메뉴 건너뛰기




Volumn 115, Issue 24, 2010, Pages 5111-5120

Factor XII stimulates ERK1/2 and Akt through uPAR, integrins, and the EGFR to initiate angiogenesis

Author keywords

[No Author keywords available]

Indexed keywords

2 (2 AMINO 3 METHOXYPHENYL)CHROMONE; 2 MORPHOLINO 8 PHENYLCHROMONE; 4 (3 CHLOROANILINO) 6,7 DIMETHOXYQUINAZOLINE; BETA1 INTEGRIN; BLOOD CLOTTING FACTOR 12; BROXURIDINE; EPIDERMAL GROWTH FACTOR RECEPTOR; HIGH MOLECULAR WEIGHT KININOGEN; INTEGRIN; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; PROTEIN KINASE B; UROKINASE RECEPTOR; WORTMANNIN; ZINC ION; ENZYME INHIBITOR;

EID: 77954672298     PISSN: 00064971     EISSN: 15280020     Source Type: Journal    
DOI: 10.1182/blood-2009-08-236430     Document Type: Article
Times cited : (100)

References (37)
  • 1
    • 37049242417 scopus 로고
    • Waterfall sequence for intrinsic blood coagulation
    • Davie EW, Ratnoff OD. Waterfall sequence for intrinsic blood coagulation. Science. 1964;145:1310-1320.
    • (1964) Science , vol.145 , pp. 1310-1320
    • Davie, E.W.1    Ratnoff, O.D.2
  • 2
    • 68249137277 scopus 로고    scopus 로고
    • Dual role of collagen in factor XII-dependent thrombus formation
    • van der Meijden PEJ, Munnix ICA, Auger JM, et al. Dual role of collagen in factor XII-dependent thrombus formation. Blood. 2009;114(4):881-890.
    • (2009) Blood , vol.114 , Issue.4 , pp. 881-890
    • Van Der Meijden, P.E.J.1    Munnix, I.C.A.2    Auger, J.M.3
  • 4
    • 34447322451 scopus 로고    scopus 로고
    • Extracellular RNA constitutes a natural procoagulant cofactor in blood coagulation
    • Kannemeier C, Shibamiya A, Nakazawa F, et al. Extracellular RNA constitutes a natural procoagulant cofactor in blood coagulation. Proc Natl Acad Sci U S A. 2007;104(15):6388-6393.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , Issue.15 , pp. 6388-6393
    • Kannemeier, C.1    Shibamiya, A.2    Nakazawa, F.3
  • 5
    • 51349160073 scopus 로고    scopus 로고
    • Misfolded proteins activate factor XII in humans, leading to kallikrein formation without initiating coagulation
    • Maas C, Govers-Riemslag JW, Bouma B, et al. Misfolded proteins activate factor XII in humans, leading to kallikrein formation without initiating coagulation. J Clin Invest. 2008;118(9):3208-3218.
    • (2008) J Clin Invest , vol.118 , Issue.9 , pp. 3208-3218
    • Maas, C.1    Govers-Riemslag, J.W.2    Bouma, B.3
  • 7
    • 0037093204 scopus 로고    scopus 로고
    • Factor XII interacts with the multiprotein assembly of urokinase plasminogen activator receptor, gC1qR, and cytokeratin on endothelial cell membranes
    • Mahdi F, Shariat-Madar Z, Figueroa CD, Schmaier AH. Factor XII interacts with the multiprotein assembly of urokinase plasminogen activator receptor, gC1qR, and cytokeratin on endothelial cell membranes. Blood. 2002;99(10):3585-3596.
    • (2002) Blood , vol.99 , Issue.10 , pp. 3585-3596
    • Mahdi, F.1    Shariat-Madar, Z.2    Figueroa, C.D.3    Schmaier, A.H.4
  • 8
    • 1942533421 scopus 로고    scopus 로고
    • Mapping the interaction between high molecular weight kininogen and the urokinase plasminogen activator receptor
    • Mahdi F, Shariat-Madar Z, Kuo A, Carinato M, Cines DB, Schmaier AH. Mapping the interaction between high molecular weight kininogen and the urokinase plasminogen activator receptor. J Biol Chem. 2004;279(16):16621-16628.
    • (2004) J Biol Chem , vol.279 , Issue.16 , pp. 16621-16628
    • Mahdi, F.1    Shariat-Madar, Z.2    Kuo, A.3    Carinato, M.4    Cines, D.B.5    Schmaier, A.H.6
  • 9
    • 0027212538 scopus 로고
    • Human Hageman factor (factor XII) and high molecular weight kininogen compete for the same binding site on human umbilical vein endothelial cells
    • Reddigari S, Shibayama Y, Brunnee T, Kaplan A. Human Hageman factor (factor XII) and high molecular weight kininogen compete for the same binding site on human umbilical vein endothelial cells. J Biol Chem. 1993;268(16):11982-11987. (Pubitemid 23168160)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.16 , pp. 11982-11987
    • Reddigari, S.R.1    Shibayama, Y.2    Brunnee, T.3    Kaplan, A.P.4
  • 10
    • 0042531666 scopus 로고    scopus 로고
    • Sequences within domain II of the urokinase receptor critical for differential ligand recognition
    • DOI 10.1074/jbc.M300751200
    • Li Y, Lawrence DA, Zhang L. Sequences within domain II of the urokinase receptor critical for differential ligand recognition. J Biol. Chem. 2003;278(32):29925-29932. (Pubitemid 36962380)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.32 , pp. 29925-29932
    • Li, Y.1    Lawrence, D.A.2    Zhang, L.3
  • 11
    • 0029970618 scopus 로고    scopus 로고
    • Factor XII-induced mitogenesis is mediated via a distinct signal transduction pathway that activates a mitogen-activated protein kinase
    • Gordon EM, Venkatesan N, Salazar R, et al. Factor XII-induced mitogenesis is mediated via a distinct signal transduction pathway that activates a mitogen-activated protein kinase. Proc Natl Acad Sci. U S A. 1996;93(5):2174-2179.
    • (1996) Proc Natl Acad Sci. U S A , vol.93 , Issue.5 , pp. 2174-2179
    • Gordon, E.M.1    Venkatesan, N.2    Salazar, R.3
  • 12
    • 21644457354 scopus 로고    scopus 로고
    • Assembly, activation, and signaling by kinin-forming proteins on human vascular smooth muscle cells
    • Fernando AN, Fernand LP, Fukuda Y, Kaplan AP. Assembly, activation, and signaling by kinin-forming proteins on human vascular smooth muscle cells. Am J Physiol Heart Circ Physiol. 2005;289(1):H251-H257.
    • (2005) Am J Physiol Heart Circ Physiol , vol.289 , Issue.1
    • Fernando, A.N.1    Fernand, L.P.2    Fukuda, Y.3    Kaplan, A.P.4
  • 13
    • 0344875558 scopus 로고    scopus 로고
    • Soluble Urokinase-type Plasminogen Activator Receptor Inhibits Cancer Cell Growth and Invasion by Direct Urokinase-independent Effects on Cell Signaling
    • DOI 10.1074/jbc.M308808200
    • Jo M, Thomas KS, Wu L, Gonias SL. Soluble urokinase-type plasminogen activator receptor inhibits cancer cell growth and invasion by direct urokinase-independent effects on cell signaling. J Biol Chem. 2003;278(47):46692-46698. (Pubitemid 37452247)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.47 , pp. 46692-46698
    • Jo, M.1    Thomas, K.S.2    Wu, L.3    Gonias, S.L.4
  • 14
    • 2442671521 scopus 로고    scopus 로고
    • Urokinase-type plasminogen activator receptor is involved in mediating the apoptotic effect of cleaved high molecular weight kininogen in human endothelial cells
    • Cao DJ, Guo Y-L, Colman RW. Urokinase-type plasminogen activator receptor is involved in mediating the apoptotic effect of cleaved high molecular weight kininogen in human endothelial cells. Circ Res. 2004;94(9):1227-1234.
    • (2004) Circ Res , vol.94 , Issue.9 , pp. 1227-1234
    • Cao, D.J.1    Guo, Y.-L.2    Colman, R.W.3
  • 15
    • 0032540943 scopus 로고    scopus 로고
    • The urokinase-type plasminogen activator receptor mediates tyrosine phosphorylation of focal adhesion proteins and activation of mitogen-activates protein kinase in cultured endothelial cells
    • Tang H, Kerins DM, Hao Q, Inagami T, Vaughan DE. The urokinase-type plasminogen activator receptor mediates tyrosine phosphorylation of focal adhesion proteins and activation of mitogen-activates protein kinase in cultured endothelial cells. J Biol Chem. 1998;273(29):18268-18272.
    • (1998) J Biol Chem , vol.273 , Issue.29 , pp. 18268-18272
    • Tang, H.1    Kerins, D.M.2    Hao, Q.3    Inagami, T.4    Vaughan, D.E.5
  • 16
    • 0029096807 scopus 로고
    • Mapping the cell binding site on high molecular weight kininogen's domain 5
    • Hasan AAK, Cines DB, Herwald H, Schmaier AH, Muller-Esterl W. Mapping the cell binding site on high molecular weight kininogen's domain 5. J Biol Chem. 1995;270(33):19256-19261.
    • (1995) J Biol Chem , vol.270 , Issue.33 , pp. 19256-19261
    • Hasan, A.A.K.1    Cines, D.B.2    Herwald, H.3    Schmaier, A.H.4    Muller-Esterl, W.5
  • 17
    • 21644432642 scopus 로고    scopus 로고
    • Domain 2 of the urokinase receptor contains an integrin-interacting epitope with intrinsic signaling activity: Generation of a new integrin inhibitor
    • DOI 10.1074/jbc.M413954200
    • Degryse B, Resnati M, Czekay RP, Loskutoff DJ, Blasi F. Domain 2 of the urokinase receptor contains an integrin-interacting epitope with intrinsic signaling activity: generation of a new integrin inhibitor. J Biol Chem. 2005;280(26):24792-24803. (Pubitemid 40934570)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.26 , pp. 24792-24803
    • Degryse, B.1    Resnati, M.2    Czekay, R.-P.3    Loskutoff, D.J.4    Blasi, F.5
  • 18
    • 13444274458 scopus 로고    scopus 로고
    • Regulation of alpha5beta1 integrin conformation and function by urokinase receptor binding
    • Wei Y, Czekay R-P, Robillard L, et al. Regulation of alpha5beta1 integrin conformation and function by urokinase receptor binding. J Cell Biol. 2005;168(3):501-511.
    • (2005) J Cell Biol , vol.168 , Issue.3 , pp. 501-511
    • Wei, Y.1    Czekay, R.-P.2    Robillard, L.3
  • 19
    • 33749076673 scopus 로고    scopus 로고
    • SIN1/MIP1 maintains rictor-mTOR complex integrity and regulates Akt phosphorylation and substrate specificity
    • Jacinto E, Facchinetti V, Liu D, et al. SIN1/MIP1 maintains rictor-mTOR complex integrity and regulates Akt phosphorylation and substrate specificity. Cell. 2006;127(1):125-137.
    • (2006) Cell , vol.127 , Issue.1 , pp. 125-137
    • Jacinto, E.1    Facchinetti, V.2    Liu, D.3
  • 21
    • 0029067419 scopus 로고
    • The receptor for urokinase-type plasminogen activator is not essential for mouse development or fertility
    • Bugge TH, Suh TT, Flick MJ, et al. The receptor for urokinase-type plasminogen activator is not essential for mouse development or fertility. J Biol Chem. 1995;270(28):16886-16894.
    • (1995) J Biol Chem , vol.270 , Issue.28 , pp. 16886-16894
    • Bugge, T.H.1    Suh, T.T.2    Flick, M.J.3
  • 22
    • 4143083096 scopus 로고    scopus 로고
    • Histidine-proline rich glycoprotein (HPRG) binds and transduces anti-angiogenic signals through cell surface tropomyosin on endothelial cells
    • Guan X, Juarez JC, Qi X, et al. Histidine-proline rich glycoprotein (HPRG) binds and transduces anti-angiogenic signals through cell surface tropomyosin on endothelial cells. Thromb Haemost. 2004;92(2):403-412.
    • (2004) Thromb Haemost , vol.92 , Issue.2 , pp. 403-412
    • Guan, X.1    Juarez, J.C.2    Qi, X.3
  • 23
    • 33745320535 scopus 로고    scopus 로고
    • Plasma levels of bradykinin are suppressed in factor XII-deficient mice
    • Iwaki T, Castellino FJ. Plasma levels of bradykinin are suppressed in factor XII-deficient mice. Thromb Haemost. 2006;95(6):1003-1010.
    • (2006) Thromb Haemost , vol.95 , Issue.6 , pp. 1003-1010
    • Iwaki, T.1    Castellino, F.J.2
  • 24
    • 0037449805 scopus 로고    scopus 로고
    • Epidermal growth factor receptor-dependent and -independent cell-signaling pathways originating from the urokinase receptor
    • DOI 10.1074/jbc.M210877200
    • Jo M, Thomas KS, O'Donnell DM, Gonias SL. Epidermal growth factor receptor-dependent and -independent cell-signaling pathways originating from the urokinase receptor. J Biol Chem. 2003;278(3):1642-1646. (Pubitemid 36801395)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.3 , pp. 1642-1646
    • Jo, M.1    Thomas, K.S.2    O'Donnell, D.M.3    Gonias, S.L.4
  • 25
    • 0032515047 scopus 로고    scopus 로고
    • Vascular endothelial growth factor regulates endothelial cell survival through the phosphatidylinositol 3′-kinase/Akt signal transduction pathway. Requirement for Flk-1/KDR activation
    • Gerber H-P, McMurtrey A, Kowalski J, et al. Vascular endothelial growth factor regulates endothelial cell survival through the phosphatidylinositol 3′-kinase/Akt signal transduction pathway. Requirement for Flk-1/KDR activation. J Biol Chem. 1998;273(46):30336-30343.
    • (1998) J Biol Chem , vol.273 , Issue.46 , pp. 30336-30343
    • Gerber, H.-P.1    McMurtrey, A.2    Kowalski, J.3
  • 26
    • 12344256951 scopus 로고    scopus 로고
    • Wortmannin, a widely used phosphoinositide 3-kinase inhibitor, also potently inhibits mammalian polo-like kinase
    • DOI 10.1016/j.chembiol.2004.11.009, PII S1074552104003291
    • Liu Y, Shreder KR, Gai W, Corral S, Ferris DK, Rosenblum JS. Wortmannin, a widely used phosphoinositide 3-kinase inhibitor, also potently inhibits mammalian polo-like kinase, Chem Biol. 2005;12(1):99-107. (Pubitemid 40118330)
    • (2005) Chemistry and Biology , vol.12 , Issue.1 , pp. 99-107
    • Liu, Y.1    Shreder, K.R.2    Gai, W.3    Corral, S.4    Ferris, D.K.5    Rosenblum, J.S.6
  • 28
    • 73049113141 scopus 로고    scopus 로고
    • The mitogen-activated protein kinase signaling pathways: Role in megakaryocyte differentiation
    • Séverin S, Ghevaert C, Mazharian A. The mitogen-activated protein kinase signaling pathways: role in megakaryocyte differentiation. J Thromb Haemost. 2010;8(1):17-26.
    • (2010) J Thromb Haemost , vol.8 , Issue.1 , pp. 17-26
    • Séverin, S.1    Ghevaert, C.2    Mazharian, A.3
  • 29
    • 33947542987 scopus 로고    scopus 로고
    • Urokinase receptors are required for alpha 5 beta 1 integrin-mediated signaling in tumor cells
    • Wei Y, Tang C-H, Kim Y, et al. Urokinase receptors are required for alpha 5 beta 1 integrin-mediated signaling in tumor cells. J Biol Chem. 2007;282(6):3929-3939.
    • (2007) J Biol Chem , vol.282 , Issue.6 , pp. 3929-3939
    • Wei, Y.1    Tang, C.-H.2    Kim, Y.3
  • 30
    • 54449096395 scopus 로고    scopus 로고
    • Urokinase-type plasminogen activator receptor induces conformational changes in the integrin alphaMbeta2 head-piece and reorientation of its transmembrane domains
    • Tang M-L, Vararattanavech A, Tan S-M. Urokinase-type plasminogen activator receptor induces conformational changes in the integrin alphaMbeta2 head-piece and reorientation of its transmembrane domains. J Biol Chem. 2008;283(37):25392-25403.
    • (2008) J Biol Chem , vol.283 , Issue.37 , pp. 25392-25403
    • Tang, M.-L.1    Vararattanavech, A.2    Tan, S.-M.3
  • 31
    • 65549139348 scopus 로고    scopus 로고
    • Beta1 integrin cytoplasmic domain residues selectively modulate fibronectin matrix assembly and cell spreading through talin and Akt-1
    • Green JA, Berrier AL, Pankov R, Yamada KM. Beta1 integrin cytoplasmic domain residues selectively modulate fibronectin matrix assembly and cell spreading through talin and Akt-1. J Biol Chem. 2009;284(12):8148-8159.
    • (2009) J Biol Chem , vol.284 , Issue.12 , pp. 8148-8159
    • Green, J.A.1    Berrier, A.L.2    Pankov, R.3    Yamada, K.M.4
  • 32
    • 33744948988 scopus 로고    scopus 로고
    • A region in urokinase plasminogen receptor domain III controlling a functional association with alpha5beta1 integrin and tumor growth
    • DOI 10.1074/jbc.M512311200
    • Chaurasia P, Aguirre-Ghiso JA, Liang OD, Gardsvoll H, Ploug M, Ossowski L. A region in urokinase plasminogen receptor domain III controlling a functional association with alpha5beta1 integrin and tumor growth. J Biol Chem. 2006;281(26):14852-14863. (Pubitemid 43855190)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.21 , pp. 14852-14863
    • Chaurasia, P.1    Aguirre-Ghiso, J.A.2    Liang, O.D.3    Gardsvoll, H.4    Ploug, M.5    Ossowski, L.6
  • 33
    • 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
    • DOI 10.1016/S1535-6108(02)00072-7
    • Liu D, Aguirre Ghiso JA, 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(5):445-457. (Pubitemid 41039125)
    • (2002) Cancer Cell , vol.1 , Issue.5 , pp. 445-457
    • Liu, D.1    Aguirre Ghiso, J.A.2    Estrada, Y.3    Ossowski, L.4
  • 34
    • 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
    • DOI 10.1074/jbc.M413141200
    • Jo M, Thomas KS, Marozkina N, et al. Dynamic assembly of the urokinase-type plasminogen activator signaling receptor complex determined the mitogenic activity of urokinase-type plasminogen activator. J Biol Chem. 2005;280(17):17449-17457. (Pubitemid 41389216)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.17 , pp. 17449-17457
    • Jo, M.1    Thomas, K.S.2    Marozkina, N.3    Amin, T.J.4    Silva, C.M.5    Parsons, S.J.6    Gonias, S.L.7
  • 35
    • 34247340196 scopus 로고    scopus 로고
    • Urokinase receptor primes cells to proliferate in response to epidermal growth factor
    • DOI 10.1038/sj.onc.1210066, PII 1210066
    • Jo M, Thomas KS, Takimoto S, et al. Urokinase receptor primes cells to proliferate in response to epidermal growth factor. Oncogene. 2007;26(18):2585-2594. (Pubitemid 46632010)
    • (2007) Oncogene , vol.26 , Issue.18 , pp. 2585-2594
    • Jo, M.1    Thomas, K.S.2    Takimoto, S.3    Gaultier, A.4    Hsieh, E.H.5    Lester, R.D.6    Gonias, S.L.7
  • 36
    • 0033669311 scopus 로고    scopus 로고
    • Two-chain high molecular weight kininogen induces endothelial cell apoptosis and inhibits angiogenesis: Partial activity within domain 5
    • Zhang JC, Claffey K, Sakthivel R, et al. Two-chain high molecular weight kininogen induces endothelial cell apoptosis and inhibits angiogenesis: partial activity within domain 5. FASEB J. 2000;14(15):2589-2600.
    • (2000) FASEB J , vol.14 , Issue.15 , pp. 2589-2600
    • Zhang, J.C.1    Claffey, K.2    Sakthivel, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.