.L.6
  • 7
    • 11144230059 scopus 로고    scopus 로고
    • Platelets and fibrin(ogen) increase metastatic potential by impeding natural killer cell-mediated elimination of tumor cells
    • Palumbo JS, Talmage KE, Massari JV, La Jeunesse CM, Flick MJ, Kombrinck KW, et al. Platelets and fibrin(ogen) increase metastatic potential by impeding natural killer cell-mediated elimination of tumor cells. Blood. 2005;105:178-85.
    • (2005) Blood , vol.105 , pp. 178-85
    • Palumbo, J.S.1    Talmage, K.E.2    Massari, J.V.3    La Jeunesse, C.M.4    Flick, M.J.5    Kombrinck, K.W.6
  • 8
    • 9244265563 scopus 로고    scopus 로고
    • Coagulation facilitates tumor cell spreading in the pulmonary vasculature during early metastatic colony formation
    • Im JH, Fu W, Wang H, Bhatia SK, Hammer DA, Kowalska MA, et al. Coagulation facilitates tumor cell spreading in the pulmonary vasculature during early metastatic colony formation. Cancer Res. 2004;64:8613-9.
    • (2004) Cancer Res. , vol.64 , pp. 8613-9
    • Im, J.H.1    Fu, W.2    Wang, H.3    Bhatia, S.K.4    Hammer, D.A.5    Kowalska, M.A.6
  • 10
    • 79952827058 scopus 로고    scopus 로고
    • Targeting Cell Spreading: A Method of Sensitizing Metastatic Tumor Cells to TRAIL-Induced Apoptosis
    • Phipps LE, Hino S, Muschel RJ. Targeting Cell Spreading: A Method of Sensitizing Metastatic Tumor Cells to TRAIL-Induced Apoptosis. Molecular Cancer Research. 2011;9:249-58.
    • (2011) Molecular Cancer Research , vol.9 , pp. 249-58
    • Phipps, L.E.1    Hino, S.2    Muschel, R.J.3
  • 11
    • 51349153709 scopus 로고    scopus 로고
    • The progenitor cell marker NG2/MPG promotes chemoresistance by activation of integrin-dependent PI3K/Akt signaling
    • Chekenya M, Krakstad C, Svendsen A, Netland IA, Staalesen V, Tysnes BB, et al. The progenitor cell marker NG2/MPG promotes chemoresistance by activation of integrin-dependent PI3K/Akt signaling. Oncogene. 2008;27:5182-94.
    • (2008) Oncogene. , vol.27 , pp. 5182-94
    • Chekenya, M.1    Krakstad, C.2    Svendsen, A.3    Netland, I.A.4    Staalesen, V.5    Tysnes, B.B.6
  • 13
    • 0021309519 scopus 로고
    • Fibronectin in cell adhesion and invasion
    • Ruoslahti E. Fibronectin in cell adhesion and invasion. Cancer Metastasis Rev. 1984;3:43-51.
    • (1984) Cancer Metastasis Rev. , vol.3 , pp. 43-51
    • Ruoslahti, E.1
  • 14
    • 51049119424 scopus 로고    scopus 로고
    • Inhibition of metastatic outgrowth from single dormant tumor cells by targeting the cytoskeleton
    • Barkan D, Kleinman H, Simmons JL, Asmussen H, Kamaraju AK, Hoenorhoff MJ, et al. Inhibition of metastatic outgrowth from single dormant tumor cells by targeting the cytoskeleton. Cancer Res. 2008;68:6241-50.
    • (2008) Cancer Res. , vol.68 , pp. 6241-50
    • Barkan, D.1    Kleinman, H.2    Simmons, J.L.3    Asmussen, H.4    Kamaraju, A.K.5    Hoenorhoff, M.J.6
  • 17
    • 0032582686 scopus 로고    scopus 로고
    • Matrix metalloproteinases regulate neovascularization by acting as pericellular fibrinolysins
    • Hiraoka N, Allen E, Apel IJ, Gyetko MR, Weiss SJ. Matrix metalloproteinases regulate neovascularization by acting as pericellular fibrinolysins. Cell. 1998;95:365-77.
    • (1998) Cell , vol.95 , pp. 365-77
    • Hiraoka, N.1    Allen, E.2    Apel, I.J.3    Gyetko, M.R.4    Weiss, S.J.5
  • 20
    • 0029947854 scopus 로고    scopus 로고
    • Changes in cell spreading and cytoskeletal organization are induced by adhesion to a fibronectin-fibrin matrix
    • Corbett SA, Wilson CL, Schwarzbauer JE. Changes in cell spreading and cytoskeletal organization are induced by adhesion to a fibronectin-fibrin matrix. Blood. 1996;88:158-66.
    • (1996) Blood , vol.88 , pp. 158-66
    • Corbett, S.A.1    Wilson, C.L.2    Schwarzbauer, J.E.3
  • 21
    • 0037077225 scopus 로고    scopus 로고
    • Unique ability of integrin alpha(v)beta 3 to support tumor cell arrest under dynamic flow conditions
    • Pilch J, Habermann R, Felding-Habermann B. Unique ability of integrin alpha(v)beta 3 to support tumor cell arrest under dynamic flow conditions. J Biol Chem. 2002;277:21930-8.
    • (2002) J Biol Chem. , vol.277 , pp. 21930-8
    • Pilch, J.1    Habermann, R.2    Felding-Habermann, B.3
  • 22
    • 0029739950 scopus 로고    scopus 로고
    • Control of adhesion-dependent cell survival by focal adhesion kinase
    • Frisch SM, Vuori K, Ruoslahti E, Chan-Hui PY. Control of adhesion-dependent cell survival by focal adhesion kinase. J Cell Biol. 1996;134:793-9.
    • (1996) J Cell Biol. , vol.134 , pp. 793-9
    • Frisch, S.M.1    Vuori, K.2    Ruoslahti, E.3    Chan-Hui, P.Y.4
  • 23
    • 0032534025 scopus 로고    scopus 로고
    • The presence of a constitutively active phosphoinositide 3-kinase in small cell lung cancer cells mediates anchorage-independent proliferation via a protein kinase B and p70s6k-dependent pathway
    • Moore SM, Rintoul RC, Walker TR, Chilvers ER, Haslett C, Sethi T. The presence of a constitutively active phosphoinositide 3-kinase in small cell lung cancer cells mediates anchorage-independent proliferation via a protein kinase B and p70s6k-dependent pathway. Cancer Res. 1998;58:5239-47.
    • (1998) Cancer Res. , vol.58 , pp. 5239-47
    • Moore, S.M.1    Rintoul, R.C.2    Walker, T.R.3    Chilvers, E.R.4    Haslett, C.5    Sethi, T.6
  • 24
    • 70450222098 scopus 로고    scopus 로고
    • Matrix crosslinking forces tumor progression by enhancing integrin signaling
    • Levental KR, Yu H, Kass L, Lakins JN, Egeblad M, Erler JT, et al. Matrix crosslinking forces tumor progression by enhancing integrin signaling. Cell. 2009;139:891-906.
    • (2009) Cell , vol.139 , pp. 891-906
    • Levental, K.R.1    Yu, H.2    Kass, L.3    Lakins, J.N.4    Egeblad, M.5    Erler, J.T.6
  • 25
    • 0033636606 scopus 로고    scopus 로고
    • A mechanism for modulation of cellular responses to VEGF: activation of the integrins
    • Byzova TV, Goldman CK, Pampori N, Thomas KA, Bett A, Shattil SJ, et al. A mechanism for modulation of cellular responses to VEGF: activation of the integrins. Mol Cell. 2000;6:851-60.
    • (2000) Mol Cell. , vol.6 , pp. 851-60
    • Byzova, T.V.1    Goldman, C.K.2    Pampori, N.3    Thomas, K.A.4    Bett, A.5    Shattil, S.J.6
  • 26
    • 0030911052 scopus 로고    scopus 로고
    • Role of phosphoinositide 3-OH kinase in cell transformation and control of the actin cytoskeleton by Ras
    • Rodriguez-Viciana P, Warne PH, Khwaja A, Marte BM, Pappin D, Das P, et al. Role of phosphoinositide 3-OH kinase in cell transformation and control of the actin cytoskeleton by Ras. Cell. 1997;89:457-67.
    • (1997) Cell. , vol.89 , pp. 457-67
    • Rodriguez-Viciana, P.1    Warne, P.H.2    Khwaja, A.3    Marte, B.M.4    Pappin, D.5    Das, P.6
  • 27
    • 33745833345 scopus 로고    scopus 로고
    • Genetic deletion of Rac1 GTPase reveals its critical role in actin stress fiber formation and focal adhesion complex assembly
    • Guo FK, Debidda M, Yang L, Williams DA, Zheng Y. Genetic deletion of Rac1 GTPase reveals its critical role in actin stress fiber formation and focal adhesion complex assembly. Journal of Biological Chemistry. 2006;281:18652-9.
    • (2006) Journal of Biological Chemistry , vol.281 , pp. 18652-9
    • Guo, F.K.1    Debidda, M.2    Yang, L.3    Williams, D.A.4    Zheng, Y.5
  • 28
    • 0032572557 scopus 로고    scopus 로고
    • Integrin-mediated signals regulated by members of the rho family of GTPases
    • Clark EA, King WG, Brugge JS, Symons M, Hynes RO. Integrin-mediated signals regulated by members of the rho family of GTPases. J Cell Biol. 1998;142:573-86.
    • (1998) J Cell Biol. , vol.142 , pp. 573-86
    • Clark, E.A.1    King, W.G.2    Brugge, J.S.3    Symons, M.4    Hynes, R.O.5
  • 29
    • 0040056864 scopus 로고    scopus 로고
    • p21-activated kinase 1 phosphorylates the death agonist bad and protects cells from apoptosis
    • Schurmann A, Mooney AF, Sanders LC, Sells MA, Wang HG, Reed JC, et al. p21-activated kinase 1 phosphorylates the death agonist bad and protects cells from apoptosis. Mol Cell Biol. 2000;20:453-61.
    • (2000) Mol Cell Biol. , vol.20 , pp. 453-61
    • Schurmann, A.1    Mooney, A.F.2    Sanders, L.C.3    Sells, M.A.4    Wang, H.G.5    Reed, J.C.6
  • 30
    • 0035958923 scopus 로고    scopus 로고
    • Rac1 protects epithelial cells against anoikis
    • Coniglio SJ, Jou TS, Symons M. Rac1 protects epithelial cells against anoikis. J Biol Chem. 2001;276:28113-20.
    • (2001) J Biol Chem. , vol.276 , pp. 28113-20
    • Coniglio, S.J.1    Jou, T.S.2    Symons, M.3
  • 32
    • 0030702123 scopus 로고    scopus 로고
    • Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery
    • Datta SR, Dudek H, Tao X, Masters S, Fu H, Gotoh Y, et al. Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery. Cell. 1997;91:231-41.
    • (1997) Cell , vol.91 , pp. 231-41
    • Datta, S.R.1    Dudek, H.2    Tao, X.3    Masters, S.4    Fu, H.5    Gotoh, Y.6
  • 34
    • 0032482169 scopus 로고    scopus 로고
    • Inhibition of caspases increases the sensitivity of L929 cells to necrosis mediated by tumor necrosis factor
    • Vercammen D, Beyaert R, Denecker G, Goossens V, Van Loo G, Declercq W, et al. Inhibition of caspases increases the sensitivity of L929 cells to necrosis mediated by tumor necrosis factor. J Exp Med. 1998;187:1477-85.
    • (1998) J Exp Med. , vol.187 , pp. 1477-85
    • Vercammen, D.1    Beyaert, R.2    Denecker, G.3    Goossens, V.4    Van Loo, G.5    Declercq, W.6
  • 35
    • 66749183275 scopus 로고    scopus 로고
    • Receptor interacting protein kinase-3 determines cellular necrotic response to TNF-alpha
    • He S, Wang L, Miao L, Wang T, Du F, Zhao L, et al. Receptor interacting protein kinase-3 determines cellular necrotic response to TNF-alpha. Cell. 2009;137:1100-11.
    • (2009) Cell , vol.137 , pp. 1100-11
    • He, S.1    Wang, L.2    Miao, L.3    Wang, T.4    Du, F.5    Zhao, L.6
  • 36
    • 1642299768 scopus 로고    scopus 로고
    • Tumor necrosis factor-induced nonapoptotic cell death requires receptor-interacting protein-mediated cellular reactive oxygen species accumulation
    • Lin Y, Choksi S, Shen HM, Yang QF, Hur GM, Kim YS, et al. Tumor necrosis factor-induced nonapoptotic cell death requires receptor-interacting protein-mediated cellular reactive oxygen species accumulation. J Biol Chem. 2004;279:10822-8.
    • (2004) J Biol Chem. , vol.279 , pp. 10822-8
    • Lin, Y.1    Choksi, S.2    Shen, H.M.3    Yang, Q.F.4    Hur, G.M.5    Kim, Y.S.6
  • 38
    • 44949240664 scopus 로고    scopus 로고
    • cIAP1 and cIAP2 facilitate cancer cell survival by functioning as E3 ligases that promote RIP1 ubiquitination
    • Bertrand MJ, Milutinovic S, Dickson KM, Ho WC, Boudreault A, Durkin J, et al. cIAP1 and cIAP2 facilitate cancer cell survival by functioning as E3 ligases that promote RIP1 ubiquitination. Mol Cell. 2008;30:689-700.
    • (2008) Mol Cell. , vol.30 , pp. 689-700
    • Bertrand, M.J.1    Milutinovic, S.2    Dickson, K.M.3    Ho, W.C.4    Boudreault, A.5    Durkin, J.6
  • 39
    • 33646034316 scopus 로고    scopus 로고
    • Activation of IKK by TNFalpha requires site-specific ubiquitination of RIP1 and polyubiquitin binding by NEMO
    • Ea CK, Deng L, Xia ZP, Pineda G, Chen ZJ. Activation of IKK by TNFalpha requires site-specific ubiquitination of RIP1 and polyubiquitin binding by NEMO. Mol Cell. 2006;22:245-57.
    • (2006) Mol Cell. , vol.22 , pp. 245-57
    • Ea, C.K.1    Deng, L.2    Xia, Z.P.3    Pineda, G.4    Chen, Z.J.5
  • 40
    • 44849117768 scopus 로고    scopus 로고
    • Akt-dependent regulation of NF-{kappa}B is controlled by mTOR and Raptor in association with IKK
    • Dan HC, Cooper MJ, Cogswell PC, Duncan JA, Ting JP, Baldwin AS. Akt-dependent regulation of NF-{kappa}B is controlled by mTOR and Raptor in association with IKK. Genes Dev. 2008;22:1490-500.
    • (2008) Genes Dev. , vol.22 , pp. 1490-500
    • Dan, H.C.1    Cooper, M.J.2    Cogswell, P.C.3    Duncan, J.A.4    Ting, J.P.5    Baldwin, A.S.6
  • 41
    • 0033517189 scopus 로고    scopus 로고
    • NF-kappaB activation by tumour necrosis factor requires the Akt serine-threonine kinase
    • Ozes ON, Mayo LD, Gustin JA, Pfeffer SR, Pfeffer LM, Donner DB. NF-kappaB activation by tumour necrosis factor requires the Akt serine-threonine kinase. Nature. 1999;401:82-5.
    • (1999) Nature , vol.401 , pp. 82-5
    • Ozes, O.N.1    Mayo, L.D.2    Gustin, J.A.3    Pfeffer, S.R.4    Pfeffer, L.M.5    Donner, D.B.6
  • 42
    • 0025260779 scopus 로고
    • Regulation of tumor necrosis factor alpha transcription in macrophages: involvement of four kappa B-like motifs and of constitutive and inducible forms of NF-kappa B
    • Collart MA, Baeuerle P, Vassalli P. Regulation of tumor necrosis factor alpha transcription in macrophages: involvement of four kappa B-like motifs and of constitutive and inducible forms of NF-kappa B. Mol Cell Biol. 1990;10:1498-506.
    • (1990) Mol Cell Biol. , vol.10 , pp. 1498-506
    • Collart, M.A.1    Baeuerle, P.2    Vassalli, P.3
  • 44
    • 34249979533 scopus 로고    scopus 로고
    • Identification of proangiogenic TIE2-expressing monocytes (TEMs) in human peripheral blood and cancer
    • Venneri MA, De Palma M, Ponzoni M, Pucci F, Scielzo C, Zonari E, et al. Identification of proangiogenic TIE2-expressing monocytes (TEMs) in human peripheral blood and cancer. Blood. 2007;109:5276-85.
    • (2007) Blood. , vol.109 , pp. 5276-85
    • Venneri, M.A.1    De Palma, M.2    Ponzoni, M.3    Pucci, F.4    Scielzo, C.5    Zonari, E.6
  • 45
    • 0035503218 scopus 로고    scopus 로고
    • Dok-R plays a pivotal role in angiopoietin-1-dependent cell migration through recruitment and activation of Pak
    • Master Z, Jones N, Tran J, Jones J, Kerbel RS, Dumont DJ. Dok-R plays a pivotal role in angiopoietin-1-dependent cell migration through recruitment and activation of Pak. EMBO J. 2001;20:5919-28.
    • (2001) EMBO J. , vol.20 , pp. 5919-28
    • Master, Z.1    Jones, N.2    Tran, J.3    Jones, J.4    Kerbel, R.S.5    Dumont, D.J.6
  • 46
    • 0031834338 scopus 로고    scopus 로고
    • Tyrosine 1101 of Tie2 is the major site of association of p85 and is required for activation of phosphatidylinositol 3-kinase and Akt
    • Kontos CD, Stauffer TP, Yang WP, York JD, Huang L, Blanar MA, et al. Tyrosine 1101 of Tie2 is the major site of association of p85 and is required for activation of phosphatidylinositol 3-kinase and Akt. Mol Cell Biol. 1998;18:4131-40.
    • (1998) Mol Cell Biol. , vol.18 , pp. 4131-40
    • Kontos, C.D.1    Stauffer, T.P.2    Yang, W.P.3    York, J.D.4    Huang, L.5    Blanar, M.A.6
  • 47
    • 84864351290 scopus 로고    scopus 로고
    • Soft fibrin gels promote selection and growth of tumorigenic cells
    • Liu J, Tan Y, Zhang H, Zhang Y, Xu P, Chen J, et al. Soft fibrin gels promote selection and growth of tumorigenic cells. Nat Mater. 2012;11:734-41.
    • (2012) Nat Mater. , vol.11 , pp. 734-41
    • Liu, J.1    Tan, Y.2    Zhang, H.3    Zhang, Y.4    Xu, P.5    Chen, J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.