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Volumn 211, Issue 6, 2014, Pages 1167-1183

Imatinib inhibits VEGF-independent angiogenesis by targeting neuropilin 1- dependent ABL1 activation in endothelial cells

Author keywords

[No Author keywords available]

Indexed keywords

ABELSON KINASE; ABL 1 PROTEIN; ACTIN; BCR ABL PROTEIN; FIBRONECTIN; IMATINIB; INTEGRIN; NEUROPILIN 1; PAXILLIN; UNCLASSIFIED DRUG; VASCULOTROPIN A; VASCULOTROPIN RECEPTOR 2;

EID: 84901760004     PISSN: 00221007     EISSN: 15409538     Source Type: Journal    
DOI: 10.1084/jem.20132330     Document Type: Article
Times cited : (114)

References (69)
  • 1
    • 84865153310 scopus 로고    scopus 로고
    • c-ABL modulates MAP kinases activation downstream of VEGFR-2 signaling by direct phosphorylation of the adaptor proteins GRB2 and NCK1
    • Anselmi, F., M. Orlandini, M. Rocchigiani, C. De Clemente, A. Salameh, C. Lentucci, S. Oliviero, and F. Galvagni. 2012. c-ABL modulates MAP kinases activation downstream of VEGFR-2 signaling by direct phosphorylation of the adaptor proteins GRB2 and NCK1. Angiogenesis. 15:187-197. http://dx.doi.org/10.1007/s10456-012-9252-6.
    • (2012) Angiogenesis , vol.15 , pp. 187-197
    • Anselmi, F.1    Orlandini, M.2    Rocchigiani, M.3    De Clemente, C.4    Salameh, A.5    Lentucci, C.6    Oliviero, S.7    Galvagni, F.8
  • 2
    • 79960690759 scopus 로고    scopus 로고
    • Neuropilin-1 promotes VEGFR-2 trafficking through Rab11 vesicles thereby specifying signal output
    • Ballmer-Hofer, K., A.E. Andersson, L.E. Ratcliffe, and P. Berger. 2011. Neuropilin-1 promotes VEGFR-2 trafficking through Rab11 vesicles thereby specifying signal output. Blood. 118:816-826. http://dx.doi.org/ 10.1182/blood-2011-01-328773.
    • (2011) Blood , vol.118 , pp. 816-826
    • Ballmer-Hofer, K.1    Andersson, A.E.2    Ratcliffe, L.E.3    Berger, P.4
  • 3
    • 71549122270 scopus 로고    scopus 로고
    • c-Abl and Src-family kinases cross-talk in regulation of myeloid cell migration
    • Baruzzi, A., I. Iacobucci, S. Soverini, C.A. Lowell, G. Martinelli, and G. Berton. 2010. c-Abl and Src-family kinases cross-talk in regulation of myeloid cell migration. FEBS Lett. 584:15-21. http://dx.doi.org/10.1016/j.febslet.2009.11.009.
    • (2010) FEBS Lett , vol.584 , pp. 15-21
    • Baruzzi, A.1    Iacobucci, I.2    Soverini, S.3    Lowell, C.A.4    Martinelli, G.5    Berton, G.6
  • 4
    • 58149356253 scopus 로고    scopus 로고
    • Paxillin is involved in the differential regulation of endothelial barrier by HGF and VEGF
    • Birukova, A.A., I. Cokic, N. Moldobaeva, and K.G. Birukov. 2009. Paxillin is involved in the differential regulation of endothelial barrier by HGF and VEGF. Am. J. Respir. Cell Mol. Biol. 40:99-107. http://dx.doi.org/ 10.1165/rcmb.2008-0099OC.
    • (2009) Am. J. Respir. Cell Mol. Biol , vol.40 , pp. 99-107
    • Birukova, A.A.1    Cokic, I.2    Moldobaeva, N.3    Birukov, K.G.4
  • 5
    • 0036769158 scopus 로고    scopus 로고
    • Pharmacology of imatinib (STI571)
    • Buchdunger, E., T. O'Reilly, and J. Wood. 2002. Pharmacology of imatinib (STI571). Eur. J. Cancer. 38(Suppl 5):S28-S36. http://dx.doi.org/ 10.1016/S0959-8049(02)80600-1.
    • (2002) Eur. J. Cancer , vol.38 , Issue.SUPPL. 5
    • Buchdunger, E.1    O'Reilly, T.2    Wood, J.3
  • 6
    • 84881336175 scopus 로고    scopus 로고
    • Ocular neovascularization
    • Campochiaro, P.A. 2013. Ocular neovascularization. J. Mol. Med. 91:311-321. http://dx.doi.org/10.1007/s00109-013-0993-5.
    • (2013) J. Mol. Med , vol.91 , pp. 311-321
    • Campochiaro, P.A.1
  • 7
    • 79956328903 scopus 로고    scopus 로고
    • Molecular mechanisms and clinical applications of angiogenesis
    • Carmeliet, P., and R.K. Jain. 2011. Molecular mechanisms and clinical applications of angiogenesis. Nature. 473:298-307. http://dx.doi.org/10.1038/ nature10144.
    • (2011) Nature , vol.473 , pp. 298-307
    • Carmeliet, P.1    Jain, R.K.2
  • 8
    • 26644471951 scopus 로고    scopus 로고
    • Drug resistance by evasion of antiangiogenic targeting of VEGF signaling in late-stage pancreatic islet tumors
    • Casanovas, O., D.J. Hicklin, G. Bergers, and D. Hanahan. 2005. Drug resistance by evasion of antiangiogenic targeting of VEGF signaling in late-stage pancreatic islet tumors. Cancer Cell. 8:299-309. http://dx.doi.org/10.1016/ j.ccr.2005.09.005.
    • (2005) Cancer Cell , vol.8 , pp. 299-309
    • Casanovas, O.1    Hicklin, D.J.2    Bergers, G.3    Hanahan, D.4
  • 9
    • 0029979722 scopus 로고    scopus 로고
    • Phosphorylation of tyrosine 397 in focal adhesion kinase is required for binding phosphatidylinositol 3-kinase
    • Chen, H.C., P.A. Appeddu, H. Isoda, and J.L. Guan. 1996. Phosphorylation of tyrosine 397 in focal adhesion kinase is required for binding phosphatidylinositol 3-kinase. J. Biol Chem. 271:26329-26334. http://dx.doi.org/10.1074/jbc.271.42.26329.
    • (1996) J. Biol Chem , vol.271 , pp. 26329-26334
    • Chen, H.C.1    Appeddu, P.A.2    Isoda, H.3    Guan, J.L.4
  • 10
    • 77149150968 scopus 로고    scopus 로고
    • Anchorage of VEGF to the extracellular matrix conveys differential signaling responses to endothelial cells
    • Chen, T.T., A. Luque, S. Lee, S.M. Anderson, T. Segura, and M.L. Iruela-Arispe. 2010. Anchorage of VEGF to the extracellular matrix conveys differential signaling responses to endothelial cells. J. Cell Biol. 188:595-609. http://dx.doi.org/10.1083/jcb.200906044.
    • (2010) J. Cell Biol , vol.188 , pp. 595-609
    • Chen, T.T.1    Luque, A.2    Lee, S.3    Anderson, S.M.4    Segura, T.5    Iruela-Arispe, M.L.6
  • 11
    • 84880692698 scopus 로고    scopus 로고
    • Abl kinases are required for vascular function, Tie2 expression, and angiopoietin-1-mediated survival
    • Chislock, E.M., C. Ring, and A.M. Pendergast. 2013. Abl kinases are required for vascular function, Tie2 expression, and angiopoietin-1-mediated survival. Proc. Natl. Acad. Sci. USA. 110:12432-12437. http://dx.doi.org/ 10.1073/pnas.1304188110.
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 12432-12437
    • Chislock, E.M.1    Ring, C.2    Pendergast, A.M.3
  • 12
    • 33645508703 scopus 로고    scopus 로고
    • COMP-angiopoietin-1 promotes wound healing through enhanced angiogenesis, lymphangiogenesis, and blood flow in a diabetic mouse model
    • Cho, C.H., H.K. Sung, K.T. Kim, H.G. Cheon, G.T. Oh, H.J. Hong, O.J. Yoo, and G.Y. Koh. 2006. COMP-angiopoietin-1 promotes wound healing through enhanced angiogenesis, lymphangiogenesis, and blood flow in a diabetic mouse model. Proc. Natl. Acad. Sci. USA. 103:4946-4951. http:// dx.doi.org/10.1073/pnas.0506352103.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 4946-4951
    • Cho, C.H.1    Sung, H.K.2    Kim, K.T.3    Cheon, H.G.4    Oh, G.T.5    Hong, H.J.6    Yoo, O.J.7    Koh, G.Y.8
  • 13
    • 34250639027 scopus 로고    scopus 로고
    • Phospholipase C-γ1 potentiates integrin-dependent cell spreading and migration through Pyk2/paxillin activation
    • Choi, J.H., Y.R. Yang, S.K. Lee, I.S. Kim, S.H. Ha, E.K. Kim, Y.S. Bae, S.H. Ryu, and P.G. Suh. 2007. Phospholipase C-γ1 potentiates integrin-dependent cell spreading and migration through Pyk2/paxillin activation. Cell. Signal. 19:1784-1796. http://dx.doi.org/10.1016/j.cellsig.2007.04.002.
    • (2007) Cell. Signal , vol.19 , pp. 1784-1796
    • Choi, J.H.1    Yang, Y.R.2    Lee, S.K.3    Kim, I.S.4    Ha, S.H.5    Kim, E.K.6    Bae, Y.S.7    Ryu, S.H.8    Suh, P.G.9
  • 14
    • 0022453149 scopus 로고
    • Fibronectin mediates adherence of rat alveolar type II epithelial cells via the fibroblastic cell-attachment domain
    • Clark, R.A., R.J. Mason, J.M. Folkvord, and J.A. McDonald. 1986. Fibronectin mediates adherence of rat alveolar type II epithelial cells via the fibroblastic cell-attachment domain. J. Clin. Invest. 77:1831-1840. http:// dx.doi.org/10.1172/JCI112509.
    • (1986) J. Clin. Invest , vol.77 , pp. 1831-1840
    • Clark, R.A.1    Mason, R.J.2    Folkvord, J.M.3    McDonald, J.A.4
  • 15
    • 77956920417 scopus 로고    scopus 로고
    • ABL tyrosine kinases: evolution of function, regulation, and specificity
    • re6
    • Colicelli, J. 2010. ABL tyrosine kinases: evolution of function, regulation, and specificity. Sci. Signal. 3:re6. http://dx.doi.org/10.1126/scisignal.3139re6.
    • (2010) Sci. Signal , vol.3
    • Colicelli, J.1
  • 16
    • 70350036077 scopus 로고    scopus 로고
    • Quantification of oxygen-induced retinopathy in the mouse: a model of vessel loss, vessel regrowth and pathological angiogenesis
    • Connor, K.M., N.M. Krah, R.J. Dennison, C.M. Aderman, J. Chen, K.I. Guerin, P. Sapieha, A. Stahl, K.L. Willett, and L.E. Smith. 2009. Quantification of oxygen-induced retinopathy in the mouse: a model of vessel loss, vessel regrowth and pathological angiogenesis. Nat. Protoc. 4:1565-1573. http://dx.doi.org/10.1038/nprot.2009.187.
    • (2009) Nat. Protoc , vol.4 , pp. 1565-1573
    • Connor, K.M.1    Krah, N.M.2    Dennison, R.J.3    Aderman, C.M.4    Chen, J.5    Guerin, K.I.6    Sapieha, P.7    Stahl, A.8    Willett, K.L.9    Smith, L.E.10
  • 17
    • 64849109776 scopus 로고    scopus 로고
    • c-Abl kinase is required for β2 integrin-mediated neutrophil adhesion
    • Cui, L., C. Chen, T. Xu, J. Zhang, X. Shang, J. Luo, L. Chen, X. Ba, and X. Zeng. 2009. c-Abl kinase is required for β2 integrin-mediated neutrophil adhesion. J. Immunol. 182:3233-3242. http://dx.doi.org/10.4049/jimmunol.0802621.
    • (2009) J. Immunol , vol.182 , pp. 3233-3242
    • Cui, L.1    Chen, C.2    Xu, T.3    Zhang, J.4    Shang, X.5    Luo, J.6    Chen, L.7    Ba, X.8    Zeng, X.9
  • 18
    • 0036008852 scopus 로고    scopus 로고
    • Selection of v-abl tyrosine kinase substrate sequences from randomized peptide and cellular proteomic libraries using mRNA display
    • Cujec, T.P., P.F. Medeiros, P. Hammond, C. Rise, and B.L. Kreider. 2002. Selection of v-abl tyrosine kinase substrate sequences from randomized peptide and cellular proteomic libraries using mRNA display. Chem. Biol. 9:253-264. http://dx.doi.org/10.1016/S1074-5521(02)00098-4.
    • (2002) Chem. Biol , vol.9 , pp. 253-264
    • Cujec, T.P.1    Medeiros, P.F.2    Hammond, P.3    Rise, C.4    Kreider, B.L.5
  • 19
    • 0025259188 scopus 로고
    • Fibrinogen induces endothelial cell adhesion and spreading via the release of endogenous matrix proteins and the recruitment of more than one integrin receptor
    • Dejana, E., M.G. Lampugnani, M. Giorgi, M. Gaboli, and P.C. Marchisio. 1990. Fibrinogen induces endothelial cell adhesion and spreading via the release of endogenous matrix proteins and the recruitment of more than one integrin receptor. Blood. 75:1509-1517.
    • (1990) Blood , vol.75 , pp. 1509-1517
    • Dejana, E.1    Lampugnani, M.G.2    Giorgi, M.3    Gaboli, M.4    Marchisio, P.C.5
  • 20
    • 0029947186 scopus 로고    scopus 로고
    • Effects of a selective inhibitor of the Abl tyrosine kinase on the growth of Bcr-Abl positive cells
    • Druker, B.J., S. Tamura, E. Buchdunger, S. Ohno, G.M. Segal, S. Fanning, J. Zimmermann, and N.B. Lydon. 1996. Effects of a selective inhibitor of the Abl tyrosine kinase on the growth of Bcr-Abl positive cells. Nat. Med. 2:561-566. http://dx.doi.org/10.1038/nm0596-561.
    • (1996) Nat. Med , vol.2 , pp. 561-566
    • Druker, B.J.1    Tamura, S.2    Buchdunger, E.3    Ohno, S.4    Segal, G.M.5    Fanning, S.6    Zimmermann, J.7    Lydon, N.B.8
  • 21
    • 77956273530 scopus 로고    scopus 로고
    • Tissue macrophages act as cellular chaperones for vascular anastomosis downstream of VEGF-mediated endothelial tip cell induction
    • Fantin, A., J.M. Vieira, G. Gestri, L. Denti, Q. Schwarz, S. Prykhozhij, F. Peri, S.W. Wilson, and C. Ruhrberg. 2010. Tissue macrophages act as cellular chaperones for vascular anastomosis downstream of VEGF-mediated endothelial tip cell induction. Blood. 116:829-840. http://dx.doi.org/ 10.1182/blood-2009-12-257832.
    • (2010) Blood , vol.116 , pp. 829-840
    • Fantin, A.1    Vieira, J.M.2    Gestri, G.3    Denti, L.4    Schwarz, Q.5    Prykhozhij, S.6    Peri, F.7    Wilson, S.W.8    Ruhrberg, C.9
  • 22
    • 80052515065 scopus 로고    scopus 로고
    • The cytoplasmic domain of neuropilin 1 is dispensable for angiogenesis, but promotes the spatial separation of retinal arteries and veins
    • Fantin, A., Q. Schwarz, K. Davidson, E.M. Normando, L. Denti, and C. Ruhrberg. 2011. The cytoplasmic domain of neuropilin 1 is dispensable for angiogenesis, but promotes the spatial separation of retinal arteries and veins. Development. 138:4185-4191. http://dx.doi.org/10.1242/dev.070037.
    • (2011) Development , vol.138 , pp. 4185-4191
    • Fantin, A.1    Schwarz, Q.2    Davidson, K.3    Normando, E.M.4    Denti, L.5    Ruhrberg, C.6
  • 23
    • 84877929726 scopus 로고    scopus 로고
    • NRP1 acts cell autonomously in endothelium to promote tip cell function during sprouting angiogenesis
    • Fantin, A., J.M. Vieira, A. Plein, L. Denti, M. Fruttiger, J.W. Pollard, and C. Ruhrberg. 2013. NRP1 acts cell autonomously in endothelium to promote tip cell function during sprouting angiogenesis. Blood. 121:2352-2362. http://dx.doi.org/10.1182/blood-2012-05-424713.
    • (2013) Blood , vol.121 , pp. 2352-2362
    • Fantin, A.1    Vieira, J.M.2    Plein, A.3    Denti, L.4    Fruttiger, M.5    Pollard, J.W.6    Ruhrberg, C.7
  • 24
    • 84892730229 scopus 로고    scopus 로고
    • Neuropilin 1 (NRP1) hypomorphism combined with defective VEGF-A binding reveals novel roles for NRP1 in developmental and pathological angiogenesis
    • Fantin, A., B. Herzog, M. Mahmoud, M. Yamaji, A. Plein, L. Denti, C. Ruhrberg, and I. Zachary. 2014. Neuropilin 1 (NRP1) hypomorphism combined with defective VEGF-A binding reveals novel roles for NRP1 in developmental and pathological angiogenesis. Development. 141:556-562. http://dx.doi.org/10.1242/dev.103028.
    • (2014) Development , vol.141 , pp. 556-562
    • Fantin, A.1    Herzog, B.2    Mahmoud, M.3    Yamaji, M.4    Plein, A.5    Denti, L.6    Ruhrberg, C.7    Zachary, I.8
  • 25
    • 84875185167 scopus 로고    scopus 로고
    • VEGF-A is necessary and sufficient for retinal neuroprotection in models of experimental glaucoma
    • Foxton, R.H., A. Finkelstein, S. Vijay, A. Dahlmann-Noor, P.T. Khaw, J.E. Morgan, D.T. Shima, and Y.S. Ng. 2013. VEGF-A is necessary and sufficient for retinal neuroprotection in models of experimental glaucoma. Am. J. Pathol. 182:1379-1390. http://dx.doi.org/10.1016/j.ajpath.2012.12.032.
    • (2013) Am. J. Pathol , vol.182 , pp. 1379-1390
    • Foxton, R.H.1    Finkelstein, A.2    Vijay, S.3    Dahlmann-Noor, A.4    Khaw, P.T.5    Morgan, J.E.6    Shima, D.T.7    Ng, Y.S.8
  • 26
    • 35948965519 scopus 로고    scopus 로고
    • Neuropilin-1 interacts with integrin beta1 and modulates pancreatic cancer cell growth, survival and invasion
    • Fukasawa, M., A. Matsushita, and M. Korc. 2007. Neuropilin-1 interacts with integrin beta1 and modulates pancreatic cancer cell growth, survival and invasion. Cancer Biol. Ther. 6:1184-1191. http://dx.doi.org/10.4161/cbt.6.8.4363.
    • (2007) Cancer Biol. Ther , vol.6 , pp. 1184-1191
    • Fukasawa, M.1    Matsushita, A.2    Korc, M.3
  • 28
    • 6944225400 scopus 로고    scopus 로고
    • Neuropilin-1 is required for endothelial tip cell guidance in the developing central nervous system
    • Gerhardt, H., C. Ruhrberg, A. Abramsson, H. Fujisawa, D. Shima, and C. Betsholtz. 2004. Neuropilin-1 is required for endothelial tip cell guidance in the developing central nervous system. Dev. Dyn. 231:503-509. http://dx.doi.org/10.1002/dvdy.20148.
    • (2004) Dev. Dyn , vol.231 , pp. 503-509
    • Gerhardt, H.1    Ruhrberg, C.2    Abramsson, A.3    Fujisawa, H.4    Shima, D.5    Betsholtz, C.6
  • 29
    • 79961042374 scopus 로고    scopus 로고
    • VEGF binding to NRP1 is essential for VEGF stimulation of endothelial cell migration, complex formation between NRP1 and VEGFR2, and signaling via FAK Tyr407 phosphorylation
    • Herzog, B., C. Pellet-Many, G. Britton, B. Hartzoulakis, and I.C. Zachary. 2011. VEGF binding to NRP1 is essential for VEGF stimulation of endothelial cell migration, complex formation between NRP1 and VEGFR2, and signaling via FAK Tyr407 phosphorylation. Mol. Biol. Cell. 22:2766-2776. http://dx.doi.org/10.1091/mbc.E09-12-1061.
    • (2011) Mol. Biol. Cell , vol.22 , pp. 2766-2776
    • Herzog, B.1    Pellet-Many, C.2    Britton, G.3    Hartzoulakis, B.4    Zachary, I.C.5
  • 32
    • 84864149171 scopus 로고    scopus 로고
    • A brief history of anti-VEGF for the treatment of ocular angiogenesis
    • Kim, L.A., and P.A. D'Amore. 2012. A brief history of anti-VEGF for the treatment of ocular angiogenesis. Am. J. Pathol. 181:376-379. http:// dx.doi.org/10.1016/j.ajpath.2012.06.006.
    • (2012) Am. J. Pathol , vol.181 , pp. 376-379
    • Kim, L.A.1    D'Amore, P.A.2
  • 33
    • 0030778454 scopus 로고    scopus 로고
    • Neuropilin-semaphorin III/D-mediated chemorepulsive signals play a crucial role in peripheral nerve projection in mice
    • Kitsukawa, T., M. Shimizu, M. Sanbo, T. Hirata, M. Taniguchi, Y. Bekku, T. Yagi, and H. Fujisawa. 1997. Neuropilin-semaphorin III/D-mediated chemorepulsive signals play a crucial role in peripheral nerve projection in mice. Neuron. 19:995-1005. http://dx.doi.org/10.1016/S0896-6273(00)80392-X.
    • (1997) Neuron , vol.19 , pp. 995-1005
    • Kitsukawa, T.1    Shimizu, M.2    Sanbo, M.3    Hirata, T.4    Taniguchi, M.5    Bekku, Y.6    Yagi, T.7    Fujisawa, H.8
  • 34
    • 79957902010 scopus 로고    scopus 로고
    • Signal transduction by vascular endothelial growth factor receptors
    • Koch, S., S. Tugues, X. Li, L. Gualandi, and L. Claesson-Welsh. 2011. Signal transduction by vascular endothelial growth factor receptors. Biochem. J. 437:169-183. http://dx.doi.org/10.1042/BJ20110301.
    • (2011) Biochem. J , vol.437 , pp. 169-183
    • Koch, S.1    Tugues, S.2    Li, X.3    Gualandi, L.4    Claesson-Welsh, L.5
  • 37
    • 0032486386 scopus 로고    scopus 로고
    • Integrins regulate the association and phosphorylation of paxillin by c-Abl
    • Lewis, J.M., and M.A. Schwartz. 1998. Integrins regulate the association and phosphorylation of paxillin by c-Abl. J. Biol. Chem. 273:14225-14230. http://dx.doi.org/10.1074/jbc.273.23.14225.
    • (1998) J. Biol. Chem , vol.273 , pp. 14225-14230
    • Lewis, J.M.1    Schwartz, M.A.2
  • 38
    • 0030459950 scopus 로고    scopus 로고
    • Integrin regulation of c-Abl tyrosine kinase activity and cytoplasmicnuclear transport
    • Lewis, J.M., R. Baskaran, S. Taagepera, M.A. Schwartz, and J.Y. Wang. 1996. Integrin regulation of c-Abl tyrosine kinase activity and cytoplasmicnuclear transport. Proc. Natl. Acad. Sci. USA. 93:15174-15179. http:// dx.doi.org/10.1073/pnas.93.26.15174.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 15174-15179
    • Lewis, J.M.1    Baskaran, R.2    Taagepera, S.3    Schwartz, M.A.4    Wang, J.Y.5
  • 39
    • 0037025311 scopus 로고    scopus 로고
    • Neuropilin-1 binds vascular endothelial growth factor 165, placenta growth factor-2, and heparin via its b1b2 domain
    • Mamluk, R., Z. Gechtman, M.E. Kutcher, N. Gasiunas, J. Gallagher, and M. Klagsbrun. 2002. Neuropilin-1 binds vascular endothelial growth factor 165, placenta growth factor-2, and heparin via its b1b2 domain. J. Biol. Chem. 277:24818-24825. http://dx.doi.org/10.1074/jbc.M200730200.
    • (2002) J. Biol. Chem , vol.277 , pp. 24818-24825
    • Mamluk, R.1    Gechtman, Z.2    Kutcher, M.E.3    Gasiunas, N.4    Gallagher, J.5    Klagsbrun, M.6
  • 40
    • 14944344614 scopus 로고    scopus 로고
    • Neuropilin-1 regulates attachment in human endothelial cells independently of vascular endothelial growth factor receptor-2
    • Murga, M., O. Fernandez-Capetillo, and G. Tosato. 2005. Neuropilin-1 regulates attachment in human endothelial cells independently of vascular endothelial growth factor receptor-2. Blood. 105:1992-1999. http:// dx.doi.org/10.1182/blood-2004-07-2598.
    • (2005) Blood , vol.105 , pp. 1992-1999
    • Murga, M.1    Fernandez-Capetillo, O.2    Tosato, G.3
  • 41
    • 34547702738 scopus 로고    scopus 로고
    • Vascular endothelial growth factor-A is a survival factor for retinal neurons and a critical neuroprotectant during the adaptive response to ischemic injury
    • Nishijima, K., Y.S. Ng, L. Zhong, J. Bradley, W. Schubert, N. Jo, J. Akita, S.J. Samuelsson, G.S. Robinson, A.P. Adamis, and D.T. Shima. 2007. Vascular endothelial growth factor-A is a survival factor for retinal neurons and a critical neuroprotectant during the adaptive response to ischemic injury. Am. J. Pathol. 171:53-67. http://dx.doi.org/10.2353/ajpath.2007.061237.
    • (2007) Am. J. Pathol , vol.171 , pp. 53-67
    • Nishijima, K.1    Ng, Y.S.2    Zhong, L.3    Bradley, J.4    Schubert, W.5    Jo, N.6    Akita, J.7    Samuelsson, S.J.8    Robinson, G.S.9    Adamis, A.P.10    Shima, D.T.11
  • 44
    • 0034693854 scopus 로고    scopus 로고
    • Focal adhesion kinase: a regulator of focal adhesion dynamics and cell movement
    • Parsons, J.T., K.H. Martin, J.K. Slack, J.M. Taylor, and S.A. Weed. 2000. Focal adhesion kinase: a regulator of focal adhesion dynamics and cell movement. Oncogene. 19:5606-5613. http://dx.doi.org/10.1038/sj.onc.1203877.
    • (2000) Oncogene , vol.19 , pp. 5606-5613
    • Parsons, J.T.1    Martin, K.H.2    Slack, J.K.3    Taylor, J.M.4    Weed, S.A.5
  • 45
    • 77949754056 scopus 로고    scopus 로고
    • Myosin II activity regulates vinculin recruitment to focal adhesions through FAK-mediated paxillin phosphorylation
    • Pasapera, A.M., I.C. Schneider, E. Rericha, D.D. Schlaepfer, and C.M. Waterman. 2010. Myosin II activity regulates vinculin recruitment to focal adhesions through FAK-mediated paxillin phosphorylation. J. Cell Biol. 188:877-890. http://dx.doi.org/10.1083/jcb.200906012.
    • (2010) J. Cell Biol , vol.188 , pp. 877-890
    • Pasapera, A.M.1    Schneider, I.C.2    Rericha, E.3    Schlaepfer, D.D.4    Waterman, C.M.5
  • 46
    • 84884258983 scopus 로고    scopus 로고
    • Filopodia are dispensable for endothelial tip cell guidance
    • Phng, L.K., F. Stanchi, and H. Gerhardt. 2013. Filopodia are dispensable for endothelial tip cell guidance. Development. 140:4031-4040. http://dx.doi.org/10.1242/dev.097352.
    • (2013) Development , vol.140 , pp. 4031-4040
    • Phng, L.K.1    Stanchi, F.2    Gerhardt, H.3
  • 47
    • 84875631991 scopus 로고    scopus 로고
    • Neuropilin signalling in vessels, neurons and tumours
    • Raimondi, C., and C. Ruhrberg. 2013. Neuropilin signalling in vessels, neurons and tumours. Semin. Cell Dev. Biol. 24:172-178. http://dx.doi.org/10.1016/j.semcdb.2013.01.001.
    • (2013) Semin. Cell Dev. Biol , vol.24 , pp. 172-178
    • Raimondi, C.1    Ruhrberg, C.2
  • 50
    • 0034687708 scopus 로고    scopus 로고
    • Functional interaction between c-Abl and the p21-activated protein kinase gamma-PAK
    • Roig, J., P.T. Tuazon, P.A. Zipfel, A.M. Pendergast, and J.A. Traugh. 2000. Functional interaction between c-Abl and the p21-activated protein kinase gamma-PAK. Proc. Natl. Acad. Sci. USA. 97:14346-14351. http:// dx.doi.org/10.1073/pnas.97.26.14346.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 14346-14351
    • Roig, J.1    Tuazon, P.T.2    Zipfel, P.A.3    Pendergast, A.M.4    Traugh, J.A.5
  • 51
    • 33749445317 scopus 로고    scopus 로고
    • Ranibizumab for neovascular age-related macular degeneration
    • MARINA Study Group
    • Rosenfeld, P.J., D.M. Brown, J.S. Heier, D.S. Boyer, P.K. Kaiser, C.Y. Chung, and R.Y. Kim; MARINA Study Group. 2006. Ranibizumab for neovascular age-related macular degeneration. N. Engl. J. Med. 355:1419-1431. http://dx.doi.org/10.1056/NEJMoa054481.
    • (2006) N. Engl. J. Med , vol.355 , pp. 1419-1431
    • Rosenfeld, P.J.1    Brown, D.M.2    Heier, J.S.3    Boyer, D.S.4    Kaiser, P.K.5    Chung, C.Y.6    Kim, R.Y.7
  • 52
    • 0242636164 scopus 로고    scopus 로고
    • Growing and shaping the vascular tree: multiple roles for VEGF
    • Ruhrberg, C. 2003. Growing and shaping the vascular tree: multiple roles for VEGF. Bioessays. 25:1052-1060. http://dx.doi.org/10.1002/bies.10351.
    • (2003) Bioessays , vol.25 , pp. 1052-1060
    • Ruhrberg, C.1
  • 53
    • 0037108152 scopus 로고    scopus 로고
    • Spatially restricted patterning cues provided by heparin-binding VEGF-A control blood vessel branching morphogenesis
    • Ruhrberg, C., H. Gerhardt, M. Golding, R. Watson, S. Ioannidou, H. Fujisawa, C. Betsholtz, and D.T. Shima. 2002. Spatially restricted patterning cues provided by heparin-binding VEGF-A control blood vessel branching morphogenesis. Genes Dev. 16:2684-2698. http://dx.doi.org/10.1101/gad.242002.
    • (2002) Genes Dev , vol.16 , pp. 2684-2698
    • Ruhrberg, C.1    Gerhardt, H.2    Golding, M.3    Watson, R.4    Ioannidou, S.5    Fujisawa, H.6    Betsholtz, C.7    Shima, D.T.8
  • 55
    • 53249096017 scopus 로고    scopus 로고
    • Vascular endothelial growth factor and semaphorin induce neuropilin-1 endocytosis via separate pathways
    • Salikhova, A., L. Wang, A.A. Lanahan, M. Liu, M. Simons, W.P. Leenders, D. Mukhopadhyay, and A. Horowitz. 2008. Vascular endothelial growth factor and semaphorin induce neuropilin-1 endocytosis via separate pathways. Circ. Res. 103:e71-e79. http://dx.doi.org/10.1161/CIRCRESAHA.108.183327.
    • (2008) Circ. Res , vol.103
    • Salikhova, A.1    Wang, L.2    Lanahan, A.A.3    Liu, M.4    Simons, M.5    Leenders, W.P.6    Mukhopadhyay, D.7    Horowitz, A.8
  • 56
    • 0034688995 scopus 로고    scopus 로고
    • Determination of cell adhesion sites of neuropilin-1
    • Shimizu, M., Y. Murakami, F. Suto, and H. Fujisawa. 2000. Determination of cell adhesion sites of neuropilin-1. J. Cell Biol. 148:1283-1294. http:// dx.doi.org/10.1083/jcb.148.6.1283.
    • (2000) J. Cell Biol , vol.148 , pp. 1283-1294
    • Shimizu, M.1    Murakami, Y.2    Suto, F.3    Fujisawa, H.4
  • 59
    • 0036009760 scopus 로고    scopus 로고
    • VEGF165 mediates formation of complexes containing VEGFR-2 and neuropilin-1 that enhance VEGF165-receptor binding
    • Soker, S., H.Q. Miao, M. Nomi, S. Takashima, and M. Klagsbrun. 2002. VEGF165 mediates formation of complexes containing VEGFR-2 and neuropilin-1 that enhance VEGF165-receptor binding. J. Cell. Biochem. 85:357-368. http://dx.doi.org/10.1002/jcb.10140.
    • (2002) J. Cell. Biochem , vol.85 , pp. 357-368
    • Soker, S.1    Miao, H.Q.2    Nomi, M.3    Takashima, S.4    Klagsbrun, M.5
  • 60
    • 0031730895 scopus 로고    scopus 로고
    • Fibronectin matrix assembly enhances adhesion-dependent cell growth
    • Sottile, J., D.C. Hocking, and P.J. Swiatek. 1998. Fibronectin matrix assembly enhances adhesion-dependent cell growth. J. Cell Sci. 111:2933-2943.
    • (1998) J. Cell Sci , vol.111 , pp. 2933-2943
    • Sottile, J.1    Hocking, D.C.2    Swiatek, P.J.3
  • 62
    • 14644397216 scopus 로고    scopus 로고
    • Integrin-dependent PLC-γ1 phosphorylation mediates fibronectin-dependent adhesion
    • Tvorogov, D., X.J. Wang, R. Zent, and G. Carpenter. 2005. Integrin-dependent PLC-γ1 phosphorylation mediates fibronectin-dependent adhesion. J. Cell Sci. 118:601-610. http://dx.doi.org/10.1242/jcs.01643.
    • (2005) J. Cell Sci , vol.118 , pp. 601-610
    • Tvorogov, D.1    Wang, X.J.2    Zent, R.3    Carpenter, G.4
  • 63
    • 32444434289 scopus 로고    scopus 로고
    • Tlx acts as a proangiogenic switch by regulating extracellular assembly of fibronectin matrices in retinal astrocytes
    • Uemura, A., S. Kusuhara, S.J. Wiegand, R.T. Yu, and S. Nishikawa. 2006. Tlx acts as a proangiogenic switch by regulating extracellular assembly of fibronectin matrices in retinal astrocytes. J. Clin. Invest. 116:369-377. http://dx.doi.org/10.1172/JCI25964.
    • (2006) J. Clin. Invest , vol.116 , pp. 369-377
    • Uemura, A.1    Kusuhara, S.2    Wiegand, S.J.3    Yu, R.T.4    Nishikawa, S.5
  • 65
    • 33845678052 scopus 로고    scopus 로고
    • C terminus of RGSGAIP-interacting protein conveys neuropilin-1-mediated signaling during angiogenesis
    • Wang, L., D. Mukhopadhyay, and X. Xu. 2006. C terminus of RGSGAIP-interacting protein conveys neuropilin-1-mediated signaling during angiogenesis. FASEB J. 20:1513-1515. http://dx.doi.org/10.1096/ fj.05-5504fje.
    • (2006) FASEB J , vol.20 , pp. 1513-1515
    • Wang, L.1    Mukhopadhyay, D.2    Xu, X.3
  • 66
    • 84881232071 scopus 로고    scopus 로고
    • Recent molecular discoveries in angiogenesis and antiangiogenic therapies in cancer
    • Welti, J., S. Loges, S. Dimmeler, and P. Carmeliet. 2013. Recent molecular discoveries in angiogenesis and antiangiogenic therapies in cancer. J. Clin. Invest. 123:3190-3200. http://dx.doi.org/10.1172/JCI70212.
    • (2013) J. Clin. Invest , vol.123 , pp. 3190-3200
    • Welti, J.1    Loges, S.2    Dimmeler, S.3    Carmeliet, P.4
  • 67
    • 84865140752 scopus 로고    scopus 로고
    • Neuropilin-1 stimulates tumor growth by increasing fibronectin fibril assembly in the tumor microenvironment
    • Yaqoob, U., S. Cao, U. Shergill, K. Jagavelu, Z. Geng, M. Yin, T.M. de Assuncao, Y. Cao, A. Szabolcs, S. Thorgeirsson, et al. 2012. Neuropilin-1 stimulates tumor growth by increasing fibronectin fibril assembly in the tumor microenvironment. Cancer Res. 72:4047-4059. http://dx.doi.org/10.1158/0008-5472.CAN-11-3907.
    • (2012) Cancer Res , vol.72 , pp. 4047-4059
    • Yaqoob, U.1    Cao, S.2    Shergill, U.3    Jagavelu, K.4    Geng, Z.5    Yin, M.6    de Assuncao, T.M.7    Cao, Y.8    Szabolcs, A.9    Thorgeirsson, S.10
  • 68
    • 33846781373 scopus 로고    scopus 로고
    • A paxillin tyrosine phosphorylation switch regulates the assembly and form of cell-matrix adhesions
    • Zaidel-Bar, R., R. Milo, Z. Kam, and B. Geiger. 2007. A paxillin tyrosine phosphorylation switch regulates the assembly and form of cell-matrix adhesions. J. Cell Sci. 120:137-148. http://dx.doi.org/10.1242/jcs.03314.
    • (2007) J. Cell Sci , vol.120 , pp. 137-148
    • Zaidel-Bar, R.1    Milo, R.2    Kam, Z.3    Geiger, B.4
  • 69
    • 84866093563 scopus 로고    scopus 로고
    • Tumour-secreted miR-9 promotes endothelial cell migration and angiogenesis by activating the JAKSTAT pathway
    • Zhuang, G., X. Wu, Z. Jiang, I. Kasman, J. Yao, Y. Guan, J. Oeh, Z. Modrusan, C. Bais, D. Sampath, and N. Ferrara. 2012. Tumour-secreted miR-9 promotes endothelial cell migration and angiogenesis by activating the JAKSTAT pathway. EMBO J. 31:3513-3523. http://dx.doi.org/10.1038/ emboj.2012.183.
    • (2012) EMBO J , vol.31 , pp. 3513-3523
    • Zhuang, G.1    Wu, X.2    Jiang, Z.3    Kasman, I.4    Yao, J.5    Guan, Y.6    Oeh, J.7    Modrusan, Z.8    Bais, C.9    Sampath, D.10    Ferrara, N.11


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