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Volumn 287, Issue 14, 2012, Pages 11082-11089

Structural basis for selective vascular endothelial growth factor-A (VEGF-A) binding to neuropilin-1

Author keywords

[No Author keywords available]

Indexed keywords

ANGIOGENESIS; HEPARIN BINDING DOMAINS; HIGH AFFINITY; IN-VITRO; ISOFORMS; PRIMARY SEQUENCES; RELATIVE CONTRIBUTION; SELECTIVE BINDING; STRUCTURAL BASIS; VASCULAR ENDOTHELIAL GROWTH;

EID: 84859488831     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.331140     Document Type: Article
Times cited : (153)

References (38)
  • 1
    • 42449148407 scopus 로고    scopus 로고
    • Neuropilins: Structure, function and role in disease
    • DOI 10.1042/BJ20071639
    • Pellet-Many, C., Frankel, P., Jia, H., and Zachary, I. (2008) Neuropilins: structure, function and role in disease. Biochem. J. 411, 211-226 (Pubitemid 351580173)
    • (2008) Biochemical Journal , vol.411 , Issue.2 , pp. 211-226
    • Pellet-Many, C.1    Frankel, P.2    Jia, H.3    Zachary, I.4
  • 2
    • 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 (Pubitemid 27512361)
    • (1997) Neuron , vol.19 , Issue.5 , 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
  • 3
    • 75349091269 scopus 로고    scopus 로고
    • Structure-function analysis of VEGF receptor activation and the role of coreceptors in angiogenic signaling
    • Grünewald, F. S., Prota, A. E., Giese, A., and Ballmer-Hofer, K. (2010) Structure-function analysis of VEGF receptor activation and the role of coreceptors in angiogenic signaling. Biochim. Biophys. Acta 1804, 567-580
    • (2010) Biochim. Biophys. Acta , vol.1804 , pp. 567-580
    • Grünewald, F.S.1    Prota, A.E.2    Giese, A.3    Ballmer-Hofer, K.4
  • 4
    • 0029937679 scopus 로고    scopus 로고
    • The carboxyl-terminal domain (111-165) of vascular endothelial growth factor is critical for its mitogenic potency
    • DOI 10.1074/jbc.271.13.7788
    • Keyt, B. A., Berleau, L. T., Nguyen, H. V., Chen, H., Heinsohn, H., Vandlen, R., and Ferrara, N. (1996) The carboxyl-terminal domain(111-165) of vascular endothelial growth factor is critical for its mitogenic potency. J. Biol. Chem. 271, 7788-7795 (Pubitemid 26111064)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.13 , pp. 7788-7795
    • Keyt, B.A.1    Berleau, L.T.2    Nguyen, H.V.3    Chen, H.4    Heinsohn, H.5    Vandlen, R.6    Ferrara, N.7
  • 5
    • 0027064888 scopus 로고
    • Dual regulation of vascular endothelial growth factor bioavailability by genetic and proteolytic mechanisms
    • Houck, K. A., Leung, D. W., Rowland, A. M., Winer, J., and Ferrara, N. (1992) Dual regulation of vascular endothelial growth factor bioavailability by genetic and proteolytic mechanisms. J. Biol. Chem. 267, 26031-26037 (Pubitemid 23014012)
    • (1992) Journal of Biological Chemistry , vol.267 , Issue.36 , pp. 26031-26037
    • Houck, K.A.1    Leung, D.W.2    Rowland, A.M.3    Winer, J.4    Ferrara, N.5
  • 6
    • 0024818355 scopus 로고
    • Vascular endothelial growth factor is a secreted angiogenic mitogen
    • Leung, D. W., Cachianes, G., Kuang, W. J., Goeddel, D. V., and Ferrara, N. (1989) Vascular endothelial growth factor is a secreted angiogenic mitogen. Science 246, 1306-1309 (Pubitemid 20066716)
    • (1989) Science , vol.246 , Issue.4935 , pp. 1306-1309
    • Leung, D.W.1    Cachianes, G.2    Kuang, W.-J.3    Goeddel, D.V.4    Ferrara, N.5
  • 7
    • 0032524762 scopus 로고    scopus 로고
    • Solution structure of the heparin-binding domain of vascular endothelial growth factor
    • Fairbrother, W. J., Champe, M. A., Christinger, H. W., Keyt, B. A., and Starovasnik, M. A. (1998) Solution structure of the heparin-binding domain of vascular endothelial growth factor. Structure 6, 637-648 (Pubitemid 28258116)
    • (1998) Structure , vol.6 , Issue.5 , pp. 637-648
    • Fairbrother, W.J.1    Champe, M.A.2    Christinger, H.W.3    Keyt, B.A.4    Starovasnik, M.A.5
  • 8
    • 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
  • 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
    • DOI 10.1016/S0092-8674(00)81402-6
    • 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 (Pubitemid 28155313)
    • (1998) Cell , vol.92 , Issue.6 , pp. 735-745
    • Soker, S.1    Takashima, S.2    Miao, H.Q.3    Neufeld, G.4    Klagsbrun, M.5
  • 10
    • 0037124068 scopus 로고    scopus 로고
    • Characterization of neuropilin-1 structural features that confer binding to semaphorin 3A and vascular endothelial growth factor 165
    • DOI 10.1074/jbc.M201681200
    • Gu, C., Limberg, B. J., Whitaker, G. B., Perman, B., Leahy, D. J., Rosenbaum, J. S., Ginty, D. D., and Kolodkin, A. L. (2002) Characterization of neuropilin-1 structural features that confer binding to semaphorin 3A and vascular endothelial growth factor 165. J. Biol. Chem. 277, 18069-18076 (Pubitemid 34967620)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.20 , pp. 18069-18076
    • Gu, C.1    Limberg, B.J.2    Brian, W.G.3    Perman, B.4    Leahy, D.J.5    Rosenbaum, J.S.6    Ginty, D.D.7    Kolodkin, A.L.8
  • 11
    • 0037025311 scopus 로고    scopus 로고
    • Neuropilin-1 binds vascular endothelial growth factor 165, placenta growth factor-2, and heparin via its b1b2 domain
    • DOI 10.1074/jbc.M200730200
    • 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 (Pubitemid 34952014)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.27 , pp. 24818-24825
    • Mamluk, R.1    Gechtman, Z.2    Kutcher, M.E.3    Gasiunas, N.4    Gallagher, J.5    Klagsbrun, M.6
  • 12
    • 0031438075 scopus 로고    scopus 로고
    • 165
    • DOI 10.1074/jbc.272.50.31582
    • Soker, S., Gollamudi-Payne, S., Fidder, H., Charmahelli, H., and Klagsbrun, M. (1997) Inhibition of vascular endothelial growth factor (VEGF)-induced endothelial cell proliferation by a peptide corresponding to the exon 7-encoded domain of VEGF165. J. Biol. Chem. 272, 31582-31588 (Pubitemid 28013301)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.50 , pp. 31582-31588
    • Soker, S.1    Gollamudi-Payne, S.2    Fidder, H.3    Charmahelli, H.4    Klagsbrun, M.5
  • 13
    • 0037098860 scopus 로고    scopus 로고
    • 165b, an inhibitory splice variant of vascular endothelial growth factor, is down-regulated in renal cell carcinoma
    • Bates, D. O., Cui, T. G., Doughty, J. M., Winkler, M., Sugiono, M., Shields, J. D., Peat, D., Gillatt, D., and Harper, S. J. (2002) VEGF165b, an inhibitory splice variant of vascular endothelial growth factor, is down-regulated in renal cell carcinoma. Cancer Res. 62, 4123-4131 (Pubitemid 34791084)
    • (2002) Cancer Research , vol.62 , Issue.14 , pp. 4123-4131
    • Bates, D.O.1    Cui, T.-G.2    Doughty, J.M.3    Winkler, M.4    Sugiono, M.5    Shields, J.D.6    Peat, D.7    Gillatt, D.8    Harper, S.J.9
  • 17
    • 36148969690 scopus 로고    scopus 로고
    • 165 binding to neuropilin-1 and molecular dynamics simulations of the ATWLPPR/neuropilin-1 complex
    • DOI 10.1016/j.peptides.2007.09.013, PII S0196978107003853
    • Starzec, A., Ladam, P., Vassy, R., Badache, S., Bouchemal, N., Navaza, A., du Penhoat, C. H., and Perret, G. Y. (2007) Structure-function analysis of the antiangiogenic ATWLPPR peptide inhibiting VEGF(165) binding to neuropilin-1 and molecular dynamics simulations of the ATWLPPR/neuropilin-1 complex. Peptides 28, 2397-2402 (Pubitemid 350116304)
    • (2007) Peptides , vol.28 , Issue.12 , pp. 2397-2402
    • Starzec, A.1    Ladam, P.2    Vassy, R.3    Badache, S.4    Bouchemal, N.5    Navaza, A.6    Du, P.C.H.7    Perret, G.Y.8
  • 18
    • 70349482671 scopus 로고    scopus 로고
    • C-end rule peptides mediate neuropilin-1-dependent cell, vascular, and tissue penetration
    • Teesalu, T., Sugahara, K. N., Kotamraju, V. R., and Ruoslahti, E. (2009) C-end rule peptides mediate neuropilin-1-dependent cell, vascular, and tissue penetration. Proc. Natl. Acad. Sci. U.S.A. 106, 16157-16162
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 16157-16162
    • Teesalu, T.1    Sugahara, K.N.2    Kotamraju, V.R.3    Ruoslahti, E.4
  • 19
    • 77952341533 scopus 로고    scopus 로고
    • Furin processing of semaphorin 3F determines its anti-angiogenic activity by regulating direct binding and competition for neuropilin
    • Parker, M. W., Hellman, L. M., Xu, P., Fried, M. G., and Vander Kooi, C. W. (2010) Furin processing of semaphorin 3F determines its anti-angiogenic activity by regulating direct binding and competition for neuropilin. Biochemistry 49, 4068-4075
    • (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
  • 21
    • 0030829388 scopus 로고    scopus 로고
    • Neuropilin is a semaphorin III receptor
    • DOI 10.1016/S0092-8674(00)80535-8
    • Kolodkin, A. L., Levengood, D. V., Rowe, E. G., Tai, Y. T., Giger, R. J., and Ginty, D. D. (1997) Neuropilin is a semaphorin III receptor. Cell 90, 753-762 (Pubitemid 27357966)
    • (1997) Cell , vol.90 , Issue.4 , pp. 753-762
    • Kolodkin, A.L.1    Levengood, D.V.2    Rowe, E.G.3    Tai, Y.-T.4    Giger, R.J.5    Ginty, D.D.6
  • 22
    • 0035266283 scopus 로고    scopus 로고
    • Vascular endothelial growth factor C promotes tumor lymphangiogenesis and intralymphatic tumor growth
    • Karpanen, T., Egeblad, M., Karkkainen, M. J., Kubo, H., Ylä-Herttuala, S., Jäättelä, M., and Alitalo, K. (2001) Vascular endothelial growth factor C promotes tumor lymphangiogenesis and intralymphatic tumor growth. Cancer Res. 61, 1786-1790 (Pubitemid 32691984)
    • (2001) Cancer Research , vol.61 , Issue.5 , pp. 1786-1790
    • Karpanen, T.1    Egeblad, M.2    Karkkainen, M.J.3    Kubo, H.4    Yla-Herttuala, S.5    Jaattela, M.6    Alitalo, K.7
  • 23
    • 34347332447 scopus 로고    scopus 로고
    • Neuropilins in physiological and pathological angiogenesis
    • DOI 10.1002/path.2182
    • Staton, C. A., Kumar, I., Reed, M. W., and Brown, N. J. (2007) Neuropilins in physiological and pathological angiogenesis. J. Pathol. 212, 237-248 (Pubitemid 47010058)
    • (2007) Journal of Pathology , vol.212 , Issue.3 , pp. 237-248
    • Staton, C.A.1    Kumar, I.2    Reed, M.W.R.3    Brown, N.J.4
  • 24
    • 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 (Pubitemid 24332901)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.43 , pp. 26988-26995
    • Waltenberger, J.1    Claesson-Welsh, L.2    Siegbahn, A.3    Shibuya, M.4    Heldin, C.-H.5
  • 25
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Otwinowski, Z., and Minor, W. (1997) Processing of x-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 29
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov, G. N. (1997) Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D Biol. Crystallogr. 53, 240-255
    • (1997) Acta Crystallogr. D Biol. Crystallogr. , vol.53 , pp. 240-255
    • Murshudov, G.N.1
  • 31
    • 46149116542 scopus 로고    scopus 로고
    • Expression of SEAP (secreted alkaline phosphatase) by baculovirus-mediated transduction of HEK 293 cells in a hollow fiber bioreactor system
    • Jardin, B. A., Zhao, Y., Selvaraj, M., Montes, J., Tran, R., Prakash, S., and Elias, C. B. (2008) Expression of SEAP (secreted alkaline phosphatase) by baculovirus-mediated transduction of HEK 293 cells in a hollow fiber bioreactor system. J. Biotechnol. 135, 272-280
    • (2008) J. Biotechnol. , vol.135 , pp. 272-280
    • Jardin, B.A.1    Zhao, Y.2    Selvaraj, M.3    Montes, J.4    Tran, R.5    Prakash, S.6    Elias, C.B.7
  • 32
    • 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 Tyr-407 phosphorylation
    • Herzog, B., Pellet-Many, C., Britton, G., Hartzoulakis, B., and Zachary, I. C. (2011) VEGF binding to NRP1 is essential for VEGF stimulation of endothelial cell migration, complex formation between NRP1 and VEGFR2, and signaling via FAK Tyr-407 phosphorylation. Mol. Biol. Cell 22, 2766-2776
    • (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
  • 35
    • 34548500340 scopus 로고    scopus 로고
    • 165, but not to semaphorin 3F
    • DOI 10.1074/jbc.M702942200
    • Geretti, E., Shimizu, A., Kurschat, P., and Klagsbrun, M. (2007) Site-directed mutagenesis in the B-neuropilin-2 domain selectively enhances its affinity to VEGF165, but not to semaphorin 3F. J. Biol. Chem. 282, 25698-25707 (Pubitemid 47372796)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.35 , pp. 25698-25707
    • Geretti, E.1    Shimizu, A.2    Kurschat, P.3    Klagsbrun, M.4
  • 36
    • 76649105135 scopus 로고    scopus 로고
    • Direct contacts between extracellular membrane-proximal domains are required for VEGF receptor activation and cell signaling
    • Yang, Y., Xie, P., Opatowsky, Y., and Schlessinger, J. (2010) Direct contacts between extracellular membrane-proximal domains are required for VEGF receptor activation and cell signaling. Proc. Natl. Acad. Sci. U.S.A. 107, 1906-1911
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 1906-1911
    • Yang, Y.1    Xie, P.2    Opatowsky, Y.3    Schlessinger, J.4
  • 37
    • 75149176738 scopus 로고    scopus 로고
    • Transmembrane domain-mediated orientation of receptor monomers in active VEGFR-2 dimers
    • Dosch, D. D., and Ballmer-Hofer, K. (2010) Transmembrane domain-mediated orientation of receptor monomers in active VEGFR-2 dimers. FASEB J. 24, 32-38
    • (2010) FASEB J. , vol.24 , pp. 32-38
    • Dosch, D.D.1    Ballmer-Hofer, K.2


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