메뉴 건너뛰기




Volumn 5, Issue 2, 2014, Pages 157-166

Control of cellular motility by neuropilin-mediated physical interactions

Author keywords

cellular motility; neuropilin; receptor signaling; semaphorin; VEGF

Indexed keywords

NEUROPILIN; SEMAPHORIN; VASCULOTROPIN A;

EID: 84900412270     PISSN: 18685021     EISSN: 1868503X     Source Type: Journal    
DOI: 10.1515/bmc-2013-0035     Document Type: Review
Times cited : (6)

References (133)
  • 1
    • 84870206736 scopus 로고    scopus 로고
    • Function of members of the neuropilin family as essential pleiotropic cell surface receptors
    • Parker MW, Guo HF, Li X, Linkugel AD, Vander Kooi CW. Function of members of the neuropilin family as essential pleiotropic cell surface receptors. Biochemistry 2012; 51: 9437-46.
    • (2012) Biochemistry , vol.51 , pp. 9437-9446
    • Parker, M.W.1    Guo, H.F.2    Li, X.3    Linkugel, A.D.4    Vander Kooi, C.W.5
  • 2
    • 84934444702 scopus 로고    scopus 로고
    • Semaphorin signals in cell adhesion and cell migration: Functional role and molecular mechanisms
    • Casazza A, Fazzari P, Tamagnone L. Semaphorin signals in cell adhesion and cell migration: functional role and molecular mechanisms. Adv Exp Med Biol 2007; 600: 90-108.
    • (2007) Adv Exp Med Biol , vol.600 , pp. 90-108
    • Casazza, A.1    Fazzari, P.2    Tamagnone, L.3
  • 3
    • 84872065517 scopus 로고    scopus 로고
    • Autocrine functions of VEGF in breast tumor cells: Adhesion, survival, migration and invasion
    • Perrot-Applanat M, Di Benedetto M. Autocrine functions of VEGF in breast tumor cells: adhesion, survival, migration and invasion. Cell Adh Migr 2012; 6: 547-53.
    • (2012) Cell Adh Migr , vol.6 , pp. 547-553
    • Perrot-Applanat, M.1    Di Benedetto, M.2
  • 5
    • 0036942108 scopus 로고    scopus 로고
    • Neuropilins as Semaphorin receptors: In vivo functions in neuronal cell migration and axon guidance
    • Bagri A, Tessier-Lavigne M. Neuropilins as Semaphorin receptors: in vivo functions in neuronal cell migration and axon guidance. Adv Exp Med Biol 2002; 515: 13-31.
    • (2002) Adv Exp Med Biol , vol.515 , pp. 13-31
    • Bagri, A.1    Tessier-Lavigne, M.2
  • 7
    • 0030847193 scopus 로고    scopus 로고
    • Neuropilin is a receptor for the axonal chemorepellent Semaphorin III
    • He Z, Tessier-Lavigne M. Neuropilin is a receptor for the axonal chemorepellent Semaphorin III. Cell 1997; 90: 739-51.
    • (1997) Cell , vol.90 , pp. 739-751
    • He, Z.1    Tessier-Lavigne, M.2
  • 9
    • 0032549799 scopus 로고    scopus 로고
    • Neuropilin-1 is expressed by endothelial and tumor cells as an isoform-specific receptor for vascular endothelial growth factor
    • Soker S, Takashima S, Miao HQ, Neufeld G, Klagsbrun M. Neuropilin-1 is expressed by endothelial and tumor cells as an isoform-specific receptor for vascular endothelial growth factor. Cell 1998; 92: 735-45.
    • (1998) Cell , vol.92 , pp. 735-745
    • Soker, S.1    Takashima, S.2    Miao, H.Q.3    Neufeld, G.4    Klagsbrun, M.5
  • 11
    • 84880742193 scopus 로고    scopus 로고
    • Signal transduction by vascular endothelial growth factor receptors
    • Koch S, Claesson-Welsh L. Signal transduction by vascular endothelial growth factor receptors. Cold Spring Harb Perspect Med 2012; 2: a006502.
    • (2012) Cold Spring Harb Perspect Med , vol.2
    • Koch, S.1    Claesson-Welsh, L.2
  • 12
    • 84855261162 scopus 로고    scopus 로고
    • The reception and the party after: How vascular endothelial growth factor receptor 2 explores cytoplasmic space
    • Berger P, Ballmer-Hofer K. The reception and the party after: how vascular endothelial growth factor receptor 2 explores cytoplasmic space. Swiss Med Wkly 2011; 141: w13318.
    • (2011) Swiss Med Wkly , vol.141
    • Berger, P.1    Ballmer-Hofer, K.2
  • 13
    • 84867848485 scopus 로고    scopus 로고
    • Plexin structures are coming: Opportunities for multilevel investigations of semaphorin guidance receptors, their cell signaling mechanisms, and functions
    • Hota PK, Buck M. Plexin structures are coming: opportunities for multilevel investigations of semaphorin guidance receptors, their cell signaling mechanisms, and functions. Cell Mol Life Sci 2012; 69: 3765-805.
    • (2012) Cell Mol Life Sci , vol.69 , pp. 3765-3805
    • Hota, P.K.1    Buck, M.2
  • 14
    • 77449085256 scopus 로고    scopus 로고
    • Neuropilin, you gotta let me know: Should I stay or should I go?
    • Schwarz Q, Ruhrberg C. Neuropilin, you gotta let me know: should I stay or should I go? Cell Adh Migr 2010; 4: 61-6.
    • (2010) Cell Adh Migr , vol.4 , pp. 61-66
    • Schwarz, Q.1    Ruhrberg, C.2
  • 15
    • 84872089227 scopus 로고    scopus 로고
    • Enhancing integrin function by VEGF/neuropilin signaling: Implications for tumor biology
    • Goel HL, Mercurio AM. Enhancing integrin function by VEGF/neuropilin signaling: implications for tumor biology. Cell Adh Migr 2012; 6: 554-60.
    • (2012) Cell Adh Migr , vol.6 , pp. 554-560
    • Goel, H.L.1    Mercurio, A.M.2
  • 16
    • 0034282885 scopus 로고    scopus 로고
    • The interaction of neuropilin-1 with vascular endothelial growth factor and its receptor flt-1
    • Fuh G, Garcia KC, de Vos AM. The interaction of neuropilin-1 with vascular endothelial growth factor and its receptor flt-1. J Biol Chem 2000; 275: 26690-5.
    • (2000) J Biol Chem , vol.275 , pp. 26690-26695
    • Fuh, G.1    Garcia, K.C.2    De Vos, A.M.3
  • 17
    • 84934441066 scopus 로고    scopus 로고
    • Proteoglycans as modulators of axon guidance cue function
    • de Wit J, Verhaagen J. Proteoglycans as modulators of axon guidance cue function. Adv Exp Med Biol 2007; 600: 73-89.
    • (2007) Adv Exp Med Biol , vol.600 , pp. 73-89
    • De Wit, J.1    Verhaagen, J.2
  • 18
    • 0025866476 scopus 로고
    • The A5 antigen, a candidate for the neuronal recognition molecule, has homologies to complement components and coagulation factors
    • Takagi S, Hirata T, Agata K, Mochii M, Eguchi G, Fujisawa H. The A5 antigen, a candidate for the neuronal recognition molecule, has homologies to complement components and coagulation factors. Neuron 1991; 7: 295-307.
    • (1991) Neuron , vol.7 , pp. 295-307
    • Takagi, S.1    Hirata, T.2    Agata, K.3    Mochii, M.4    Eguchi, G.5    Fujisawa, H.6
  • 21
    • 0033179591 scopus 로고    scopus 로고
    • Cloning and characterization of neuropilin- 1-interacting protein: A PSD-95/Dlg/ZO-1 domain-containing protein that interacts with the cytoplasmic domain of neuropilin-1
    • Cai H, Reed RR. Cloning and characterization of neuropilin- 1-interacting protein: a PSD-95/Dlg/ZO-1 domain-containing protein that interacts with the cytoplasmic domain of neuropilin-1. J Neurosci 1999; 19: 6519-27.
    • (1999) J Neurosci , vol.19 , pp. 6519-6527
    • Cai, H.1    Reed, R.R.2
  • 22
    • 33845678052 scopus 로고    scopus 로고
    • C terminus of RGS-GAIPinteracting protein conveys neuropilin-1-mediated signaling during angiogenesis
    • Wang L, Mukhopadhyay D, Xu X. C terminus of RGS-GAIPinteracting protein conveys neuropilin-1-mediated signaling during angiogenesis. FASEB J 2006; 20: 1513-5.
    • (2006) FASEB J , vol.20 , pp. 1513-1515
    • Wang, L.1    Mukhopadhyay, D.2    Xu, X.3
  • 26
    • 0037124068 scopus 로고    scopus 로고
    • Characterization of neuropilin-1 structural features that confer binding to semaphorin 3A and vascular endothelial growth factor 165
    • Gu C, Limberg BJ, Whitaker GB, Perman B, Leahy DJ, Rosenbaum JS, Ginty DD, Kolodkin AL. Characterization of neuropilin-1 structural features that confer binding to semaphorin 3A and vascular endothelial growth factor 165. J Biol Chem 2002; 277: 18069-76.
    • (2002) J Biol Chem , vol.277 , pp. 18069-18076
    • Gu, C.1    Limberg, B.J.2    Whitaker, G.B.3    Perman, B.4    Leahy, D.J.5    Rosenbaum, J.S.6    Ginty, D.D.7    Kolodkin, A.L.8
  • 27
    • 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, Gechtman Z, Kutcher ME, Gasiunas N, Gallagher J, Klagsbrun M. Neuropilin-1 binds vascular endothelial growth factor 165, placenta growth factor-2, and heparin via its b1b2 domain. J Biol Chem 2002; 277: 24818-25.
    • (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
  • 28
    • 84869038134 scopus 로고    scopus 로고
    • Mechanism of selective VEGF-A binding by neuropilin-1 reveals a basis for specific ligand inhibition
    • Parker MW, Xu P, Guo HF, Vander Kooi CW. Mechanism of selective VEGF-A binding by neuropilin-1 reveals a basis for specific ligand inhibition. PLoS One 2012; 7: e49177.
    • (2012) PLoS One , vol.7
    • Parker, M.W.1    Xu, P.2    Guo, H.F.3    Vander Kooi, C.W.4
  • 29
    • 84859488831 scopus 로고    scopus 로고
    • Structural basis for selective vascular endothelial growth factor-A (VEGF-A) binding to neuropilin-1
    • Parker MW, Xu P, Li X, Vander Kooi CW. Structural basis for selective vascular endothelial growth factor-A (VEGF-A) binding to neuropilin-1. J Biol Chem 2012; 287: 11082-9.
    • (2012) J Biol Chem , vol.287 , pp. 11082-11089
    • Parker, M.W.1    Xu, P.2    Li, X.3    Vander Kooi, C.W.4
  • 30
    • 0032408496 scopus 로고    scopus 로고
    • Semaphorinneuropilin interactions underlying sympathetic axon responses to class III semaphorins
    • Chen H, He Z, Bagri A, Tessier-Lavigne M. Semaphorinneuropilin interactions underlying sympathetic axon responses to class III semaphorins. Neuron 1998; 21: 1283-90.
    • (1998) Neuron , vol.21 , pp. 1283-1290
    • Chen, H.1    He, Z.2    Bagri, A.3    Tessier-Lavigne, M.4
  • 31
    • 0030886550 scopus 로고    scopus 로고
    • A 70 amino acid region within the semaphorin domain activates specific cellular response of semaphorin family members
    • Koppel AM, Feiner L, Kobayashi H, Raper JA. A 70 amino acid region within the semaphorin domain activates specific cellular response of semaphorin family members. Neuron 19: 531-7.
    • Neuron , vol.19 , pp. 531-537
    • Koppel, A.M.1    Feiner, L.2    Kobayashi, H.3    Raper, J.A.4
  • 32
    • 0032215144 scopus 로고    scopus 로고
    • Neuropilin-2 is a receptor for semaphorin IV: Insight into the structural basis of receptor function and specificity
    • Giger RJ, Urquhart ER, Gillespie SK, Levengood DV, Ginty DD, Kolodkin AL. Neuropilin-2 is a receptor for semaphorin IV: insight into the structural basis of receptor function and specificity. Neuron 1998; 21: 1079-92.
    • (1998) Neuron , vol.21 , pp. 1079-1092
    • Giger, R.J.1    Urquhart, E.R.2    Gillespie, S.K.3    Levengood, D.V.4    Ginty, D.D.5    Kolodkin, A.L.6
  • 33
    • 0032215735 scopus 로고    scopus 로고
    • Neuropilin-1 extracellular domains mediate semaphorin D/III-induced growth cone collapse
    • Nakamura F, Tanaka M, Takahashi T, Kalb RG, Strittmatter SM. Neuropilin-1 extracellular domains mediate semaphorin D/III-induced growth cone collapse. Neuron 1998; 21: 1093-100.
    • (1998) Neuron , vol.21 , pp. 1093-1100
    • Nakamura, F.1    Tanaka, M.2    Takahashi, T.3    Kalb, R.G.4    Strittmatter, S.M.5
  • 34
    • 0033568863 scopus 로고    scopus 로고
    • A dominant negative receptor for specific secreted semaphorins is generated by deleting an extracellular domain from neuropilin-1
    • Renzi MJ, Feiner L, Koppel AM, Raper JA. A dominant negative receptor for specific secreted semaphorins is generated by deleting an extracellular domain from neuropilin-1. J Neurosci 1999; 19: 7870-80.
    • (1999) J Neurosci , vol.19 , pp. 7870-7880
    • Renzi, M.J.1    Feiner, L.2    Koppel, A.M.3    Raper, J.A.4
  • 35
  • 38
    • 84875608683 scopus 로고    scopus 로고
    • Structural insights into semaphorins and their receptors
    • Siebold C, Jones EY. Structural insights into semaphorins and their receptors. Semin Cell Dev Biol 2013; 24: 139-45.
    • (2013) Semin Cell Dev Biol , vol.24 , pp. 139-145
    • Siebold, C.1    Jones, E.Y.2
  • 39
    • 0027751890 scopus 로고
    • The vascular endothelial growth factor (VEGF) isoforms: Differential deposition into the subepithelial extracellular matrix and bioactivity of extracellular matrix-bound VEGF
    • Park JE, Keller GA, Ferrara N. The vascular endothelial growth factor (VEGF) isoforms: differential deposition into the subepithelial extracellular matrix and bioactivity of extracellular matrix-bound VEGF. Mol Biol Cell 1993; 4: 1317-26.
    • (1993) Mol Biol Cell , vol.4 , pp. 1317-1326
    • Park, J.E.1    Keller, G.A.2    Ferrara, N.3
  • 42
    • 0035143709 scopus 로고    scopus 로고
    • Differential expression of VEGF isoforms in mouse during development and in the adult
    • Ng YS, Rohan R, Sunday ME, Demello DE, D'Amore PA. Differential expression of VEGF isoforms in mouse during development and in the adult. Dev Dyn 2001; 220: 112-21.
    • (2001) Dev Dyn , vol.220 , pp. 112-121
    • Ng, Y.S.1    Rohan, R.2    Sunday, M.E.3    Demello, D.E.4    D'Amore, P.A.5
  • 44
    • 77952341533 scopus 로고    scopus 로고
    • Furin processing of semaphorin 3F determines its anti-angiogenic activity by regulating direct binding and competition for neuropilin
    • Parker MW, Hellman LM, Xu P, Fried MG, Vander Kooi CW. Furin processing of semaphorin 3F determines its anti-angiogenic activity by regulating direct binding and competition for neuropilin. Biochemistry 2010; 49: 4068-75.
    • (2010) Biochemistry , vol.49 , pp. 4068-4075
    • Parker, M.W.1    Hellman, L.M.2    Xu, P.3    Fried, M.G.4    Vander Kooi, C.W.5
  • 45
    • 84886725991 scopus 로고    scopus 로고
    • Effect of C-terminal sequence on competitive semaphorin binding to neuropilin-1
    • Parker MW, Linkugel AD, Vander Kooi CW. Effect of C-terminal sequence on competitive semaphorin binding to neuropilin-1. J Mol Biol 2013; 425: 4405-14.
    • (2013) J Mol Biol , vol.425 , pp. 4405-4414
    • Parker, M.W.1    Linkugel, A.D.2    Vander Kooi, C.W.3
  • 46
    • 0030722135 scopus 로고    scopus 로고
    • The chemorepulsive activity of secreted semaphorins is regulated by furin-dependent proteolytic processing
    • Adams RH, Lohrum M, Klostermann A, Betz H, Puschel AW. The chemorepulsive activity of secreted semaphorins is regulated by furin-dependent proteolytic processing. EMBO J 1997; 16: 6077-86.
    • (1997) EMBO J , vol.16 , pp. 6077-6086
    • Adams, R.H.1    Lohrum, M.2    Klostermann, A.3    Betz, H.4    Puschel, A.W.5
  • 47
    • 52049103578 scopus 로고    scopus 로고
    • Semaphorin-3B is an angiogenesis inhibitor that is inactivated by furin-like pro-protein convertases
    • Varshavsky A, Kessler O, Abramovitch S, Kigel B, Zaffryar S, Akiri G, Neufeld G. Semaphorin-3B is an angiogenesis inhibitor that is inactivated by furin-like pro-protein convertases. Cancer Res 2008; 68: 6922-31.
    • (2008) Cancer Res , vol.68 , pp. 6922-6931
    • Varshavsky, A.1    Kessler, O.2    Abramovitch, S.3    Kigel, B.4    Zaffryar, S.5    Akiri, G.6    Neufeld, G.7
  • 50
    • 0023217141 scopus 로고
    • Specific cell surface labels in the visual centers of Xenopus laevis tadpole identified using monoclonal antibodies
    • Takagi S, Tsuji T, Amagai T, Takamatsu T, Fujisawa H. Specific cell surface labels in the visual centers of Xenopus laevis tadpole identified using monoclonal antibodies. Dev Biol 1987; 122: 90-100.
    • (1987) Dev Biol , vol.122 , pp. 90-100
    • Takagi, S.1    Tsuji, T.2    Amagai, T.3    Takamatsu, T.4    Fujisawa, H.5
  • 52
    • 0034688995 scopus 로고    scopus 로고
    • Determination of cell adhesion sites of neuropilin-1
    • Shimizu M, Murakami Y, Suto F, Fujisawa H. Determination of cell adhesion sites of neuropilin-1. J Cell Biol 2000; 148: 1283-93.
    • (2000) J Cell Biol , vol.148 , pp. 1283-1293
    • Shimizu, M.1    Murakami, Y.2    Suto, F.3    Fujisawa, H.4
  • 54
    • 72249096538 scopus 로고    scopus 로고
    • Angiogenesis: A balancing act between integrin activation and inhibition?
    • Bussolino F, Caccavari F, Valdembri D, Serini G. Angiogenesis: a balancing act between integrin activation and inhibition? Eur Cytokine Netw 2009; 20: 191-6.
    • (2009) Eur Cytokine Netw , vol.20 , pp. 191-196
    • Bussolino, F.1    Caccavari, F.2    Valdembri, D.3    Serini, G.4
  • 55
    • 42449148407 scopus 로고    scopus 로고
    • Neuropilins: Structure, function and role in disease
    • Pellet-Many C, Frankel P, Jia H, Zachary I. Neuropilins: structure, function and role in disease. Biochem J 2008; 411: 211-26.
    • (2008) Biochem J , vol.411 , pp. 211-226
    • Pellet-Many, C.1    Frankel, P.2    Jia, H.3    Zachary, I.4
  • 57
    • 34347332447 scopus 로고    scopus 로고
    • Neuropilins in physiological and pathological angiogenesis
    • Staton CA, Kumar I, Reed MW, Brown NJ. Neuropilins in physiological and pathological angiogenesis. J Pathol 2007; 212: 237-48.
    • (2007) J Pathol , vol.212 , pp. 237-248
    • Staton, C.A.1    Kumar, I.2    Reed, M.W.3    Brown, N.J.4
  • 58
    • 0036139515 scopus 로고    scopus 로고
    • The neuropilins: Multifunctional semaphorin and VEGF receptors that modulate axon guidance and angiogenesis
    • Neufeld G, Cohen T, Shraga N, Lange T, Kessler O, Herzog Y. The neuropilins: multifunctional semaphorin and VEGF receptors that modulate axon guidance and angiogenesis. Trends Cardiovasc Med 2002; 12: 13-9.
    • (2002) Trends Cardiovasc Med , vol.12 , pp. 13-19
    • Neufeld, G.1    Cohen, T.2    Shraga, N.3    Lange, T.4    Kessler, O.5    Herzog, Y.6
  • 59
    • 0036678171 scopus 로고    scopus 로고
    • Neuropilin-1 is required for vascular development and is a mediator of VEGF-dependent angiogenesis in zebrafish
    • Lee P, Goishi K, Davidson AJ, Mannix R, Zon L, Klagsbrun M. Neuropilin-1 is required for vascular development and is a mediator of VEGF-dependent angiogenesis in zebrafish. Proc Natl Acad Sci USA 2002; 99: 10470-5.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 10470-10475
    • Lee, P.1    Goishi, K.2    Davidson, A.J.3    Mannix, R.4    Zon, L.5    Klagsbrun, M.6
  • 62
    • 0030778454 scopus 로고    scopus 로고
    • Neuropilin-semaphorin III/Dmediated chemorepulsive signals play a crucial role in peripheral nerve projection in mice
    • Kitsukawa T, Shimizu M, Sanbo M, Hirata T, Taniguchi M, Bekku Y, Yagi T, Fujisawa H. Neuropilin-semaphorin III/Dmediated chemorepulsive signals play a crucial role in peripheral nerve projection in mice. Neuron 1997; 19: 995-1005.
    • (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
  • 64
    • 0029562097 scopus 로고
    • Overexpression of a membrane protein, neuropilin, in chimeric mice causes anomalies in the cardiovascular system, nervous system and limbs
    • Kitsukawa T, Shimono A, Kawakami A, Kondoh H, Fujisawa H. Overexpression of a membrane protein, neuropilin, in chimeric mice causes anomalies in the cardiovascular system, nervous system and limbs. Development 1995; 121: 4309-18.
    • (1995) Development , vol.121 , pp. 4309-4318
    • Kitsukawa, T.1    Shimono, A.2    Kawakami, A.3    Kondoh, H.4    Fujisawa, H.5
  • 68
    • 50249094553 scopus 로고    scopus 로고
    • Separating genetic and hemodynamic defects in neuropilin 1 knockout embryos
    • Jones EA, Yuan L, Breant C, Watts RJ, Eichmann A. Separating genetic and hemodynamic defects in neuropilin 1 knockout embryos. Development 2008; 135: 2479-88.
    • (2008) Development , vol.135 , pp. 2479-2488
    • Jones, E.A.1    Yuan, L.2    Breant, C.3    Watts, R.J.4    Eichmann, A.5
  • 69
    • 14944344614 scopus 로고    scopus 로고
    • Neuropilin-1 regulates attachment in human endothelial cells independently of vascular endothelial growth factor receptor-2
    • Murga M, Fernandez-Capetillo O, Tosato G. Neuropilin-1 regulates attachment in human endothelial cells independently of vascular endothelial growth factor receptor-2. Blood 2005; 105: 1992-9.
    • (2005) Blood , vol.105 , pp. 1992-1999
    • Murga, M.1    Fernandez-Capetillo, O.2    Tosato, G.3
  • 70
    • 6944225400 scopus 로고    scopus 로고
    • Neuropilin-1 is required for endothelial tip cell guidance in the developing central nervous system
    • Gerhardt H, Ruhrberg C, Abramsson A, Fujisawa H, Shima D, Betsholtz C. Neuropilin-1 is required for endothelial tip cell guidance in the developing central nervous system. Dev Dyn 2004; 231: 503-9.
    • (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
  • 72
    • 84877929726 scopus 로고    scopus 로고
    • NRP1 acts cell autonomously in endothelium to promote tip cell function during sprouting angiogenesis
    • Fantin A, Vieira JM, Plein A, Denti L, Fruttiger M, Pollard JW, Ruhrberg C. NRP1 acts cell autonomously in endothelium to promote tip cell function during sprouting angiogenesis. Blood 2013; 121: 2352-62.
    • (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
  • 76
    • 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, Schwarz Q, Davidson K, Normando EM, Denti L, Ruhrberg C. The cytoplasmic domain of neuropilin 1 is dispensable for angiogenesis, but promotes the spatial separation of retinal arteries and veins. Development 2011; 138: 4185-91.
    • (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
  • 77
    • 1542571789 scopus 로고    scopus 로고
    • Neuropilin- 1-mediated vascular permeability factor/vascular endothelial growth factor-dependent endothelial cell migration
    • Wang L, Zeng H, Wang P, Soker S, Mukhopadhyay D. Neuropilin- 1-mediated vascular permeability factor/vascular endothelial growth factor-dependent endothelial cell migration. J Biol Chem 2003; 278: 48848-60.
    • (2003) J Biol Chem , vol.278 , pp. 48848-48860
    • Wang, L.1    Zeng, H.2    Wang, P.3    Soker, S.4    Mukhopadhyay, D.5
  • 80
    • 79960690759 scopus 로고    scopus 로고
    • Neuropilin-1 promotes VEGFR-2 trafficking through Rab11 vesicles thereby specifying signal output
    • Ballmer-Hofer K, Andersson AE, Ratcliffe LE, Berger P. Neuropilin-1 promotes VEGFR-2 trafficking through Rab11 vesicles thereby specifying signal output. Blood 2011; 118: 816-26.
    • (2011) Blood , vol.118 , pp. 816-826
    • Ballmer-Hofer, K.1    Andersson, A.E.2    Ratcliffe, L.E.3    Berger, P.4
  • 81
    • 0027216956 scopus 로고
    • The membrane protein A5, a putative neuronal recognition molecule, promotes neurite outgrowth
    • Hirata T, Takagi S, Fujisawa H. The membrane protein A5, a putative neuronal recognition molecule, promotes neurite outgrowth. Neurosci Res 1993; 17: 159-69.
    • (1993) Neurosci Res , vol.17 , pp. 159-169
    • Hirata, T.1    Takagi, S.2    Fujisawa, H.3
  • 83
    • 0034284998 scopus 로고    scopus 로고
    • Signalling by semaphorin receptors: Cell guidance and beyond
    • Tamagnone L, Comoglio PM. Signalling by semaphorin receptors: cell guidance and beyond. Trends Cell Biol 2000; 10: 377-83.
    • (2000) Trends Cell Biol , vol.10 , pp. 377-383
    • Tamagnone, L.1    Comoglio, P.M.2
  • 84
    • 0342872023 scopus 로고    scopus 로고
    • Neuropilin-2, a novel member of the neuropilin family, is a high affinity receptor for the semaphorins Sema e and Sema IV but not Sema III
    • Chen H, Chedotal A, He Z, Goodman CS, Tessier-Lavigne M. Neuropilin-2, a novel member of the neuropilin family, is a high affinity receptor for the semaphorins Sema E and Sema IV but not Sema III. Neuron 1997; 19: 547-59.
    • (1997) Neuron , vol.19 , pp. 547-559
    • Chen, H.1    Chedotal, A.2    He, Z.3    Goodman, C.S.4    Tessier-Lavigne, M.5
  • 85
    • 0030930310 scopus 로고    scopus 로고
    • Secreted chick semaphorins bind recombinant neuropilin with similar affinities but bind different subsets of neurons in situ
    • Feiner L, Koppel AM, Kobayashi H, Raper JA. Secreted chick semaphorins bind recombinant neuropilin with similar affinities but bind different subsets of neurons in situ. Neuron 1997; 19: 539-45.
    • (1997) Neuron , vol.19 , pp. 539-545
    • Feiner, L.1    Koppel, A.M.2    Kobayashi, H.3    Raper, J.A.4
  • 87
    • 33845605915 scopus 로고    scopus 로고
    • In vivo analysis reveals a critical role for neuropilin-1 in cranial neural crest cell migration in chick
    • McLennan R, Kulesa PM. In vivo analysis reveals a critical role for neuropilin-1 in cranial neural crest cell migration in chick. Dev Biol 2007; 301: 227-39.
    • (2007) Dev Biol , vol.301 , pp. 227-239
    • McLennan, R.1    Kulesa, P.M.2
  • 90
    • 0041632379 scopus 로고    scopus 로고
    • Semaphorin 3F is critical for development of limbic system circuitry and is required in neurons for selective CNS axon guidance events
    • Sahay A, Molliver ME, Ginty DD, Kolodkin AL. Semaphorin 3F is critical for development of limbic system circuitry and is required in neurons for selective CNS axon guidance events. J Neurosci 2003; 23: 6671-80.
    • (2003) J Neurosci , vol.23 , pp. 6671-6680
    • Sahay, A.1    Molliver, M.E.2    Ginty, D.D.3    Kolodkin, A.L.4
  • 91
    • 0037095682 scopus 로고    scopus 로고
    • Aberrant sensory innervation of the olfactory bulb in neuropilin-2 mutant mice
    • Walz A, Rodriguez I, Mombaerts P. Aberrant sensory innervation of the olfactory bulb in neuropilin-2 mutant mice. J Neurosci 2002; 22: 4025-35.
    • (2002) J Neurosci , vol.22 , pp. 4025-4035
    • Walz, A.1    Rodriguez, I.2    Mombaerts, P.3
  • 94
    • 2442421626 scopus 로고    scopus 로고
    • Plexin signaling hampers integrin-based adhesion, leading to Rho-kinase independent cell rounding, and inhibiting lamellipodia extension and cell motility
    • Barberis D, Artigiani S, Casazza A, Corso S, Giordano S, Love CA, Jones EY, Comoglio PM, Tamagnone L. Plexin signaling hampers integrin-based adhesion, leading to Rho-kinase independent cell rounding, and inhibiting lamellipodia extension and cell motility. FASEB J 2004; 18: 592-4.
    • (2004) FASEB J , vol.18 , pp. 592-594
    • Barberis, D.1    Artigiani, S.2    Casazza, A.3    Corso, S.4    Giordano, S.5    Love, C.A.6    Jones, E.Y.7    Comoglio, P.M.8    Tamagnone, L.9
  • 95
    • 0037080330 scopus 로고    scopus 로고
    • Antagonistic effects of Rnd1 and RhoD GTPases regulate receptor activity in Semaphorin 3A-induced cytoskeletal collapse
    • Zanata SM, Hovatta I, Rohm B, Puschel AW. Antagonistic effects of Rnd1 and RhoD GTPases regulate receptor activity in Semaphorin 3A-induced cytoskeletal collapse. J Neurosci 2002; 22: 471-7.
    • (2002) J Neurosci , vol.22 , pp. 471-477
    • Zanata, S.M.1    Hovatta, I.2    Rohm, B.3    Puschel, A.W.4
  • 96
    • 3843065433 scopus 로고    scopus 로고
    • The Semaphorin 4D receptor Plexin-B1 is a GTPase activating protein for R-Ras
    • Oinuma I, Ishikawa Y, Katoh H, Negishi M. The Semaphorin 4D receptor Plexin-B1 is a GTPase activating protein for R-Ras. Science 2004; 305: 862-5.
    • (2004) Science , vol.305 , pp. 862-865
    • Oinuma, I.1    Ishikawa, Y.2    Katoh, H.3    Negishi, M.4
  • 97
    • 28644439947 scopus 로고    scopus 로고
    • R-Ras is a global regulator of vascular regeneration that suppresses intimal hyperplasia and tumor angiogenesis
    • Komatsu M, Ruoslahti E. R-Ras is a global regulator of vascular regeneration that suppresses intimal hyperplasia and tumor angiogenesis. Nat Med 2005; 11: 1346-50.
    • (2005) Nat Med , vol.11 , pp. 1346-1350
    • Komatsu, M.1    Ruoslahti, E.2
  • 98
    • 67349193305 scopus 로고    scopus 로고
    • Plexin-B1 is a GTPase activating protein for M-Ras, remodelling dendrite morphology
    • Saito Y, Oinuma I, Fujimoto S, Negishi M. Plexin-B1 is a GTPase activating protein for M-Ras, remodelling dendrite morphology. EMBO Rep 2009; 10: 614-21.
    • (2009) EMBO Rep , vol.10 , pp. 614-621
    • Saito, Y.1    Oinuma, I.2    Fujimoto, S.3    Negishi, M.4
  • 100
    • 80052285848 scopus 로고    scopus 로고
    • Extracellular inhibitors, repellents, and semaphorin/plexin/MICAL- mediated actin filament disassembly
    • Hung RJ, Terman JR. Extracellular inhibitors, repellents, and semaphorin/plexin/MICAL-mediated actin filament disassembly. Cytoskeleton (Hoboken) 2011; 68: 415-33.
    • (2011) Cytoskeleton (Hoboken) , vol.68 , pp. 415-433
    • Hung, R.J.1    Terman, J.R.2
  • 101
    • 70349973901 scopus 로고    scopus 로고
    • Autocrine semaphorin 3A signaling promotes glioblastoma dispersal
    • Bagci T, Wu JK, Pfannl R, Ilag LL, Jay DG. Autocrine semaphorin 3A signaling promotes glioblastoma dispersal. Oncogene 2009; 28: 3537-50.
    • (2009) Oncogene , vol.28 , pp. 3537-3550
    • Bagci, T.1    Wu, J.K.2    Pfannl, R.3    Ilag, L.L.4    Jay, D.G.5
  • 103
    • 0041378074 scopus 로고    scopus 로고
    • Blood vessels and nerves: Common signals, pathways and diseases
    • Carmeliet P. Blood vessels and nerves: common signals, pathways and diseases. Nat Rev Genet 2003; 4: 710-20.
    • (2003) Nat Rev Genet , vol.4 , pp. 710-720
    • Carmeliet, P.1
  • 104
    • 0033565417 scopus 로고    scopus 로고
    • Vascular endothelial growth factor has neurotrophic activity and stimulates axonal outgrowth, enhancing cell survival and Schwann cell proliferation in the peripheral nervous system
    • Sondell M, Lundborg G, Kanje M. Vascular endothelial growth factor has neurotrophic activity and stimulates axonal outgrowth, enhancing cell survival and Schwann cell proliferation in the peripheral nervous system. J Neurosci 1999; 19: 5731-40.
    • (1999) J Neurosci , vol.19 , pp. 5731-5740
    • Sondell, M.1    Lundborg, G.2    Kanje, M.3
  • 106
    • 55249110412 scopus 로고    scopus 로고
    • ABL2/ARG tyrosine kinase mediates SEMA3F-induced RhoA inactivation and cytoskeleton collapse in human glioma cells
    • Shimizu A, Mammoto A, Italiano JE Jr, Pravda E, Dudley AC, Ingber DE, Klagsbrun M. ABL2/ARG tyrosine kinase mediates SEMA3F-induced RhoA inactivation and cytoskeleton collapse in human glioma cells. J Biol Chem 2008; 283: 27230-8.
    • (2008) J Biol Chem , vol.283 , pp. 27230-27238
    • Shimizu, A.1    Mammoto, A.2    Italiano Jr., J.E.3    Pravda, E.4    Dudley, A.C.5    Ingber, D.E.6    Klagsbrun, M.7
  • 108
    • 79961213450 scopus 로고    scopus 로고
    • Semaphorin signals on the road of endothelial tip cells
    • Tamagnone L, Mazzone M. Semaphorin signals on the road of endothelial tip cells. Dev Cell 2011; 21: 189-90.
    • (2011) Dev Cell , vol.21 , pp. 189-190
    • Tamagnone, L.1    Mazzone, M.2
  • 109
    • 0033549556 scopus 로고    scopus 로고
    • Neuropilin-1 mediates collapsin-1/semaphorin III inhibition of endothelial cell motility: Functional competition of collapsin-1 and vascular endothelial growth factor-165
    • Miao HQ, Soker S, Feiner L, Alonso JL, Raper JA, Klagsbrun M. Neuropilin-1 mediates collapsin-1/semaphorin III inhibition of endothelial cell motility: functional competition of collapsin-1 and vascular endothelial growth factor-165. J Cell Biol 1999; 146: 233-42.
    • (1999) J Cell Biol , vol.146 , pp. 233-242
    • Miao, H.Q.1    Soker, S.2    Feiner, L.3    Alonso, J.L.4    Raper, J.A.5    Klagsbrun, M.6
  • 110
    • 33646552427 scopus 로고    scopus 로고
    • Ligand-induced internalization selects use of common receptor neuropilin-1 by VEGF165 and semaphorin3A
    • Narazaki M, Tosato G. Ligand-induced internalization selects use of common receptor neuropilin-1 by VEGF165 and semaphorin3A. Blood 2006; 107: 3892-901.
    • (2006) Blood , vol.107 , pp. 3892-3901
    • Narazaki, M.1    Tosato, G.2
  • 112
    • 70349941415 scopus 로고    scopus 로고
    • Autocrine semaphorin3A stimulates alpha2 beta1 integrin expression/function in breast tumor cells
    • Pan H, Wanami LS, Dissanayake TR, Bachelder RE. Autocrine semaphorin3A stimulates alpha2 beta1 integrin expression/function in breast tumor cells. Breast Cancer Res Treat 2009; 118: 197-205.
    • (2009) Breast Cancer Res Treat , vol.118 , pp. 197-205
    • Pan, H.1    Wanami, L.S.2    Dissanayake, T.R.3    Bachelder, R.E.4
  • 113
    • 33745063095 scopus 로고    scopus 로고
    • The role of neuropilins in cancer
    • Ellis LM. The role of neuropilins in cancer. Mol Cancer Ther 2006; 5: 1099-107.
    • (2006) Mol Cancer Ther , vol.5 , pp. 1099-1107
    • Ellis, L.M.1
  • 115
    • 33845957319 scopus 로고    scopus 로고
    • Neuropilin-1 is involved in regulation of apoptosis and migration of human colon cancer
    • Ochiumi T, Kitadai Y, Tanaka S, Akagi M, Yoshihara M, Chayama K. Neuropilin-1 is involved in regulation of apoptosis and migration of human colon cancer. Int J Oncol 2006; 29: 105-16.
    • (2006) Int J Oncol , vol.29 , pp. 105-116
    • Ochiumi, T.1    Kitadai, Y.2    Tanaka, S.3    Akagi, M.4    Yoshihara, M.5    Chayama, K.6
  • 117
    • 78649760815 scopus 로고    scopus 로고
    • Expression of Neuropilin-2 in salivary adenoid cystic carcinoma: Its implication in tumor progression and angiogenesis
    • Cai Y, Wang R, Zhao YF, Jia J, Sun ZJ, Chen XM. Expression of Neuropilin-2 in salivary adenoid cystic carcinoma: its implication in tumor progression and angiogenesis. Pathol Res Pract 2010; 206: 793-9.
    • (2010) Pathol Res Pract , vol.206 , pp. 793-799
    • Cai, Y.1    Wang, R.2    Zhao, Y.F.3    Jia, J.4    Sun, Z.J.5    Chen, X.M.6
  • 118
    • 84877300380 scopus 로고    scopus 로고
    • Expression of VEGF and semaphorin genes define subgroups of triple negative breast cancer
    • Bender RJ, Mac Gabhann F. Expression of VEGF and semaphorin genes define subgroups of triple negative breast cancer. PLoS One 2013; 8: e61788.
    • (2013) PLoS One , vol.8
    • Bender, R.J.1    Mac Gabhann, F.2
  • 120
    • 35948965519 scopus 로고    scopus 로고
    • Neuropilin-1 interacts with integrin beta1 and modulates pancreatic cancer cell growth, survival and invasion
    • Fukasawa M, Matsushita A, Korc M. Neuropilin-1 interacts with integrin beta1 and modulates pancreatic cancer cell growth, survival and invasion. Cancer Biol Ther 2007; 6: 1173-80.
    • (2007) Cancer Biol Ther , vol.6 , pp. 1173-1180
    • Fukasawa, M.1    Matsushita, A.2    Korc, M.3
  • 121
    • 84858118438 scopus 로고    scopus 로고
    • Neuropilin-2 regulates α6β1 integrin in the formation of focal adhesions and signaling
    • Goel HL, Pursell B, Standley C, Fogarty K, Mercurio AM. Neuropilin-2 regulates α6β1 integrin in the formation of focal adhesions and signaling. J Cell Sci 2012; 125: 497-506.
    • (2012) J Cell Sci , vol.125 , pp. 497-506
    • Goel, H.L.1    Pursell, B.2    Standley, C.3    Fogarty, K.4    Mercurio, A.M.5
  • 124
    • 33751091501 scopus 로고    scopus 로고
    • Antiangiogenic and antitumor activities of peptide inhibiting the vascular endothelial growth factor binding to neuropilin-1
    • Starzec A, Vassy R, Martin A, Lecouvey M, Di Benedetto M, Crepin M, Perret GY. Antiangiogenic and antitumor activities of peptide inhibiting the vascular endothelial growth factor binding to neuropilin-1. Life Sci 2006; 79: 2370-81.
    • (2006) Life Sci , vol.79 , pp. 2370-2381
    • Starzec, A.1    Vassy, R.2    Martin, A.3    Lecouvey, M.4    Di Benedetto, M.5    Crepin, M.6    Perret, G.Y.7
  • 127
    • 84879005229 scopus 로고    scopus 로고
    • Design of a cyclotide antagonist of neuropilin-1 and -2 that potently inhibits endothelial cell migration
    • Getz JA, Cheneval O, Craik DJ, Daugherty PS. Design of a cyclotide antagonist of neuropilin-1 and -2 that potently inhibits endothelial cell migration. ACS Chem Biol 2013; 8: 1147-54.
    • (2013) ACS Chem Biol , vol.8 , pp. 1147-1154
    • Getz, J.A.1    Cheneval, O.2    Craik, D.J.3    Daugherty, P.S.4
  • 128
    • 0035422178 scopus 로고    scopus 로고
    • Vascular endothelial growth factor is an autocrine survival factor for neuropilin-expressing breast carcinoma cells
    • Bachelder RE, Crago A, Chung J, Wendt MA, Shaw LM, Robinson G, Mercurio AM. Vascular endothelial growth factor is an autocrine survival factor for neuropilin-expressing breast carcinoma cells. Cancer Res 2001; 61: 5736-40.
    • (2001) Cancer Res , vol.61 , pp. 5736-5740
    • Bachelder, R.E.1    Crago, A.2    Chung, J.3    Wendt, M.A.4    Shaw, L.M.5    Robinson, G.6    Mercurio, A.M.7
  • 130
    • 34247602012 scopus 로고    scopus 로고
    • Binding of the C-terminal amino acids of VEGF121 directly with neuropilin-1 should be considered
    • author reply 3
    • von Wronski MA, Tweedle MF, Nunn AD. Binding of the C-terminal amino acids of VEGF121 directly with neuropilin-1 should be considered. FASEB J 2007; 21: 1292; author reply 3.
    • (2007) FASEB J , vol.21 , pp. 1292
    • Von Wronski, M.A.1    Tweedle, M.F.2    Nunn, A.D.3
  • 131
    • 70349482671 scopus 로고    scopus 로고
    • C-end rule peptides mediate neuropilin-1-dependent cell, vascular, and tissue penetration
    • Teesalu T, Sugahara KN, Kotamraju VR, Ruoslahti E. C-end rule peptides mediate neuropilin-1-dependent cell, vascular, and tissue penetration. Proc Natl Acad Sci USA 2009; 106: 16157-62.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 16157-16162
    • Teesalu, T.1    Sugahara, K.N.2    Kotamraju, V.R.3    Ruoslahti, E.4
  • 133
    • 33846025118 scopus 로고    scopus 로고
    • Targeting neuropilin-1 to inhibit VEGF signaling in cancer: Comparison of therapeutic approaches
    • Mac Gabhann F, Popel AS. Targeting neuropilin-1 to inhibit VEGF signaling in cancer: comparison of therapeutic approaches. PLoS Comput Biol 2006; 2: e180.
    • (2006) PLoS Comput Biol , vol.2
    • Mac Gabhann, F.1    Popel, A.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.