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Volumn 111, Issue 7, 2008, Pages 3479-3488

A proangiogenic peptide derived from vascular endothelial growth factor receptor-1 acts through ά5Β1 integrin

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; ANGIOGENIC PROTEIN; GROWTH FACTOR; IMMUNOGLOBULIN; PEPTIDE; VASCULOTROPIN A; VASCULOTROPIN RECEPTOR 1; VERY LATE ACTIVATION ANTIGEN 5; VEGFA PROTEIN, HUMAN;

EID: 43549106854     PISSN: 00064971     EISSN: 15280020     Source Type: Journal    
DOI: 10.1182/blood-2007-03-077537     Document Type: Article
Times cited : (31)

References (40)
  • 1
    • 0032053767 scopus 로고    scopus 로고
    • Signaling angiogenesis and lymphangiogenesis
    • Korpelainen E, Alitalo K. Signaling angiogenesis and lymphangiogenesis. Curr Opin Cell Biol. 1998;10:159-164.
    • (1998) Curr Opin Cell Biol , vol.10 , pp. 159-164
    • Korpelainen, E.1    Alitalo, K.2
  • 2
    • 0025259592 scopus 로고
    • Nucleotide sequence and expression of a novel human receptor-type tyrosine kinase (flt) closely related to the fms family
    • Shibuya M, Yamaguchi S, Yamane A, et al. Nucleotide sequence and expression of a novel human receptor-type tyrosine kinase (flt) closely related to the fms family. Oncogene. 1990;8:519-527.
    • (1990) Oncogene , vol.8 , pp. 519-527
    • Shibuya, M.1    Yamaguchi, S.2    Yamane, A.3
  • 3
    • 0030782410 scopus 로고    scopus 로고
    • Crystal structure at 1.7 A resolution of VEGF in complex with domain 2 of the Flt-1 receptor
    • Wiesmann C, Fuh G, Christinger HW, Eigenbrot C, Wells JA, de Vos AM. Crystal structure at 1.7 A resolution of VEGF in complex with domain 2 of the Flt-1 receptor. Cell. 1997;91:695-704.
    • (1997) Cell , vol.91 , pp. 695-704
    • Wiesmann, C.1    Fuh, G.2    Christinger, H.W.3    Eigenbrot, C.4    Wells, J.A.5    de Vos, A.M.6
  • 4
    • 1642297115 scopus 로고    scopus 로고
    • The crystal structure of placental growth factor in complex with domain 2 of vascular endothelial growth factor receptor-1
    • Christinger HW; Fuh G, de Vos AM, Wiesmann C. The crystal structure of placental growth factor in complex with domain 2 of vascular endothelial growth factor receptor-1. J Biol Chem. 2004;279:10382-10388.
    • (2004) J Biol Chem , vol.279 , pp. 10382-10388
    • Christinger, H.W.1    Fuh, G.2    de Vos, A.M.3    Wiesmann, C.4
  • 5
    • 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;275:26690-26695.
    • (2000) J Biol Chem , vol.275 , pp. 26690-26695
    • Fuh, G.1    Garcia, K.C.2    de Vos, A.M.3
  • 6
    • 19244379078 scopus 로고    scopus 로고
    • Synergism between vascular endothelial growth factor and placental growth factor contributes to angiogenesis and plasma extravasation in pathologic conditions
    • Carmeliet P, Moons L. Luttun A, et al. Synergism between vascular endothelial growth factor and placental growth factor contributes to angiogenesis and plasma extravasation in pathologic conditions. Nat Med. 2001;7:575-583.
    • (2001) Nat Med , vol.7 , pp. 575-583
    • Carmeliet, P.1    Moons, L.2    Luttun, A.3
  • 7
    • 0035254646 scopus 로고    scopus 로고
    • Flt-1, vascular endothelial receptor 1, is a novel cell surface marker for the lineage of monocyte-macrophages in humans
    • Sawano A, Iwai S. Sakurai Y, et al. Flt-1, vascular endothelial receptor 1, is a novel cell surface marker for the lineage of monocyte-macrophages in humans. Blood. 2001;97:785-791.
    • (2001) Blood , vol.97 , pp. 785-791
    • Sawano, A.1    Iwai, S.2    Sakurai, Y.3
  • 8
    • 0035160312 scopus 로고    scopus 로고
    • Impaired recruitment of bone-marrow-derived endothelial and hematopoietic precursor cells blocks tumor angiogenesis and growth
    • Lyden D, Hattori K. Dias S, et al. Impaired recruitment of bone-marrow-derived endothelial and hematopoietic precursor cells blocks tumor angiogenesis and growth. Nat Med. 2001;7:1194-1201.
    • (2001) Nat Med , vol.7 , pp. 1194-1201
    • Lyden, D.1    Hattori, K.2    Dias, S.3
  • 9
    • 0036344495 scopus 로고    scopus 로고
    • Revascularization of ischemic tissues by PIGF treatment, and inhibition of tumor angiogenesis, arthritis and atherosclerosis by anti-Flt-1
    • Luttun A. Tjwa M, Moons L. et al. Revascularization of ischemic tissues by PIGF treatment, and inhibition of tumor angiogenesis, arthritis and atherosclerosis by anti-Flt-1. Nat Med. 2002;8:831-840.
    • (2002) Nat Med , vol.8 , pp. 831-840
    • Luttun, A.1    Tjwa, M.2    Moons, L.3
  • 10
    • 0029021660 scopus 로고
    • Role of the Flt-1 receptor tyrosine kinase in regulating the assembly of vascular endothelium
    • Fong G, Rossant J, Gertsenstein M, Breitman M. Role of the Flt-1 receptor tyrosine kinase in regulating the assembly of vascular endothelium. Nature. 1995;376:66-70.
    • (1995) Nature , vol.376 , pp. 66-70
    • Fong, G.1    Rossant, J.2    Gertsenstein, M.3    Breitman, M.4
  • 11
    • 0032764427 scopus 로고    scopus 로고
    • Increased hemangioblast commitment, not vascular dis-organization, is the primary defect in flt-1 knock-out mice
    • Fong G, Zhang L, Bryce D, Peng J. Increased hemangioblast commitment, not vascular dis-organization, is the primary defect in flt-1 knock-out mice. Development. 1999;126:3015-3025.
    • (1999) Development , vol.126 , pp. 3015-3025
    • Fong, G.1    Zhang, L.2    Bryce, D.3    Peng, J.4
  • 12
    • 0032482978 scopus 로고    scopus 로고
    • Flt-1 lacking the tyrosine kinase domain is sufficient for normal development and angiogenesis in mice
    • Hiratsuka S, Minowa O. Kuno J, Noda T, Shibuya M. Flt-1 lacking the tyrosine kinase domain is sufficient for normal development and angiogenesis in mice. Proc Natl Acad Sci U S A. 1998;95:9349-9354.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 9349-9354
    • Hiratsuka, S.1    Minowa, O.2    Kuno, J.3    Noda, T.4    Shibuya, M.5
  • 13
    • 0027421333 scopus 로고
    • Inhibition of vascular endothelial cell growth factor activity by an endogenously encoded soluble receptor
    • Kendall RL, Thomas KA. Inhibition of vascular endothelial cell growth factor activity by an endogenously encoded soluble receptor. Proc Natl Acad Sci U S A. 1993;90:10705-10709.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 10705-10709
    • Kendall, R.L.1    Thomas, K.A.2
  • 14
    • 0034598983 scopus 로고    scopus 로고
    • Identification of a vascular endothelial growth factor (VEGF) antagonist, sFlt-1, from a human hematopoietic cell line NALM-16
    • Inoue T, Kibata K, Suzuki M. Nakamura S. Motoda R, Orita K. Identification of a vascular endothelial growth factor (VEGF) antagonist, sFlt-1, from a human hematopoietic cell line NALM-16. FEBS Lett. 2000;469:14-18.
    • (2000) FEBS Lett , vol.469 , pp. 14-18
    • Inoue, T.1    Kibata, K.2    Suzuki, M.3    Nakamura, S.4    Motoda, R.5    Orita, K.6
  • 15
    • 0042328366 scopus 로고    scopus 로고
    • Vascular endothelial growth factor receptor-1 is deposited in the extracellular matrix by endothelial cells and is a ligand for the α5β1 integrin
    • Orecchia A, Lacal PM, Schietroma C, Morea V, Zambruno G, Failla CM. Vascular endothelial growth factor receptor-1 is deposited in the extracellular matrix by endothelial cells and is a ligand for the α5β1 integrin. J Cell Sci. 2003;116:3479-3489.
    • (2003) J Cell Sci , vol.116 , pp. 3479-3489
    • Orecchia, A.1    Lacal, P.M.2    Schietroma, C.3    Morea, V.4    Zambruno, G.5    Failla, C.M.6
  • 16
    • 0035983579 scopus 로고    scopus 로고
    • Central role of alpha5beta1 integrin and fibronectin in vascular development in mouse embryos and embryoid bodies
    • Francis SE, Goh KL, Hodivala-Dilke K, et al. Central role of alpha5beta1 integrin and fibronectin in vascular development in mouse embryos and embryoid bodies. Arterioscler Thromb Vase Biol. 2002;22:927-933.
    • (2002) Arterioscler Thromb Vase Biol , vol.22 , pp. 927-933
    • Francis, S.E.1    Goh, K.L.2    Hodivala-Dilke, K.3
  • 17
    • 0033843942 scopus 로고    scopus 로고
    • Regulation of angiogenesis in vivo by ligation of integrin α5β1 with the central cell-binding domain of fibronectin
    • Kirn S, Bell K, Mausa SA, Varner JA. Regulation of angiogenesis in vivo by ligation of integrin α5β1 with the central cell-binding domain of fibronectin. Am J Pathol. 2000;156:1345-1362.
    • (2000) Am J Pathol , vol.156 , pp. 1345-1362
    • Kirn, S.1    Bell, K.2    Mausa, S.A.3    Varner, J.A.4
  • 18
  • 19
    • 0142026204 scopus 로고    scopus 로고
    • Therapeutic antagonists and conformational regulation of integrin function
    • Shimaoka M, Springer TA. Therapeutic antagonists and conformational regulation of integrin function. Nat Rev Drug Discov. 2003;2:703-716.
    • (2003) Nat Rev Drug Discov , vol.2 , pp. 703-716
    • Shimaoka, M.1    Springer, T.A.2
  • 20
    • 2242453283 scopus 로고    scopus 로고
    • Pro-angiogenic activities of CYR61 (GCN1) mediated through integrins alphavbeta3 and alpha6beta1 in human umbilical vein endothelial cells
    • Leu S. Lam S, Lau L. Pro-angiogenic activities of CYR61 (GCN1) mediated through integrins alphavbeta3 and alpha6beta1 in human umbilical vein endothelial cells. J Biol Chem. 2002;277:46248-46255.
    • (2002) J Biol Chem , vol.277 , pp. 46248-46255
    • Leu, S.1    Lam, S.2    Lau, L.3
  • 21
    • 2342417499 scopus 로고    scopus 로고
    • The rabbit corneal pocket assay for the study of angiogenesis
    • Morbidelli L, Ziche M. The rabbit corneal pocket assay for the study of angiogenesis. Gancer Treat Res. 2004;117:147-151.
    • (2004) Gancer Treat Res , vol.117 , pp. 147-151
    • Morbidelli, L.1    Ziche, M.2
  • 23
    • 46149129351 scopus 로고
    • Interactive program for visualization and modelling of proteins, nucleic acids and small molecules
    • Dayringer HE, Tramontano A, Spang SR, Fletterick RJ. Interactive program for visualization and modelling of proteins, nucleic acids and small molecules. J Mol Graph. 1986;4:82-87.
    • (1986) J Mol Graph , vol.4 , pp. 82-87
    • Dayringer, H.E.1    Tramontano, A.2    Spang, S.R.3    Fletterick, R.J.4
  • 24
    • 0035853460 scopus 로고    scopus 로고
    • A small peptide derived from Fit-1 (VEGFR-1) functions as an angiogenic inhibitor
    • Tan DCW, Manjunatha Kini R, Jois SDS, Lim DKF, Xin L, Ge R. A small peptide derived from Fit-1 (VEGFR-1) functions as an angiogenic inhibitor. FEBS Lett. 2001;494:150-156.
    • (2001) FEBS Lett , vol.494 , pp. 150-156
    • Tan, D.C.W.1    Manjunatha Kini, R.2    Jois, S.D.S.3    Lim, D.K.F.4    Xin, L.5    Ge, R.6
  • 25
    • 0031050449 scopus 로고    scopus 로고
    • Molecular interactions in cell adhesion complexes
    • Yamada KM, Geiger B. Molecular interactions in cell adhesion complexes. Gurr Opin Gell Biol. 1997;9:76-85.
    • (1997) Gurr Opin Gell Biol , vol.9 , pp. 76-85
    • Yamada, K.M.1    Geiger, B.2
  • 26
    • 0032488966 scopus 로고    scopus 로고
    • Mapping the charged residues in the second immunoglobulin-like domain of the vascular endothelial growth factor/placenta growth factor receptor Fit-1 required for binding and structural stability
    • Davis-Smyth T, Presta LG, Ferrara N. Mapping the charged residues in the second immunoglobulin-like domain of the vascular endothelial growth factor/placenta growth factor receptor Fit-1 required for binding and structural stability. J Biol Chem. 1998;273:3216-3222.
    • (1998) J Biol Chem , vol.273 , pp. 3216-3222
    • Davis-Smyth, T.1    Presta, L.G.2    Ferrara, N.3
  • 27
    • 33947416658 scopus 로고    scopus 로고
    • Sunitinib: A VEGF and PDGF receptor protein kinase and angiogenesis inhibitor
    • Roskoski RJ. Sunitinib: a VEGF and PDGF receptor protein kinase and angiogenesis inhibitor. Biochem Biophys Res Commun. 2007;356:323-328.
    • (2007) Biochem Biophys Res Commun , vol.356 , pp. 323-328
    • Roskoski, R.J.1
  • 28
    • 0034711221 scopus 로고    scopus 로고
    • Distinct roles of the adaptor protein She and focal adhesion kinase in integrin signaling to ERK
    • Barberis L, Wary KK, Fiucci G, et al. Distinct roles of the adaptor protein She and focal adhesion kinase in integrin signaling to ERK. J Biol Chem. 2000;275:36532-36540.
    • (2000) J Biol Chem , vol.275 , pp. 36532-36540
    • Barberis, L.1    Wary, K.K.2    Fiucci, G.3
  • 29
    • 0035824920 scopus 로고    scopus 로고
    • Integrin and growth factor receptor crosstalk
    • Eliceri BP. Integrin and growth factor receptor crosstalk. Circ Res. 2001;89:1104-1110.
    • (2001) Circ Res , vol.89 , pp. 1104-1110
    • Eliceri, B.P.1
  • 30
    • 34548036519 scopus 로고    scopus 로고
    • VEGFR-1(FLT-1), β1 integrin, and hERG k+ channel for a macromolecular signaling complex in acute myeloid leukemia: Role in cell migration and clinical outcome
    • Pillozzi S, Brizzi ME Bernabei PA, et al. VEGFR-1(FLT-1), β1 integrin, and hERG k+ channel for a macromolecular signaling complex in acute myeloid leukemia: role in cell migration and clinical outcome. Blood. 2007;110:1238-1250.
    • (2007) Blood , vol.110 , pp. 1238-1250
    • Pillozzi, S.1    Brizzi, M.E.2    Bernabei, P.A.3
  • 31
    • 0027267959 scopus 로고
    • Selection of peptides binding to the α5β1 integrin from phage display library
    • Koivunen E, Gay DA, Ruoslahti E. Selection of peptides binding to the α5β1 integrin from phage display library. J Biol Chem. 1993;268:20205-20210.
    • (1993) J Biol Chem , vol.268 , pp. 20205-20210
    • Koivunen, E.1    Gay, D.A.2    Ruoslahti, E.3
  • 32
    • 0027976103 scopus 로고
    • Isolation of a highly specific ligand for the alpha5 betal integrin from a phage display library
    • Koivunen E, Wang B, Ruoslahti E. Isolation of a highly specific ligand for the alpha5 betal integrin from a phage display library. J Cell Biol. 1994;124:373-380.
    • (1994) J Cell Biol , vol.124 , pp. 373-380
    • Koivunen, E.1    Wang, B.2    Ruoslahti, E.3
  • 33
    • 34547941252 scopus 로고    scopus 로고
    • Autocrine VEGF signaling is required for vascular homeostasis
    • Lee S, Chen TT, Barber CL, et al. Autocrine VEGF signaling is required for vascular homeostasis. Cell. 2007;130:691-703.
    • (2007) Cell , vol.130 , pp. 691-703
    • Lee, S.1    Chen, T.T.2    Barber, C.L.3
  • 34
    • 33749676409 scopus 로고    scopus 로고
    • Heparin-ll domain of tibronectin is a vascular endothelial growth factor-binding domain
    • Wijelath ES, Rahman S, Namekata M, et al. Heparin-ll domain of tibronectin is a vascular endothelial growth factor-binding domain. Circ Res. 2006;99:853-860.
    • (2006) Circ Res , vol.99 , pp. 853-860
    • Wijelath, E.S.1    Rahman, S.2    Namekata, M.3
  • 35
    • 0033558087 scopus 로고    scopus 로고
    • Role of αvβ3 integrin in the activation of vascular endothelial growth factor receptor-2
    • Soldi R, Mitola S, Stasly M, Defilippi P, Tarone G, Bussolino F. Role of αvβ3 integrin in the activation of vascular endothelial growth factor receptor-2. EMBO J. 1999;18:882-892.
    • (1999) EMBO J , vol.18 , pp. 882-892
    • Soldi, R.1    Mitola, S.2    Stasly, M.3    Defilippi, P.4    Tarone, G.5    Bussolino, F.6
  • 36
    • 2942556514 scopus 로고    scopus 로고
    • The VEGF receptor fit-1 (VEGFR-1) is a positive modulator of vascular sprout formation and branching morphogenesis
    • Kearney JB. Kappas NC. Ellerstrom C. DiPaola FW, Bautch VL. The VEGF receptor fit-1 (VEGFR-1) is a positive modulator of vascular sprout formation and branching morphogenesis. Blood. 2004;103:4527-4535.
    • (2004) Blood , vol.103 , pp. 4527-4535
    • Kearney, J.B.1    Kappas, N.C.2    Ellerstrom, C.3    DiPaola, F.W.4    Bautch, V.L.5
  • 37
    • 1942437424 scopus 로고    scopus 로고
    • The VEGF receptor flt-1 (VEGFR-1) modulates flk-1 (VEGFR-2) signaling during blood vessel formation
    • Roberts DM, Kearney JB, Johnson JH, Rosenberg MP, Kumar R, Bautch VL. The VEGF receptor flt-1 (VEGFR-1) modulates flk-1 (VEGFR-2) signaling during blood vessel formation. Am J Pathol. 2004;164:1531-1535.
    • (2004) Am J Pathol , vol.164 , pp. 1531-1535
    • Roberts, D.M.1    Kearney, J.B.2    Johnson, J.H.3    Rosenberg, M.P.4    Kumar, R.5    Bautch, V.L.6
  • 38
    • 0032502843 scopus 로고    scopus 로고
    • Regional suppression of tumor growth by in vivo transfer of a cDNA encoding a secreted form of the extracellular domain of the flt-1 vascular endothelial growth factor receptor
    • Kong HL, Hecht D, Song W, et al. Regional suppression of tumor growth by in vivo transfer of a cDNA encoding a secreted form of the extracellular domain of the flt-1 vascular endothelial growth factor receptor. Hum Gene Ther. 1998;9:823-833.
    • (1998) Hum Gene Ther , vol.9 , pp. 823-833
    • Kong, H.L.1    Hecht, D.2    Song, W.3
  • 39
    • 33750430869 scopus 로고    scopus 로고
    • Corneal avascularity is due to soluble VEGF receptor-1
    • Ambati BK, Nozaki M, Singh N, et al. Corneal avascularity is due to soluble VEGF receptor-1. Nature. 2006;443:993-997.
    • (2006) Nature , vol.443 , pp. 993-997
    • Ambati, B.K.1    Nozaki, M.2    Singh, N.3
  • 40
    • 84975525035 scopus 로고
    • Clinical applications of research on angiogenesis
    • Folkman J. Clinical applications of research on angiogenesis. N Engl J Med. 1995;333:1757-1763.
    • (1995) N Engl J Med , vol.333 , pp. 1757-1763
    • Folkman, J.1


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