메뉴 건너뛰기




Volumn 9, Issue 7, 2003, Pages 936-943

Role of PlGF in the intra- and intermolecular cross talk between the VEGF receptors Flt1 and Flk1

(28)  Autiero, Monica a   Waltenberger, Johannes b   Communi, Didier a   Kranz, Andrea b   Moons, Lieve a   Lambrechts, Diether a   Kroll, Jens b   Plaisance, Stephane a   De Mol, Maria a   Bono, Françoise c   Kliche, Stefanie b   Fellbrich, Guido b   Ballmer Hofer, Kurt d   Maglione, Domenico e   Mayr Beyrle, Ulrike b   Dewerchin, Mieke a   Dombrowski, Saskia b   Stanimirovic, Danica f   Van Hummelen, Paul a   Dehio, Christoph g   more..

c SANOFI   (France)

Author keywords

[No Author keywords available]

Indexed keywords

ANGIOPOIETIN; DECORIN; EARLY GROWTH RESPONSE FACTOR 1; FOLLISTATIN; GROWTH FACTOR; JANUS KINASE; MITOGEN ACTIVATED PROTEIN KINASE; NEUROPILIN 2; PLACENTAL GROWTH FACTOR; PROTEIN TYROSINE KINASE; UNCLASSIFIED DRUG; VASCULOTROPIN RECEPTOR; VASCULOTROPIN RECEPTOR 1; VASCULOTROPIN RECEPTOR 2;

EID: 0037703184     PISSN: 10788956     EISSN: None     Source Type: Journal    
DOI: 10.1038/nm884     Document Type: Article
Times cited : (674)

References (46)
  • 1
    • 0033547805 scopus 로고    scopus 로고
    • Age-dependent impairment of angiogenesis
    • Rivard, A. et al. Age-dependent impairment of angiogenesis. Circulation 99, 111-120 (1999).
    • (1999) Circulation , vol.99 , pp. 111-120
    • Rivard, A.1
  • 3
    • 0035895708 scopus 로고    scopus 로고
    • Impaired collateral vessel development in diabetes: Potential cellular mechanisms and therapeutic implications
    • Waltenberger, J. Impaired collateral vessel development in diabetes: potential cellular mechanisms and therapeutic implications. Cardiovasc. Res. 49, 554-560 (2001).
    • (2001) Cardiovasc. Res. , vol.49 , pp. 554-560
    • Waltenberger, J.1
  • 5
    • 0034644539 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • Schlessinger, J. Cell signaling by receptor tyrosine kinases. Cell 103, 211-225 (2000).
    • (2000) Cell , vol.103 , pp. 211-225
    • Schlessinger, J.1
  • 6
    • 0034979273 scopus 로고    scopus 로고
    • Role of vascular endothelial growth factor in regulation of physiological angiogenesis
    • Ferrara, N. Role of vascular endothelial growth factor in regulation of physiological angiogenesis, Am. J. Physiol. Cell. Physiol. 280, C1358-C1366 (2001).
    • (2001) Am. J. Physiol. Cell. Physiol. , vol.280
    • Ferrara, N.1
  • 7
    • 0028134936 scopus 로고
    • Placenta growth factor. Potentiation of vascular endothelial growth factor bioactivity, in vitro and in vivo, and high affinity binding to Flt-1 but not to Flk-1/KDR
    • Park, J.E., Chen, H.H., Winer, J., Houck, K.A. & Ferrara, N. Placenta growth factor. Potentiation of vascular endothelial growth factor bioactivity, in vitro and in vivo, and high affinity binding to Flt-1 but not to Flk-1/KDR. J. Biol. Chem. 269, 25646-25654 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 25646-25654
    • Park, J.E.1    Chen, H.H.2    Winer, J.3    Houck, K.A.4    Ferrara, N.5
  • 8
    • 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. USA 95, 9349-9354 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 9349-9354
    • Hiratsuka, S.1    Minowa, O.2    Kuno, J.3    Noda, T.4    Shibuya, M.5
  • 9
    • 0035114105 scopus 로고    scopus 로고
    • Involvement of Flt-1 tyrosine kinase (vascular endothelial growth factor receptor-1) in pathological angiogenesis
    • Hiratsuka, S. et al. Involvement of Flt-1 tyrosine kinase (vascular endothelial growth factor receptor-1) in pathological angiogenesis. Cancer Res. 61, 1207-1213 (2001).
    • (2001) Cancer Res. , vol.61 , pp. 1207-1213
    • Hiratsuka, S.1
  • 10
    • 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. et al. Revascularization of ischemic tissues by PIGF treatment, and inhibition of tumor angiogenesis, arthritis and atherosclerosis by anti-Flt1. Nat. Med. 8, 831-840 (2002).
    • (2002) Nat. Med. , vol.8 , pp. 831-840
    • Luttun, A.1
  • 11
    • 0035920244 scopus 로고    scopus 로고
    • VPF/VEGF receptor-1 down-modulates VPF/VEGF receptor-2 mediated endothelial cell proliferation, but not migration, through phosphatidylinositol 3-kinase dependent pathways
    • Zeng, H., Dvorak, H.F. & Mukhopadhyay, D. VPF/VEGF receptor-1 down-modulates VPF/VEGF receptor-2 mediated endothelial cell proliferation, but not migration, through phosphatidylinositol 3-kinase dependent pathways. J. Biol. Chem. 276, 26969-26979 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 26969-26979
    • Zeng, H.1    Dvorak, H.F.2    Mukhopadhyay, D.3
  • 12
    • 0037040225 scopus 로고    scopus 로고
    • Flt-1-mediated down-regulation of endothelial cell proliferation through pertussis toxin-sensitive G proteins, beta gamma subunits, small GTPase CDC42, and partly by Rac-1
    • Zeng, H., Zhao, D. & Mukhopadhyay, D. Flt-1-mediated down-regulation of endothelial cell proliferation through pertussis toxin-sensitive G proteins, beta gamma subunits, small GTPase CDC42, and partly by Rac-1. J. Biol. Chem. 277, 4003-4009 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 4003-4009
    • Zeng, H.1    Zhao, D.2    Mukhopadhyay, D.3
  • 13
    • 0034254273 scopus 로고    scopus 로고
    • A repressor sequence in the juxtamembrane domain of Flt-1 (VEGFR-1) constitutively inhibits vascular endothelial growth factor-dependent phosphatidylinositol 3′-kinase activation and endothelial cell migration
    • Gille, H. et al. A repressor sequence in the juxtamembrane domain of Flt-1 (VEGFR-1) constitutively inhibits vascular endothelial growth factor-dependent phosphatidylinositol 3′-kinase activation and endothelial cell migration. EMBO J. 19, 4064-4073 (2000).
    • (2000) EMBO J. , vol.19 , pp. 4064-4073
    • Gille, H.1
  • 14
    • 0036845084 scopus 로고    scopus 로고
    • Vascular endothelial growth factor-induced genes in human umbilical vein endothelial cells. Relative roles of KDR and Flt-1 receptors
    • Yang, S. et al. Vascular endothelial growth factor-induced genes in human umbilical vein endothelial cells. Relative roles of KDR and Flt-1 receptors. Arterioscler. Thromb. Vasc. Biol. 22, 1797-1803 (2002).
    • (2002) Arterioscler. Thromb. Vasc. Biol. , vol.22 , pp. 1797-1803
    • Yang, S.1
  • 15
    • 0034595635 scopus 로고    scopus 로고
    • Receptor chimeras indicate that the VEGFR-1 modulates mitogenic activity of VEGFR-2 in endothelial cells
    • Rahimi, N., Dayanir, V. & Lashkari, K. Receptor chimeras indicate that the VEGFR-1 modulates mitogenic activity of VEGFR-2 in endothelial cells. J. Biol. Chem. 275, 16986-16992 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 16986-16992
    • Rahimi, N.1    Dayanir, V.2    Lashkari, K.3
  • 16
    • 0034690028 scopus 로고    scopus 로고
    • Roles of two VEGF receptors, Flt-1 and KDR, in the signal transduction of VEGF effects in human vascular endothelial cells
    • Kanno, S. et al. Roles of two VEGF receptors, Flt-1 and KDR, in the signal transduction of VEGF effects in human vascular endothelial cells. Oncogene 19, 2138-2146 (2000).
    • (2000) Oncogene , vol.19 , pp. 2138-2146
    • Kanno, S.1
  • 17
    • 19244379078 scopus 로고    scopus 로고
    • Synergism between vascular endothelial growth factor and placental growth factor contributes to angiogenesis and plasma extravasation in pathological conditions
    • Carmeliet, P. et al. Synergism between vascular endothelial growth factor and placental growth factor contributes to angiogenesis and plasma extravasation in pathological conditions. Nat. Med. 7, 575-583 (2001).
    • (2001) Nat. Med. , vol.7 , pp. 575-583
    • Carmeliet, P.1
  • 18
    • 0037093078 scopus 로고    scopus 로고
    • Placental growth factor is a survival factor for tumor endothelial cells and macrophages
    • Adini, A., Kornaga, T., Firoozbakht, F. & Benjamin, L.E. Placental growth factor is a survival factor for tumor endothelial cells and macrophages. Cancer Res. 62, 2749-2752 (2002).
    • (2002) Cancer Res. , vol.62 , pp. 2749-2752
    • Adini, A.1    Kornaga, T.2    Firoozbakht, F.3    Benjamin, L.E.4
  • 19
    • 0037096168 scopus 로고    scopus 로고
    • Mice overexpressing placenta growth factor exhibit increased vascularization and vessel permeability
    • Odorisio, T. et al. Mice overexpressing placenta growth factor exhibit increased vascularization and vessel permeability. J. Cell Sci. 115, 2559-2567 (2002).
    • (2002) J. Cell Sci. , vol.115 , pp. 2559-2567
    • Odorisio, T.1
  • 20
    • 0036344496 scopus 로고    scopus 로고
    • Placental growth factor reconstitutes hematopoiesis by recruiting VEGFRI(+) stem cells from bone-marrow microenvironment
    • Hattori, K. et al. Placental growth factor reconstitutes hematopoiesis by recruiting VEGFRI(+) stem cells from bone-marrow microenvironment. Nat. Med. 8, 841-849 (2002).
    • (2002) Nat. Med. , vol.8 , pp. 841-849
    • Hattori, K.1
  • 21
    • 0036310966 scopus 로고    scopus 로고
    • Effects of angiogenic growth factor combinations on retinal endothelial cells
    • Castellon, R. et al. Effects of angiogenic growth factor combinations on retinal endothelial cells. Exp. Eye Res. 74, 523-535 (2002).
    • (2002) Exp. Eye Res. , vol.74 , pp. 523-535
    • Castellon, R.1
  • 22
    • 0030582384 scopus 로고    scopus 로고
    • Identification of a natural soluble form of the vascular endothelial growth factor receptor, FLT-1, and its heterodimerization with KDR
    • Kendall, R.L., Wang, G. & Thomas, K.A. Identification of a natural soluble form of the vascular endothelial growth factor receptor, FLT-1, and its heterodimerization with KDR. Biochem. Biophys. Res. Commun. 226, 324-328 (1996).
    • (1996) Biochem. Biophys. Res. Commun. , vol.226 , pp. 324-328
    • Kendall, R.L.1    Wang, G.2    Thomas, K.A.3
  • 24
    • 0029849637 scopus 로고    scopus 로고
    • In vivo angiogenic activity and hypoxia induction of heterodimers of placenta growth factor/vascular endothelial growth factor
    • Cao, Y., Linden, P., Shima, D., Browne, F. & Folkman, J. In vivo angiogenic activity and hypoxia induction of heterodimers of placenta growth factor/vascular endothelial growth factor. J. Clin. Invest. 98, 2507-2511 (1996).
    • (1996) J. Clin. Invest. , vol.98 , pp. 2507-2511
    • Cao, Y.1    Linden, P.2    Shima, D.3    Browne, F.4    Folkman, J.5
  • 25
    • 0028956308 scopus 로고
    • Purification and characterization of a naturally occurring vascular endothelial growth factor placenta growth factor heterodimer
    • DiSalvo, J. et al. Purification and characterization of a naturally occurring vascular endothelial growth factor placenta growth factor heterodimer. J. Biol. Chem. 270, 7717-7723 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 7717-7723
    • DiSalvo, J.1
  • 26
    • 17044441694 scopus 로고    scopus 로고
    • Placenta growth factor-1 antagonizes VEGF-induced angiogenesis and tumor growth by the formation of functionally inactive PGF-1/VEGF heterodimers
    • Eriksson, A. et al. Placenta growth factor-1 antagonizes VEGF-induced angiogenesis and tumor growth by the formation of functionally inactive PGF-1/VEGF heterodimers. Cancer Cell 1, 99-108 (2002).
    • (2002) Cancer Cell , vol.1 , pp. 99-108
    • Eriksson, A.1
  • 27
    • 0035355472 scopus 로고    scopus 로고
    • A single autophosphorylation site on KDR/Flk-1 is essential for VEGF-A-dependent activation of PLC-gamma and DNA synthesis in vascular endothelial cells
    • Takahashi, T., Yamaguchi, S., Chida, K. & Shibuya, M. A single autophosphorylation site on KDR/Flk-1 is essential for VEGF-A-dependent activation of PLC-gamma and DNA synthesis in vascular endothelial cells. EMBO J. 20, 2768-2778 (2001).
    • (2001) EMBO J. , vol.20 , pp. 2768-2778
    • Takahashi, T.1    Yamaguchi, S.2    Chida, K.3    Shibuya, M.4
  • 28
    • 0034703039 scopus 로고    scopus 로고
    • Receptor-selective variants of human vascular endothelial growth factor. Generation and characterization
    • Li, B. et al. Receptor-selective variants of human vascular endothelial growth factor. Generation and characterization, J. Biol. Chem. 275, 29823-29828 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 29823-29828
    • Li, B.1
  • 29
    • 0035447687 scopus 로고    scopus 로고
    • Direct identification of a major autophosphorylation site on vascular endothelial growth factor receptor Flt-1 that mediates phosphatidylinositol 3′-kinase binding
    • Yu, Y. et al. Direct identification of a major autophosphorylation site on vascular endothelial growth factor receptor Flt-1 that mediates phosphatidylinositol 3′-kinase binding. Biochem. J. 358, 465-472 (2001).
    • (2001) Biochem. J. , vol.358 , pp. 465-472
    • Yu, Y.1
  • 30
    • 0032495978 scopus 로고    scopus 로고
    • Tyrosine 1213 of Flt-1 is a major binding site of Nck and SHP-2
    • Igarashi, K. et al. Tyrosine 1213 of Flt-1 is a major binding site of Nck and SHP-2. Biochem. Biophys. Res. Commun. 246, 95-99 (1998).
    • (1998) Biochem. Biophys. Res. Commun. , vol.246 , pp. 95-99
    • Igarashi, K.1
  • 31
    • 0032483374 scopus 로고    scopus 로고
    • Identification of vascular endothelial growth factor receptor-1 tyrosine phosphorylation sites and binding of SH2 domain-containing molecules
    • Ito, N., Wernstedt, C., Engstrom, U. & Claesson-Welsh, L. Identification of vascular endothelial growth factor receptor-1 tyrosine phosphorylation sites and binding of SH2 domain-containing molecules. J. Biol. Chem. 273, 23410-23418 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 23410-23418
    • Ito, N.1    Wernstedt, C.2    Engstrom, U.3    Claesson-Welsh, L.4
  • 32
    • 0034802915 scopus 로고    scopus 로고
    • Signal transduction by VEGF receptor-1 wild type and mutant proteins
    • Ito, N., Huang, K. & Claesson-Weish, L. Signal transduction by VEGF receptor-1 wild type and mutant proteins. Cell Signal. 13, 849-854 (2001).
    • (2001) Cell Signal. , vol.13 , pp. 849-854
    • Ito, N.1    Huang, K.2    Claesson-Weish, L.3
  • 33
    • 0032826035 scopus 로고    scopus 로고
    • Inhibition of plasminogen activators or matrix metalloproteinases prevents cardiac rupture but impairs therapeutic angiogenesis and causes cardiac failure
    • Heymans, S. et al. Inhibition of plasminogen activators or matrix metalloproteinases prevents cardiac rupture but impairs therapeutic angiogenesis and causes cardiac failure. Nat. Med. 5, 1135-1142 (1999).
    • (1999) Nat. Med. , vol.5 , pp. 1135-1142
    • Heymans, S.1
  • 34
    • 0037127297 scopus 로고    scopus 로고
    • Rapid transactivation of the vascular endothelial growth factor receptor KDR/Flk-1 by the bradykinin B2 receptor contributes to endothelial nitric-oxide synthase activation in cardiac capillary endothelial cells
    • Thuringer, D., Maulon, L. & Frelin, C. Rapid transactivation of the vascular endothelial growth factor receptor KDR/Flk-1 by the bradykinin B2 receptor contributes to endothelial nitric-oxide synthase activation in cardiac capillary endothelial cells. J. Biol. Chem. 277, 2028-2032 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 2028-2032
    • Thuringer, D.1    Maulon, L.2    Frelin, C.3
  • 35
    • 0036371753 scopus 로고    scopus 로고
    • Integration of signals from receptor tyrosine kinases and G protein-coupled receptors
    • Lowes, V.L., Ip, N.Y. & Wong, Y.H. Integration of signals from receptor tyrosine kinases and G protein-coupled receptors. Neurosignals 11, 5-19 (2002).
    • (2002) Neurosignals , vol.11 , pp. 5-19
    • Lowes, V.L.1    Ip, N.Y.2    Wong, Y.H.3
  • 36
    • 0036838172 scopus 로고    scopus 로고
    • Interplay between integrins and FLK-1 in shear stress-induced signaling
    • Wang, Y. et al. Interplay between integrins and FLK-1 in shear stress-induced signaling. Am. J. Physiol. Cell. Physiol. 283, C1540-C1547 (2002).
    • (2002) Am. J. Physiol. Cell. Physiol. , vol.283
    • Wang, Y.1
  • 37
    • 0034213668 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of the vascular endothelial-growth-factor receptor-2 (VEGFR-2) is modulated by Rho proteins
    • Gingras, D., Lamy, S. & Beliveau, R. Tyrosine phosphorylation of the vascular endothelial-growth-factor receptor-2 (VEGFR-2) is modulated by Rho proteins. Biochem. J. 348, 273-280 (2000).
    • (2000) Biochem. J. , vol.348 , pp. 273-280
    • Gingras, D.1    Lamy, S.2    Beliveau, R.3
  • 38
    • 0343920277 scopus 로고    scopus 로고
    • Abnormal blood vessel development and lethality in embryos lacking a single VEGF allele
    • Carmeliet, P. et al. Abnormal blood vessel development and lethality in embryos lacking a single VEGF allele. Nature 380, 435-439 (1996).
    • (1996) Nature , vol.380 , pp. 435-439
    • Carmeliet, P.1
  • 39
    • 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 Flt-1 required for binding and structural stability
    • Davis-Smyth, T., Presta, L.G. & Ferrara, N. Mapping the charged residues in the second immunoglobulin-like domain of the vascular endothelial growth factor/placenta growth factor receptor Flt-1 required for binding and structural stability. J. Biol. Chem. 273, 3216-3222 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 3216-3222
    • Davis-Smyth, T.1    Presta, L.G.2    Ferrara, N.3
  • 40
    • 0013683165 scopus 로고    scopus 로고
    • Interactions of FLT-1 and KDR with phospholipase C gamma: Identification of the phosphotyrosine binding sites
    • Cunningham, S.A., Arrate, M.P., Brock, T.A. & Waxham, M.N. Interactions of FLT-1 and KDR with phospholipase C gamma: identification of the phosphotyrosine binding sites. Biochem. Biophys. Res. Commun. 240, 635-639 (1997).
    • (1997) Biochem. Biophys. Res. Commun. , vol.240 , pp. 635-639
    • Cunningham, S.A.1    Arrate, M.P.2    Brock, T.A.3    Waxham, M.N.4
  • 41
    • 0027403027 scopus 로고
    • SH2 domains recognize specific phosphopeptide sequences
    • Songyang, Z. et al. SH2 domains recognize specific phosphopeptide sequences. Cell 72, 767-778 (1993).
    • (1993) Cell , vol.72 , pp. 767-778
    • Songyang, Z.1
  • 42
    • 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. et al. Crystal structure at 1.7 A resolution of VEGF in complex with domain 2 of the Flt-1 receptor. Cell 91, 695-704 (1997).
    • (1997) Cell , vol.91 , pp. 695-704
    • Wiesmann, C.1
  • 43
    • 0035853679 scopus 로고    scopus 로고
    • The crystal structure of human placenta growth factor-1 (PGF-1), an angiogenic protein, at 2.0 A resolution
    • Iyer, S. et al. The crystal structure of human placenta growth factor-1 (PGF-1), an angiogenic protein, at 2.0 A resolution. J. Biol. Chem. 276, 12153-12161 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 12153-12161
    • Iyer, S.1
  • 44
    • 0032556950 scopus 로고    scopus 로고
    • Placenta growth factor stimulates MAP kinase and mitogenicity but not phospholipase C-gamma and migration of endothelial cells expressing Flt 1
    • Landgren, E., Schiller, P., Cao, Y. & Claesson-Welsh, L. Placenta growth factor stimulates MAP kinase and mitogenicity but not phospholipase C-gamma and migration of endothelial cells expressing Flt 1. Oncogene 16, 359-367 (1998).
    • (1998) Oncogene , vol.16 , pp. 359-367
    • Landgren, E.1    Schiller, P.2    Cao, Y.3    Claesson-Welsh, L.4
  • 45
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • Shevchenko, A., Wilm, M., Vorm, O. & Mann, M. Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal. Chem. 68, 850-858 (1996).
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 46
    • 0036281003 scopus 로고    scopus 로고
    • RNA amplification results in reproducible microarray data with slight ratio bias
    • Puskas, L.G., Zvara, A., Hackler, L., Jr. & Van Hummelen, P. RNA amplification results in reproducible microarray data with slight ratio bias, Biotechniques 32, 1330-1334 (2002).
    • (2002) Biotechniques , vol.32 , pp. 1330-1334
    • Puskas, L.G.1    Zvara, A.2    Hackler L., Jr.3    Van Hummelen, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.