메뉴 건너뛰기




Volumn 90, Issue 9, 1997, Pages 3507-3515

Signal transduction in human hematopoietic cells by vascular endothelial growth factor related protein, a novel ligand for the FLT4 receptor

Author keywords

[No Author keywords available]

Indexed keywords

CYTOSKELETON PROTEIN; FOCAL ADHESION KINASE; HYBRID PROTEIN; LIGAND; PHOSPHOTRANSFERASE; PROTEIN TYROSINE KINASE; RECEPTOR; STEM CELL FACTOR; TYROSINE; VASCULOTROPIN;

EID: 0030783595     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood.v90.9.3507     Document Type: Article
Times cited : (22)

References (45)
  • 1
    • 0028842903 scopus 로고
    • Role of VEGF-flt receptor system in normal and tumor angiogenesis
    • Shibuya M: Role of VEGF-flt receptor system in normal and tumor angiogenesis. Adv Cancer Res 67:281, 1995
    • (1995) Adv Cancer Res , vol.67 , pp. 281
    • Shibuya, M.1
  • 2
    • 0029021904 scopus 로고
    • Endothelial receptor tyrosine kinases involved in angiogenesis
    • Mustonen T, Alitalo K: Endothelial receptor tyrosine kinases involved in angiogenesis. J Cell Biol 129:895, 1995
    • (1995) J Cell Biol , vol.129 , pp. 895
    • Mustonen, T.1    Alitalo, K.2
  • 3
    • 0028872649 scopus 로고
    • Specificity of receptor tyrosine kinase signaling: Transient versus sustained extracellular signal-regulated kinase activation
    • Marshall CJ: Specificity of receptor tyrosine kinase signaling: Transient versus sustained extracellular signal-regulated kinase activation. Cell 80:179, 1995
    • (1995) Cell , vol.80 , pp. 179
    • Marshall, C.J.1
  • 5
    • 0027249239 scopus 로고
    • Fetal liver kinase 1 is a receptor for vascular endothelial growth factor and is selectively expressed in vascular endothelium
    • Quinn TP, Peters KG, de Vries C, Ferrara N, Williams LT: Fetal liver kinase 1 is a receptor for vascular endothelial growth factor and is selectively expressed in vascular endothelium. Proc Natl Acad Sci USA 90:7533, 1993
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 7533
    • Quinn, T.P.1    Peters, K.G.2    De Vries, C.3    Ferrara, N.4    Williams, L.T.5
  • 6
    • 0027466849 scopus 로고
    • High affinity VEGF binding and developmental expression suggest Flk-1 as a major regulator of vasculogenesis and angiogenesis
    • Millauer B, Wizigmann-Voos S, Schnurch H, Martinez R, Moller NP, Risau W, Ullrich A: High affinity VEGF binding and developmental expression suggest Flk-1 as a major regulator of vasculogenesis and angiogenesis. Cell 72:835, 1993
    • (1993) Cell , vol.72 , pp. 835
    • Millauer, B.1    Wizigmann-Voos, S.2    Schnurch, H.3    Martinez, R.4    Moller, N.P.5    Risau, W.6    Ullrich, A.7
  • 7
    • 0025998533 scopus 로고
    • A receptor tyrosine kinase cDNA isolated from a population of enriched primitive hematopoietic cells and exhibiting close genetic linkage to c-kit
    • Matthews W, Jordan CT, Gavin M, Jenkins NA, Copeland NG, Lemischka IR: A receptor tyrosine kinase cDNA isolated from a population of enriched primitive hematopoietic cells and exhibiting close genetic linkage to c-kit. Proc Natl Acad Sci USA 88:9026, 1991
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 9026
    • Matthews, W.1    Jordan, C.T.2    Gavin, M.3    Jenkins, N.A.4    Copeland, N.G.5    Lemischka, I.R.6
  • 10
    • 0027380823 scopus 로고
    • Two human FLT4 receptor tyrosine kinase isoforms with distinct carboxy terminal tails are produced by alternative processing of primary transcripts
    • Pajusola K, Aprelikova O, Armstrong E, Morris S, Alitalo K: Two human FLT4 receptor tyrosine kinase isoforms with distinct carboxy terminal tails are produced by alternative processing of primary transcripts. Oncogene 8:2931, 1993
    • (1993) Oncogene , vol.8 , pp. 2931
    • Pajusola, K.1    Aprelikova, O.2    Armstrong, E.3    Morris, S.4    Alitalo, K.5
  • 11
    • 0026699255 scopus 로고
    • FLT4 receptor tyrosine kinase contains seven immunoglobulin-like loops and is expressed in multiple human tissues and cell lines
    • Pajusola K, Aprelikova O, Korhonen J, Kaipainen A, Pertovaara L, Alitalo R, Alitalo K: FLT4 receptor tyrosine kinase contains seven immunoglobulin-like loops and is expressed in multiple human tissues and cell lines. Cancer Res 52:5738, 1992
    • (1992) Cancer Res , vol.52 , pp. 5738
    • Pajusola, K.1    Aprelikova, O.2    Korhonen, J.3    Kaipainen, A.4    Pertovaara, L.5    Alitalo, R.6    Alitalo, K.7
  • 12
    • 0028940091 scopus 로고
    • Biochemical characterization of two isoforms of FLT4, a VEGF receptor-related tyrosine kinase
    • Borg JP, deLapeyriere O, Noguchi T, Rottapel R, Dubreuil P, Birnbaum D: Biochemical characterization of two isoforms of FLT4, a VEGF receptor-related tyrosine kinase. Oncogene 10:973, 1995
    • (1995) Oncogene , vol.10 , pp. 973
    • Borg, J.P.1    DeLapeyriere, O.2    Noguchi, T.3    Rottapel, R.4    Dubreuil, P.5    Birnbaum, D.6
  • 13
    • 0029079943 scopus 로고
    • Mutation at tyrosine residue 1337 abrogates ligand-dependent transforming capacity of the FLT4 receptor
    • Fournier E, Dubreuil P, Birnbaum D, Borg JP: Mutation at tyrosine residue 1337 abrogates ligand-dependent transforming capacity of the FLT4 receptor. Oncogene 11:921, 1995
    • (1995) Oncogene , vol.11 , pp. 921
    • Fournier, E.1    Dubreuil, P.2    Birnbaum, D.3    Borg, J.P.4
  • 14
    • 17544375224 scopus 로고    scopus 로고
    • Interaction with the phosphotyrosine binding domain/phosphotyrosine interacting domain of SHC is required for the transforming activity of the FLT4/VEGFR3 receptor tyrosine kinase
    • Fournier E, Rosnet O, Marchetto S, Turck CW, Rottapel R, Pelicci PG, Birnbaum D, Borg JP: Interaction with the phosphotyrosine binding domain/phosphotyrosine interacting domain of SHC is required for the transforming activity of the FLT4/VEGFR3 receptor tyrosine kinase. J Biol Chem 271:12956, 1996
    • (1996) J Biol Chem , vol.271 , pp. 12956
    • Fournier, E.1    Rosnet, O.2    Marchetto, S.3    Turck, C.W.4    Rottapel, R.5    Pelicci, P.G.6    Birnbaum, D.7    Borg, J.P.8
  • 15
    • 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, .Alitalo K: Signalling properties of FLT4, a proteolytically processed receptor tyrosine kinase related to two VEGF receptors. Oncogene 9:3545, 1994
    • (1994) Oncogene , vol.9 , pp. 3545
    • Pajusola, K.1    Aprelikova, O.2    Pelicci, G.3    Weich, H.4    Claesson-Welsh, L.5    Alitalo, K.6
  • 17
    • 0029664716 scopus 로고    scopus 로고
    • Coexpression of flt-1, flt-4 and KDR in freshly isolated and cultured human endothelial cells
    • Hewett PW, Murray JC: Coexpression of flt-1, flt-4 and KDR in freshly isolated and cultured human endothelial cells. Biochem Biophys Res Com 221:697, 1996
    • (1996) Biochem Biophys Res Com , vol.221 , pp. 697
    • Hewett, P.W.1    Murray, J.C.2
  • 18
    • 0029962242 scopus 로고    scopus 로고
    • Vascular endothelial growth factor-related protein: A ligand and specific activator of the tyrosine kinase receptor Flt4
    • Lee J, Gray A, Yuan J, Luoh S, Avraham H, Wood WI: Vascular endothelial growth factor-related protein: A ligand and specific activator of the tyrosine kinase receptor Flt4. Proc Natl Acad Sci USA 93:1988, 1996
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 1988
    • Lee, J.1    Gray, A.2    Yuan, J.3    Luoh, S.4    Avraham, H.5    Wood, W.I.6
  • 19
    • 0030118083 scopus 로고    scopus 로고
    • A novel vascular endothelial growth factor, VEGF-C, is a ligand for the Flt4 (VEGFR-3) and KDR (VEGFR-2) receptor tyrosine kinases
    • Joukov V, Pajusola K, Kaipainen A, Chilov D, Lahtinen I, Kukk E, Saksela O, Kalkkinen N, Alitalo K: A novel vascular endothelial growth factor, VEGF-C, is a ligand for the Flt4 (VEGFR-3) and KDR (VEGFR-2) receptor tyrosine kinases. EMBO J 15:290, 1996
    • (1996) EMBO J , vol.15 , pp. 290
    • Joukov, V.1    Pajusola, K.2    Kaipainen, A.3    Chilov, D.4    Lahtinen, I.5    Kukk, E.6    Saksela, O.7    Kalkkinen, N.8    Alitalo, K.9
  • 21
    • 0029096541 scopus 로고
    • Cloning and characterization of cell adhesion kinase beta, a novel protein-tyrosine kinase of the focal adhesion kinase subfamily
    • Sasaki H, Nagura K, Ishino M, Tobioka H, Kotani K, Sasaki T: Cloning and characterization of cell adhesion kinase beta, a novel protein-tyrosine kinase of the focal adhesion kinase subfamily. J Biol Chem 270:21206, 1995
    • (1995) J Biol Chem , vol.270 , pp. 21206
    • Sasaki, H.1    Nagura, K.2    Ishino, M.3    Tobioka, H.4    Kotani, K.5    Sasaki, T.6
  • 23
    • 0029978533 scopus 로고    scopus 로고
    • Characterization of RAFTK, a novel focal adhesion kinase, and its integrin-dependent phosphorylation and activation in megakarypcytes
    • Li J, Avraham H, Rogers RA, Raja S, Avraham SA: Characterization of RAFTK, a novel focal adhesion kinase, and its integrin-dependent phosphorylation and activation in megakarypcytes. Blood 88:417, 1996
    • (1996) Blood , vol.88 , pp. 417
    • Li, J.1    Avraham, H.2    Rogers, R.A.3    Raja, S.4    Avraham, S.A.5
  • 27
    • 0029770721 scopus 로고    scopus 로고
    • Activation of Pyk2 by stress signals and coupling with JNK signaling pathway
    • Tokiwa G, Dikic I, Lev S, Schlessinger J: Activation of Pyk2 by stress signals and coupling with JNK signaling pathway. Science 273:792, 1996
    • (1996) Science , vol.273 , pp. 792
    • Tokiwa, G.1    Dikic, I.2    Lev, S.3    Schlessinger, J.4
  • 28
    • 0031025122 scopus 로고    scopus 로고
    • The related adhesion focal tyrosine kinase (RAFTK) is tyrosine phosphorylated after β1 integrin stimulation in B cells and binds to p130cas
    • Astier A, Avraham H, Manie SN, Groopman JE, Canty T, Avraham S, Freedman AS: The related adhesion focal tyrosine kinase (RAFTK) is tyrosine phosphorylated after β1 integrin stimulation in B cells and binds to p130cas. J Biol Chem 272:228, 1997
    • (1997) J Biol Chem , vol.272 , pp. 228
    • Astier, A.1    Avraham, H.2    Manie, S.N.3    Groopman, J.E.4    Canty, T.5    Avraham, S.6    Freedman, A.S.7
  • 29
    • 0028329953 scopus 로고
    • JNK1: A protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain
    • Derijard B, Hibi M, Wu IH, Barrett T, Su B, Deng T, Karin M, Davis RJ: JNK1: A protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain. Cell 76:1025, 1994
    • (1994) Cell , vol.76 , pp. 1025
    • Derijard, B.1    Hibi, M.2    Wu, I.H.3    Barrett, T.4    Su, B.5    Deng, T.6    Karin, M.7    Davis, R.J.8
  • 30
    • 0027423418 scopus 로고
    • Identification of an oncoprotein- And UV-responsive protein kinase that binds and potentiates the c-Jun activation domain
    • Hibi M, Lin A, Smeal T, Minden A, Karin M: Identification of an oncoprotein- and UV-responsive protein kinase that binds and potentiates the c-Jun activation domain. Genes Dev 7:2135, 1993
    • (1993) Genes Dev , vol.7 , pp. 2135
    • Hibi, M.1    Lin, A.2    Smeal, T.3    Minden, A.4    Karin, M.5
  • 31
    • 0027165150 scopus 로고
    • The mitogen-activated protein kinase signal transduction pathway
    • Davis RJ: The mitogen-activated protein kinase signal transduction pathway. J Biol Chem 268:14553, 1993
    • (1993) J Biol Chem , vol.268 , pp. 14553
    • Davis, R.J.1
  • 33
    • 0028609382 scopus 로고
    • Integrin-mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase
    • Schlaepfer DD, Hanks SK, Hunter T, van der Geer P: Integrin-mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase. Nature 372:786, 1994
    • (1994) Nature , vol.372 , pp. 786
    • Schlaepfer, D.D.1    Hanks, S.K.2    Hunter, T.3    Van Der Geer, P.4
  • 34
    • 0028987936 scopus 로고
    • Integrins and signal transduction pathways: The road taken
    • Clark EA, Brugge JS: Integrins and signal transduction pathways: The road taken. Science 268:233, 1995
    • (1995) Science , vol.268 , pp. 233
    • Clark, E.A.1    Brugge, J.S.2
  • 35
    • 0024382542 scopus 로고
    • Novel tyrosine kinase substrates from Rous sarcoma virus-transformed cells are present in the membrane skeleton
    • Glenney JR Jr, Zokas L: Novel tyrosine kinase substrates from Rous sarcoma virus-transformed cells are present in the membrane skeleton. J Cell Biol 108:2401, 1989
    • (1989) J Cell Biol , vol.108 , pp. 2401
    • Glenney Jr., J.R.1    Zokas, L.2
  • 37
    • 0028289562 scopus 로고
    • Primary sequence of paxillin contains putative SH2 and SH3 domain binding motifs and multiple LIM domains: Identification of a vinculin and pp125Fak-binding region
    • Turner CE, Miller JT: Primary sequence of paxillin contains putative SH2 and SH3 domain binding motifs and multiple LIM domains: Identification of a vinculin and pp125Fak-binding region. J Cell Sci 107:1583, 1994
    • (1994) J Cell Sci , vol.107 , pp. 1583
    • Turner, C.E.1    Miller, J.T.2
  • 40
    • 0029907265 scopus 로고    scopus 로고
    • A role for Pyk2 and Src in linking G-protein-coupled receptors with MAP kinase activation
    • Dikic I, Tokiwa G, Lev S, Courtneidge SA, Schlessinger J: A role for Pyk2 and Src in linking G-protein-coupled receptors with MAP kinase activation. Nature 383:547, 1996
    • (1996) Nature , vol.383 , pp. 547
    • Dikic, I.1    Tokiwa, G.2    Lev, S.3    Courtneidge, S.A.4    Schlessinger, J.5
  • 41
    • 0029032249 scopus 로고
    • The regulation of AP-1 activation by mitogen-activated protein kinases
    • Karin M: The regulation of AP-1 activation by mitogen-activated protein kinases. J Biol Chem 270:16483, 1995
    • (1995) J Biol Chem , vol.270 , pp. 16483
    • Karin, M.1
  • 42
    • 0028291525 scopus 로고
    • JNK is involved in signal integration during costimulation of T lymphocytes
    • Su B, Jacinto E, Hibi M, Kallunki T, Karin M, Ben-Neriah Y: JNK is involved in signal integration during costimulation of T lymphocytes. Cell 77:727, 1994
    • (1994) Cell , vol.77 , pp. 727
    • Su, B.1    Jacinto, E.2    Hibi, M.3    Kallunki, T.4    Karin, M.5    Ben-Neriah, Y.6
  • 43
    • 0030945261 scopus 로고    scopus 로고
    • Activation of JNK signaling pathway by erythropoietin, thrombopoietin and interleukin-3
    • Nagata Y, Nishida E, Todokoro K: Activation of JNK signaling pathway by erythropoietin, thrombopoietin and interleukin-3. Blood 89:2664, 1997
    • (1997) Blood , vol.89 , pp. 2664
    • Nagata, Y.1    Nishida, E.2    Todokoro, K.3
  • 44
    • 0028875460 scopus 로고
    • Increased tyrosine phosphorylation of focal adhesion proteins in myeloid cell lines expressing p210BCR/ABL
    • Salgia R, Brunkhorst B, Pisick E, Li JL, Lo SH, Chen LB, Griffin JD: Increased tyrosine phosphorylation of focal adhesion proteins in myeloid cell lines expressing p210BCR/ABL. Oncogene 11:1149, 1995
    • (1995) Oncogene , vol.11 , pp. 1149
    • Salgia, R.1    Brunkhorst, B.2    Pisick, E.3    Li, J.L.4    Lo, S.H.5    Chen, L.B.6    Griffin, J.D.7
  • 45
    • 0028986116 scopus 로고
    • FAK dependent tyrosine phosphorylation of paxillin creates a high-affinity binding site for Crk
    • FAK dependent tyrosine phosphorylation of paxillin creates a high-affinity binding site for Crk. Mol Cell Biol 15:2635, 1995
    • (1995) Mol Cell Biol , vol.15 , pp. 2635
    • Schaller, M.D.1    Parsons, J.T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.