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Volumn 20, Issue 9, 2006, Pages 1462-1472

Functional interaction of VEGF-C and VEGF-D with neuropilin receptors

Author keywords

Lymphatic endothelial cell; NP2; VEGFR 3

Indexed keywords

NEUROPILIN; VASCULOTROPIN C; VASCULOTROPIN D; HEPARIN; NEUROPILIN 2; PRIMER DNA; RECOMBINANT PROTEIN;

EID: 33746503288     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fj.05-5646com     Document Type: Article
Times cited : (253)

References (53)
  • 10
    • 0034794689 scopus 로고    scopus 로고
    • Plasticity of endothelial cells during arterial-venous differentiation in the avian embryo
    • Moyon, D., Pardanaud, L., Yuan, L., Breant, C., and Eichmann, A. (2001) Plasticity of endothelial cells during arterial-venous differentiation in the avian embryo. Development 128, 3359-3370
    • (2001) Development , vol.128 , pp. 3359-3370
    • Moyon, D.1    Pardanaud, L.2    Yuan, L.3    Breant, C.4    Eichmann, A.5
  • 11
    • 0034756449 scopus 로고    scopus 로고
    • Differential expression of neuropilin-1 and neuropilin-2 in arteries and veins
    • Herzog, Y., Kalcheim, C., Kahane, N., Reshef, R., and Neufeld, G. (2001) Differential expression of neuropilin-1 and neuropilin-2 in arteries and veins. Mech. Dev. 109, 115-119
    • (2001) Mech. Dev. , vol.109 , pp. 115-119
    • Herzog, Y.1    Kalcheim, C.2    Kahane, N.3    Reshef, R.4    Neufeld, G.5
  • 13
    • 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, H. Q., Neufeld, G., and Klagsbrun, M. (1998) Neuropilin-1 is expressed by endothelial and tumor cells as an isoform-specific receptor for vascular endothelial growth factor. Cell 92, 735-745
    • (1998) Cell , vol.92 , pp. 735-745
    • Soker, S.1    Takashima, S.2    Miao, H.Q.3    Neufeld, G.4    Klagsbrun, M.5
  • 14
    • 0033597813 scopus 로고    scopus 로고
    • Differential binding of vascular endothelial growth factor B splice and proteolytic isoforms to neuropilin-1
    • Mäkinen, T., Olofsson, B., Karpanen, T., Hellman, U., Soker, S., Klagsbrun, M., Eriksson, U., and Alitalo, K. (1999) Differential binding of vascular endothelial growth factor B splice and proteolytic isoforms to neuropilin-1. J. Biol. Chem. 274, 21217-21222
    • (1999) J. Biol. Chem. , vol.274 , pp. 21217-21222
    • Mäkinen, T.1    Olofsson, B.2    Karpanen, T.3    Hellman, U.4    Soker, S.5    Klagsbrun, M.6    Eriksson, U.7    Alitalo, K.8
  • 17
    • 0034674108 scopus 로고    scopus 로고
    • Neuropilin-2 and neuropilin-1 are receptors for the 165-amino acid form of vascular endothelial growth factor (VEGF) and of placenta growth factor-2, but only neuropilin-2 functions as a receptor for the 145-amino acid form of VEGF
    • Gluzman-Poltorak, Z., Cohen, T., Herzog, Y., and Neufeld, G. (2000) Neuropilin-2 and neuropilin-1 are receptors for the 165-amino acid form of vascular endothelial growth factor (VEGF) and of placenta growth factor-2, but only neuropilin-2 functions as a receptor for the 145-amino acid form of VEGF. J. Biol. Chem. 275, 18040-18045
    • (2000) J. Biol. Chem. , vol.275 , pp. 18040-18045
    • Gluzman-Poltorak, Z.1    Cohen, T.2    Herzog, Y.3    Neufeld, G.4
  • 19
    • 0036009760 scopus 로고    scopus 로고
    • VEGF165 mediates formation of complexes containing VEGFR-2 and neuropilin-1 that enhance VEGF165-receptor binding
    • Soker, S., Miao, H. Q., Nomi, M., Takashima, S., and Klagsbrun, M. (2002) VEGF165 mediates formation of complexes containing VEGFR-2 and neuropilin-1 that enhance VEGF165-receptor binding. J. Cell. Biochem. 85, 357-368
    • (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
  • 20
    • 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., and Fujisawa, H. (1995) Overexpression of a membrane protein, neuropilin, in chimeric mice causes anomalies in the cardiovascular system, nervous system and limbs. Development 121, 4309-4318
    • (1995) Development , vol.121 , pp. 4309-4318
    • Kitsukawa, T.1    Shimono, A.2    Kawakami, A.3    Kondoh, H.4    Fujisawa, H.5
  • 21
    • 0030778454 scopus 로고    scopus 로고
    • Neuropilin-semaphorin III/D-mediated 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., and Fujisawa, H. (1997) Neuropilin-semaphorin III/D-mediated chemorepulsive signals play a crucial role in peripheral nerve projection in mice. Neuron 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
  • 26
    • 0344839087 scopus 로고    scopus 로고
    • Inhibition of human leukemia in an animal model with human antibodies directed against vascular endothelial growth factor receptor 2. Correlation between antibody affinity and biological activity
    • Zhu, Z., Hattori, K., Zhang, H., Jimenez, X., Ludwig, D. L., Dias, S., Kussie, P., Koo, H., Kim, H. J., Lu, D., Liu, M., Tejada, R., Friedrich, M., Bohlen, P., Witte, L., and Rafii, S. (2003) Inhibition of human leukemia in an animal model with human antibodies directed against vascular endothelial growth factor receptor 2. Correlation between antibody affinity and biological activity. Leukemia 17, 604-611
    • (2003) Leukemia , vol.17 , pp. 604-611
    • Zhu, Z.1    Hattori, K.2    Zhang, H.3    Jimenez, X.4    Ludwig, D.L.5    Dias, S.6    Kussie, P.7    Koo, H.8    Kim, H.J.9    Lu, D.10    Liu, M.11    Tejada, R.12    Friedrich, M.13    Bohlen, P.14    Witte, L.15    Rafii, S.16
  • 27
    • 0027997863 scopus 로고
    • Different signal transduction properties of KDR and Flt1, two receptors for vascular endothelial growth factor
    • Waltenberger, J., Claesson-Welsh, L., Siegbahn, A., Shibuya, M., and Heldin, C. H. (1994) Different signal transduction properties of KDR and Flt1, two receptors for vascular endothelial growth factor. J. Biol. Chem. 269, 26988-26995
    • (1994) J. Biol. Chem. , vol.269 , pp. 26988-26995
    • Waltenberger, J.1    Claesson-Welsh, L.2    Siegbahn, A.3    Shibuya, M.4    Heldin, C.H.5
  • 28
    • 0028091775 scopus 로고
    • Signalling properties of FLT4, a proteolytically processed receptor tyrosine kinase related to two VEGF receptors
    • Pajusola, K., Aprelikova, O., Pelicci, G., Weich, H., Claesson-Welsh, L., and Alitalo, K. (1994) Signalling properties of FLT4, a proteolytically processed receptor tyrosine kinase related to two VEGF receptors. Oncogene 9, 3545-3555
    • (1994) Oncogene , vol.9 , pp. 3545-3555
    • Pajusola, K.1    Aprelikova, O.2    Pelicci, G.3    Weich, H.4    Claesson-Welsh, L.5    Alitalo, K.6
  • 32
    • 33744951970 scopus 로고    scopus 로고
    • Vascular endothelial growth factor (VEGF)/VEGF-C mosaic molecules reveal specificity determinants and feature novel receptor binding patterns
    • Jeltsch, M., Karpanen, T., Strandin, T., Aho, K., Lankinen, H., and Alitalo, K. (2006) Vascular endothelial growth factor (VEGF)/VEGF-C mosaic molecules reveal specificity determinants and feature novel receptor binding patterns. J. Biol. Chem. 281, 12187-12195
    • (2006) J. Biol. Chem. , vol.281 , pp. 12187-12195
    • Jeltsch, M.1    Karpanen, T.2    Strandin, T.3    Aho, K.4    Lankinen, H.5    Alitalo, K.6
  • 33
    • 0003364811 scopus 로고    scopus 로고
    • Endothelial receptor tyrosine kinases activate the STAT signaling pathway: Mutant Tie-2 causing venous malformations signals a distinct STAT activation response
    • Korpelainen, E. I., Karkkainen, M., Gunji, Y., Vikkula, M., and Alitalo, K. (1999) Endothelial receptor tyrosine kinases activate the STAT signaling pathway: mutant Tie-2 causing venous malformations signals a distinct STAT activation response. Oncogene 18, 1-8
    • (1999) Oncogene , vol.18 , pp. 1-8
    • Korpelainen, E.I.1    Karkkainen, M.2    Gunji, Y.3    Vikkula, M.4    Alitalo, K.5
  • 36
    • 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, M. E., Gasiunas, N., Gallagher, J., and Klagsbrun, M. (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
    • (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
  • 37
    • 0032215144 scopus 로고    scopus 로고
    • Neuropilin-2 is a receptor for semaphorin IV: Insight into the structural basis of receptor function and specificity
    • Giger, R. J., Urquhart, E. R., Gillespie, S. K., Levengood, D. V., Ginty, D. D., and Kolodkin, A. L. (1998) Neuropilin-2 is a receptor for semaphorin IV: insight into the structural basis of receptor function and specificity. Neuron 21, 1079-1092
    • (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
  • 39
    • 0030847193 scopus 로고    scopus 로고
    • Neuropilin is a receptor for the axonal chemorepellent Semaphorin III
    • He, Z., and Tessier-Lavigne, M. (1997) Neuropilin is a receptor for the axonal chemorepellent Semaphorin III. Cell 90, 739-751
    • (1997) Cell , vol.90 , pp. 739-751
    • He, Z.1    Tessier-Lavigne, M.2
  • 40
    • 13444263549 scopus 로고    scopus 로고
    • Clathrin- and non-clathrin-mediated endocytic regulation of cell signalling
    • Le Roy, C., and Wrana, J. L. (2005) Clathrin- and non-clathrin-mediated endocytic regulation of cell signalling. Nat. Rev. Mol. Cell. Biol. 6, 112-126
    • (2005) Nat. Rev. Mol. Cell. Biol. , vol.6 , pp. 112-126
    • Le Roy, C.1    Wrana, J.L.2
  • 41
    • 22944455544 scopus 로고    scopus 로고
    • Regulators of endocytosis maintain localized receptor tyrosine kinase signaling in guided migration
    • Jekely, G., Sung, H. H., Luque, C. M., and Rorth, P. (2005) Regulators of endocytosis maintain localized receptor tyrosine kinase signaling in guided migration. Dev. Cell 9, 197-207
    • (2005) Dev. Cell , vol.9 , pp. 197-207
    • Jekely, G.1    Sung, H.H.2    Luque, C.M.3    Rorth, P.4
  • 42
    • 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., and Mukhopadhyay, D. (2003) Neuropilin-1-mediated vascular permeability factor/vascular endothelial growth factor-dependent endothelial cell migration. J. Biol. Chem. 278, 48848-48860
    • (2003) J. Biol. Chem. , vol.278 , pp. 48848-48860
    • Wang, L.1    Zeng, H.2    Wang, P.3    Soker, S.4    Mukhopadhyay, D.5
  • 46
    • 0025976838 scopus 로고
    • Cell surface, heparin-like molecules are required for binding of basic fibroblast growth factor to its high affinity receptor
    • Yayon, A., Klagsbrun, M., Esko, J. D., Leder, P., and Ornitz, D. M. (1991) Cell surface, heparin-like molecules are required for binding of basic fibroblast growth factor to its high affinity receptor. Cell 64, 841-848
    • (1991) Cell , vol.64 , pp. 841-848
    • Yayon, A.1    Klagsbrun, M.2    Esko, J.D.3    Leder, P.4    Ornitz, D.M.5
  • 47
    • 0037059771 scopus 로고    scopus 로고
    • The mode of action of heparan and dermatan sulfates in the regulation of hepatocyte growth factor/scatter factor
    • Lyon, M., Deakin, J. A., and Gallagher, J. T. (2002) The mode of action of heparan and dermatan sulfates in the regulation of hepatocyte growth factor/scatter factor. J. Biol. Chem. 277, 1040-1046
    • (2002) J. Biol. Chem. , vol.277 , pp. 1040-1046
    • Lyon, M.1    Deakin, J.A.2    Gallagher, J.T.3
  • 48
    • 0029965081 scopus 로고    scopus 로고
    • Characterization of novel vascular endothelial growth factor (VEGF) receptors on tumor cells that bind VEGF165 via its exon 7-encoded domain
    • Soker, S., Fidder, H., Neufeld, G., and Klagsbrun, M. (1996) Characterization of novel vascular endothelial growth factor (VEGF) receptors on tumor cells that bind VEGF165 via its exon 7-encoded domain. J. Biol. Chem. 271, 5761-5767
    • (1996) J. Biol. Chem. , vol.271 , pp. 5761-5767
    • Soker, S.1    Fidder, H.2    Neufeld, G.3    Klagsbrun, M.4
  • 49
    • 0034282885 scopus 로고    scopus 로고
    • The interaction of neuropilin-1 with vascular endothelial growth factor and its receptor flt-1
    • Fuh, G., Garcia, K. C., and de Vos, A. M. (2000) The interaction of neuropilin-1 with vascular endothelial growth factor and its receptor flt-1. J. Biol. Chem. 275, 26690-26695
    • (2000) J. Biol. Chem. , vol.275 , pp. 26690-26695
    • Fuh, G.1    Garcia, K.C.2    De Vos, A.M.3
  • 50
    • 0035062394 scopus 로고    scopus 로고
    • The splice variants of vascular endothelial growth factor (VEGF) and their receptors
    • Robinson, C. J., and Stringer, S. E. (2001) The splice variants of vascular endothelial growth factor (VEGF) and their receptors. J. Cell Sci. 114, 853-865
    • (2001) J. Cell Sci. , vol.114 , pp. 853-865
    • Robinson, C.J.1    Stringer, S.E.2
  • 51
    • 0033602091 scopus 로고    scopus 로고
    • Autophosphorylation of KDR in the kinase domain is required for maximal VEGF-stimulated kinase activity and receptor internalization
    • Dougher, M., and Terman, B. I. (1999) Autophosphorylation of KDR in the kinase domain is required for maximal VEGF-stimulated kinase activity and receptor internalization. Oncogene 18, 1619-1627
    • (1999) Oncogene , vol.18 , pp. 1619-1627
    • Dougher, M.1    Terman, B.I.2
  • 52
  • 53
    • 0037598870 scopus 로고    scopus 로고
    • Distinct endocytic pathways regulate TGF-beta receptor signalling and turnover
    • Di Guglielmo, G. M., Le Roy, C., Goodfellow, A. F., and Wrana, J. L. (2003) Distinct endocytic pathways regulate TGF-beta receptor signalling and turnover. Nat. Cell Biol. 5, 410-421
    • (2003) Nat. Cell Biol. , vol.5 , pp. 410-421
    • Di Guglielmo, G.M.1    Le Roy, C.2    Goodfellow, A.F.3    Wrana, J.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.