메뉴 건너뛰기




Volumn 407, Issue 4, 2011, Pages 581-593

The VD1 neutralizing antibody to vascular endothelial growth factor-D: Binding epitope and relationship to receptor binding

Author keywords

cancer; mutagenesis; structure function; therapeutics; VEGF D

Indexed keywords

EPITOPE; NEUTRALIZING ANTIBODY; UNCLASSIFIED DRUG; VASCULOTROPIN D; VASCULOTROPIN RECEPTOR 2; VASCULOTROPIN RECEPTOR 3; VD1 NEUTRALIZING ANTIBODY;

EID: 79952456041     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2011.02.009     Document Type: Article
Times cited : (18)

References (51)
  • 2
    • 63749125392 scopus 로고    scopus 로고
    • VEGFs and receptors involved in angiogenesis versus lymphangiogenesis
    • Lohela M., Bry M., Tammela T., and Alitalo K. VEGFs and receptors involved in angiogenesis versus lymphangiogenesis Curr. Opin. Cell Biol. 21 2009 154 165
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 154-165
    • Lohela, M.1    Bry, M.2    Tammela, T.3    Alitalo, K.4
  • 8
    • 0036844702 scopus 로고    scopus 로고
    • Molecular control of lymphangiogenesis
    • DOI 10.1002/bies.10173
    • Baldwin M.E., Stacker S.A., and Achen M.G. Molecular control of lymphangiogenesis BioEssays 24 2002 1030 1040 (Pubitemid 35326161)
    • (2002) BioEssays , vol.24 , Issue.11 , pp. 1030-1040
    • Baldwin, M.E.1    Stacker, S.A.2    Achen, M.G.3
  • 9
    • 0141621049 scopus 로고    scopus 로고
    • Viral vascular endothelial growth factors vary extensively in amino acid sequence, receptor-binding specificities, and the ability to induce vascular permeability yet are uniformly active mitogens
    • DOI 10.1074/jbc.M301194200
    • Wise L.M., Ueda N., Dryden N.H., Fleming S.B., Caesar C., and Roufail S. Viral vascular endothelial growth factors vary extensively in amino acid sequence, receptor-binding specificities, and the ability to induce vascular permeability yet are uniformly active mitogens J. Biol. Chem. 278 2003 38004 38014 (Pubitemid 37175331)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.39 , pp. 38004-38014
    • Wise, L.M.1    Ueda, N.2    Dryden, N.H.3    Fleming, S.B.4    Caesar, C.5    Roufail, S.6    Achen, M.G.7    Stacker, S.A.8    Mercer, A.A.9
  • 11
    • 47949083776 scopus 로고    scopus 로고
    • Deletion of vascular endothelial growth factor C (VEGF-C) and VEGF-D is not equivalent to VEGF receptor 3 deletion in mouse embryos
    • Haiko P., Makinen T., Keskitalo S., Taipale J., Karkkainen M.J., and Baldwin M.E. Deletion of vascular endothelial growth factor C (VEGF-C) and VEGF-D is not equivalent to VEGF receptor 3 deletion in mouse embryos Mol. Cell. Biol. 28 2008 4843 4850
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 4843-4850
    • Haiko, P.1    Makinen, T.2    Keskitalo, S.3    Taipale, J.4    Karkkainen, M.J.5    Baldwin, M.E.6
  • 12
    • 52649159125 scopus 로고    scopus 로고
    • Role of VEGF-D and VEGFR-3 in developmental lymphangiogenesis, a chemicogenetic study in Xenopus tadpoles
    • Ny A., Koch M., Vandevelde W., Schneider M., Fischer C., and Diez-Juan A. Role of VEGF-D and VEGFR-3 in developmental lymphangiogenesis, a chemicogenetic study in Xenopus tadpoles Blood 112 2008 1740 1749
    • (2008) Blood , vol.112 , pp. 1740-1749
    • Ny, A.1    Koch, M.2    Vandevelde, W.3    Schneider, M.4    Fischer, C.5    Diez-Juan, A.6
  • 15
    • 24344509918 scopus 로고    scopus 로고
    • Vascular endothelial growth factor-D induces lymphangiogenesis and lymphatic metastasis in models of ductal pancreatic cancer
    • Von Marschall Z., Scholz A., Stacker S.A., Achen M.G., Jackson D.G., and Alves F. Vascular endothelial growth factor-D induces lymphangiogenesis and lymphatic metastasis in models of ductal pancreatic cancer Int. J. Oncol. 27 2005 669 679
    • (2005) Int. J. Oncol. , vol.27 , pp. 669-679
    • Von Marschall, Z.1    Scholz, A.2    Stacker, S.A.3    Achen, M.G.4    Jackson, D.G.5    Alves, F.6
  • 17
    • 33746012247 scopus 로고    scopus 로고
    • Tumor lymphangiogenesis and metastatic spread - New players begin to emerge
    • DOI 10.1002/ijc.21899
    • Achen M.G., and Stacker S.A. Tumor lymphangiogenesis and metastatic spread-new players begin to emerge Int. J. Cancer 119 2006 1755 1760 (Pubitemid 44356830)
    • (2006) International Journal of Cancer , vol.119 , Issue.8 , pp. 1755-1760
    • Achen, M.G.1    Stacker, S.A.2
  • 18
    • 0037086278 scopus 로고    scopus 로고
    • Vascular endothelial growth factor-D expression is an independent prognostic marker for survival in colorectal carcinoma
    • White J.D., Hewett P.W., Kosuge D., McCulloch T., Enholm B.C., Carmichael J., and Murray J.C. Vascular endothelial growth factor-D expression is an independent prognostic marker for survival in colorectal carcinoma Cancer Res. 62 2002 1669 1675 (Pubitemid 34408487)
    • (2002) Cancer Research , vol.62 , Issue.6 , pp. 1669-1675
    • White, J.D.1    Hewett, P.W.2    Kosuge, D.3    McCulloch, T.4    Enholm, B.C.5    Carmichael, J.6    Murray, J.C.7
  • 20
    • 2642542542 scopus 로고    scopus 로고
    • Δ773-1081 overexpression is diagnostic for sentinel lymph node metastasis
    • DOI 10.1038/labinvest.3700075
    • Stearns M.E., Wang M., Hu Y., Kim G., and Garcia F.U. Expression of a flt-4 (VEGFR3) splicing variant in primary human prostate tumors. VEGF D and flt-4t(Delta773-1081) overexpression is diagnostic for sentinel lymph node metastasis Lab. Invest. 84 2004 785 795 (Pubitemid 38715478)
    • (2004) Laboratory Investigation , vol.84 , Issue.6 , pp. 785-795
    • Stearns, M.E.1    Wang, M.2    Hu, Y.3    Kim, G.4    Garcia, F.U.5
  • 22
    • 78649537524 scopus 로고    scopus 로고
    • Biomarkers to predict the clinical efficacy of bevacizumab in cancer
    • Jubb A.M., and Harris A.L. Biomarkers to predict the clinical efficacy of bevacizumab in cancer Lancet Oncol. 11 2010 1172 1183
    • (2010) Lancet Oncol. , vol.11 , pp. 1172-1183
    • Jubb, A.M.1    Harris, A.L.2
  • 25
    • 65949104047 scopus 로고    scopus 로고
    • Serum vascular endothelial growth factor-D levels in patients with lymphangioleiomyomatosis reflect lymphatic involvement
    • Glasgow C.G., Avila N.A., Lin J.P., Stylianou M.P., and Moss J. Serum vascular endothelial growth factor-D levels in patients with lymphangioleiomyomatosis reflect lymphatic involvement Chest 135 2009 1293 1300
    • (2009) Chest , vol.135 , pp. 1293-1300
    • Glasgow, C.G.1    Avila, N.A.2    Lin, J.P.3    Stylianou, M.P.4    Moss, J.5
  • 27
    • 0033527634 scopus 로고    scopus 로고
    • Biosynthesis of vascular endothelial growth factor-D involves proteolytic processing which generates non-covalent homodimers
    • Stacker S.A., Stenvers K., Caesar C., Vitali A., Domagala T., and Nice E. Biosynthesis of vascular endothelial growth factor-D involves proteolytic processing which generates non-covalent homodimers J. Biol. Chem. 274 1999 32127 32136
    • (1999) J. Biol. Chem. , vol.274 , pp. 32127-32136
    • Stacker, S.A.1    Stenvers, K.2    Caesar, C.3    Vitali, A.4    Domagala, T.5    Nice, E.6
  • 31
    • 21144437844 scopus 로고    scopus 로고
    • Vascular endothelial cell growth factor receptor 3-mediated activation of lymphatic endothelium is crucial for tumor cell entry and spread via lymphatic vessels
    • DOI 10.1158/0008-5472.CAN-04-4576
    • He Y., Rajantie I., Pajusola K., Jeltsch M., Holopainen T., and Yla-Herttuala S. Vascular endothelial cell growth factor receptor 3-mediated activation of lymphatic endothelium is crucial for tumor cell entry and spread via lymphatic vessels Cancer Res. 65 2005 4739 4746 (Pubitemid 40740810)
    • (2005) Cancer Research , vol.65 , Issue.11 , pp. 4739-4746
    • He, Y.1    Rajantie, I.2    Pajusola, K.3    Jeltsch, M.4    Holopainen, T.5    Yla-Herttuala, S.6    Harding, T.7    Jooss, K.8    Takahashi, T.9    Alitalo, K.10
  • 34
    • 0035377195 scopus 로고    scopus 로고
    • The specificity of receptor binding by vascular endothelial growth factor-d is different in mouse and man
    • Baldwin M.E., Catimel B., Nice E.C., Roufail S., Hall N.E., and Stenvers K.L. The specificity of receptor binding by vascular endothelial growth factor-d is different in mouse and man J. Biol. Chem. 276 2001 19166 19171
    • (2001) J. Biol. Chem. , vol.276 , pp. 19166-19171
    • Baldwin, M.E.1    Catimel, B.2    Nice, E.C.3    Roufail, S.4    Hall, N.E.5    Stenvers, K.L.6
  • 35
    • 0032857869 scopus 로고    scopus 로고
    • The vascular endothelial growth factor family: Signalling for vascular development
    • Stacker S.A., and Achen M.G. The vascular endothelial growth factor family: signalling for vascular development Growth Factors 17 1999 1 11 (Pubitemid 29435870)
    • (1999) Growth Factors , vol.17 , Issue.1 , pp. 1-11
    • Stacker, S.A.1    Achen, M.G.2
  • 36
    • 79551635313 scopus 로고    scopus 로고
    • Structural determinants of vascular endothelial growth factor-D receptor binding and specificity
    • Leppanen V.M., Jeltsch M., Anisimov A., Tvorogov D., Aho K., and Kalkkinen N. Structural determinants of vascular endothelial growth factor-D receptor binding and specificity Blood 117 2010 1507 1515
    • (2010) Blood , vol.117 , pp. 1507-1515
    • Leppanen, V.M.1    Jeltsch, M.2    Anisimov, A.3    Tvorogov, D.4    Aho, K.5    Kalkkinen, N.6
  • 37
    • 0031572858 scopus 로고    scopus 로고
    • The crystal structure of vascular endothelial growth factor (VEGF) refined to 1.93 A resolution: Multiple copy flexibility and receptor binding
    • Muller Y.A., Christinger H.W., Keyt B.A., and de Vos A.M. The crystal structure of vascular endothelial growth factor (VEGF) refined to 1.93 Å resolution: multiple copy flexibility and receptor binding Structure 5 1997 1325 1338 (Pubitemid 27484475)
    • (1997) Structure , vol.5 , Issue.10 , pp. 1325-1338
    • Muller, Y.A.1    Christinger, H.W.2    Keyt, B.A.3    De Vos, A.M.4
  • 38
    • 0035853679 scopus 로고    scopus 로고
    • The crystal structure of human placenta growth factor-1 (PlGF-1), an angiogenic protein, at 2.0 Å resolution
    • Iyer S., Leonidas D.D., Swaminathan G.J., Maglione D., Battisti M., and Tucci M. The crystal structure of human placenta growth factor-1 (PlGF-1), an angiogenic protein, at 2.0 Å resolution J. Biol. Chem. 276 2001 12153 12161
    • (2001) J. Biol. Chem. , vol.276 , pp. 12153-12161
    • Iyer, S.1    Leonidas, D.D.2    Swaminathan, G.J.3    Maglione, D.4    Battisti, M.5    Tucci, M.6
  • 39
    • 33646185640 scopus 로고    scopus 로고
    • Crystal structure of human vascular endothelial growth factor-B: Identification of amino acids important for receptor binding
    • Iyer S., Scotney P.D., Nash A.D., and Ravi Acharya K. Crystal structure of human vascular endothelial growth factor-B: identification of amino acids important for receptor binding J. Mol. Biol. 359 2006 76 85
    • (2006) J. Mol. Biol. , vol.359 , pp. 76-85
    • Iyer, S.1    Scotney, P.D.2    Nash, A.D.3    Ravi Acharya, K.4
  • 41
    • 0026708632 scopus 로고
    • The vascular endothelial growth factor proteins: Identification of biologically relevant regions by neutralizing monoclonal antibodies
    • Kim K.J., Li B., Houck K., Winer J., and Ferrara N. The vascular endothelial growth factor proteins: identification of biologically relevant regions by neutralizing monoclonal antibodies Growth Factors 7 1992 53 64
    • (1992) Growth Factors , vol.7 , pp. 53-64
    • Kim, K.J.1    Li, B.2    Houck, K.3    Winer, J.4    Ferrara, N.5
  • 42
    • 33646562554 scopus 로고    scopus 로고
    • Structure-function studies of two synthetic anti-vascular endothelial growth factor Fabs and comparison with the Avastin™ Fab
    • DOI 10.1074/jbc.M507783200
    • Fuh G., Wu P., Liang W.C., Ultsch M., Lee C.V., Moffat B., and Wiesmann C. Structure-function studies of two synthetic anti-vascular endothelial growth factor Fabs and comparison with the Avastin Fab J. Biol. Chem. 281 2006 6625 6631 (Pubitemid 43847597)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.10 , pp. 6625-6631
    • Fuh, G.1    Wu, P.2    Liang, W.-C.3    Ultsch, M.4    Lee, C.V.5    Moffat, B.6    Wiesmann, C.7
  • 43
    • 0032530717 scopus 로고    scopus 로고
    • VEGF and the Fab fragment of a humanized neutralizing antibody: Crystal structure of the complex at 2.4 A resolution and mutational analysis of the interface
    • Muller Y.A., Chen Y., Christinger H.W., Li B., Cunningham B.C., Lowman H.B., and de Vos A.M. VEGF and the Fab fragment of a humanized neutralizing antibody: crystal structure of the complex at 2.4 Å resolution and mutational analysis of the interface Structure 6 1998 1153 1167 (Pubitemid 28434118)
    • (1998) Structure , vol.6 , Issue.9 , pp. 1153-1167
    • Muller, Y.A.1    Chen, Y.2    Christinger, H.W.3    Li, B.4    Cunningham, B.C.5    Lowman, H.B.6    De Vos, A.M.7
  • 44
    • 20544455330 scopus 로고    scopus 로고
    • Bevacizumab (Avastin), a humanized anti-VEGF monoclonal antibody for cancer therapy
    • DOI 10.1016/j.bbrc.2005.05.132, PII S0006291X05011344
    • Ferrara N., Hillan K.J., and Novotny W. Bevacizumab (Avastin), a humanized anti-VEGF monoclonal antibody for cancer therapy Biochem. Biophys. Res. Commun. 333 2005 328 335 (Pubitemid 40848295)
    • (2005) Biochemical and Biophysical Research Communications , vol.333 , Issue.2 , pp. 328-335
    • Ferrara, N.1    Hillan, K.J.2    Novotny, W.3
  • 45
    • 56949090144 scopus 로고    scopus 로고
    • Crystal structure of vascular endothelial growth factor-B in complex with a neutralising antibody Fab fragment
    • Leonard P., Scotney P.D., Jabeen T., Iyer S., Fabri L.J., Nash A.D., and Acharya K.R. Crystal structure of vascular endothelial growth factor-B in complex with a neutralising antibody Fab fragment J. Mol. Biol. 384 2008 1203 1217
    • (2008) J. Mol. Biol. , vol.384 , pp. 1203-1217
    • Leonard, P.1    Scotney, P.D.2    Jabeen, T.3    Iyer, S.4    Fabri, L.J.5    Nash, A.D.6    Acharya, K.R.7
  • 46
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • DOI 10.1002/elps.1150181505
    • Guex N., and Peitsch M.C. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling Electrophoresis 18 1997 2714 2723 (Pubitemid 28059943)
    • (1997) Electrophoresis , vol.18 , Issue.15 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 47
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: An automated protein homology-modeling server
    • DOI 10.1093/nar/gkg520
    • Schwede T., Kopp J., Guex N., and Peitsch M.C. SWISS-MODEL: an automated protein homology-modeling server Nucleic Acids Res. 31 2003 3381 3385 (Pubitemid 37442164)
    • (2003) Nucleic Acids Research , vol.31 , Issue.13 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 48
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: A web-based environment for protein structure homology modelling
    • DOI 10.1093/bioinformatics/bti770
    • Arnold K., Bordoli L., Kopp J., and Schwede T. The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling Bioinformatics 22 2006 195 201 (Pubitemid 43205406)
    • (2006) Bioinformatics , vol.22 , Issue.2 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 50
    • 0032540222 scopus 로고    scopus 로고
    • Assessing protein structures with a non-local atomic interaction energy
    • DOI 10.1006/jmbi.1998.1665
    • Melo F., and Feytmans E. Assessing protein structures with a non-local atomic interaction energy J. Mol. Biol. 277 1998 1141 1152 (Pubitemid 28190852)
    • (1998) Journal of Molecular Biology , vol.277 , Issue.5 , pp. 1141-1152
    • Melo, F.1    Feytmans, E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.