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Volumn 93, Issue 4, 2005, Pages 641-646

The urokinase receptor and the regulation of cell proliferation

Author keywords

Metastasis; Proliferation; Tumors; Urokinase receptor

Indexed keywords

CAVEOLIN; EPIDERMAL GROWTH FACTOR RECEPTOR; FIBROBLAST GROWTH FACTOR; FOCAL ADHESION KINASE; G PROTEIN COUPLED RECEPTOR; GELATINASE A; GELATINASE B; GUANOSINE TRIPHOSPHATASE; INTEGRIN; INTERSTITIAL COLLAGENASE; JANUS KINASE; MITOGEN ACTIVATED PROTEIN KINASE; PLASMIN; PLASMINOGEN ACTIVATOR INHIBITOR; PROTEIN P130; PROTEIN P16INK4A; PROTEIN P19; PROTEIN SERINE THREONINE KINASE; PROTEIN TYROSINE KINASE; SCATTER FACTOR; SOMATOMEDIN BINDING PROTEIN; STAT PROTEIN; TISSUE PLASMINOGEN ACTIVATOR; TRANSFORMING GROWTH FACTOR BETA; UROKINASE; UROKINASE RECEPTOR; VITRONECTIN;

EID: 16844385164     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: 10.1160/TH05-01-0021     Document Type: Article
Times cited : (37)

References (87)
  • 1
    • 0021984227 scopus 로고
    • A cellular binding site for the Mr 55,000 form of the human plasminogen activator, urokinase
    • Vassalli J-D, Baccino D, Belin D. A cellular binding site for the Mr 55,000 form of the human plasminogen activator, urokinase. J Cell Biol 1985; 100: 8-92.
    • (1985) J. Cell Biol. , vol.100 , pp. 8-92
    • Vassalli, J.-D.1    Baccino, D.2    Belin, D.3
  • 2
    • 0001149917 scopus 로고
    • Differentiation-enhanced binding of the amino terminal fragment of human urokinase plasminogen activator to a specific receptor on U937 monocytes
    • Stoppelli MP, Corti A, Soffientini A, et al. Differentiation-enhanced binding of the amino terminal fragment of human urokinase plasminogen activator to a specific receptor on U937 monocytes. Proc Natl Acad Sci U S A 1985; 82: 4939-43.
    • (1985) Proc. Natl. Acad. Sci. U. S. A. , vol.82 , pp. 4939-4943
    • Stoppelli, M.P.1    Corti, A.2    Soffientini, A.3
  • 3
    • 0026063532 scopus 로고
    • Cellular receptor for urokinase plasminogen activator. Carboxyl-terminal processing and membrane anchoring by glycosyl-phosphatidylinositol
    • Ploug M, Rønne E., Behrendt N., et al. Cellular receptor for urokinase plasminogen activator. Carboxyl-terminal processing and membrane anchoring by glycosyl-phosphatidylinositol. J Biol Chem 1991; 266: 1926-33.
    • (1991) J. Biol. Chem. , vol.266 , pp. 1926-1933
    • Ploug, M.1    Rønne, E.2    Behrendt, N.3
  • 4
    • 0037967310 scopus 로고    scopus 로고
    • Structure-function relationships in the interaction between the urokinase-type plasminogen activator and its receptor
    • Ploug, M. Structure-function relationships in the interaction between the urokinase-type plasminogen activator and its receptor. Curr Pharm Des 2003; 9: 1499-528.
    • (2003) Curr. Pharm. Des. , vol.9 , pp. 1499-1528
    • Ploug, M.1
  • 5
    • 0032564309 scopus 로고    scopus 로고
    • Identification of specific sites involved in ligand binding by photoaffinity labeling of the receptor for the urokinase-type plasminogen activator. Residues located at equivalent positions in uPAR domains I and III participate in the assembly of a composite ligand-binding site
    • Ploug M. Identification of specific sites involved in ligand binding by photoaffinity labeling of the receptor for the urokinase-type plasminogen activator. Residues located at equivalent positions in uPAR domains I and III participate in the assembly of a composite ligand-binding site. Biochemistry 1998; 37: 16494-505.
    • (1998) Biochemistry , vol.37 , pp. 16494-16505
    • Ploug, M.1
  • 6
    • 0026644421 scopus 로고
    • Urokinase plasminogen activator cleaves its cell surface receptor releasing the ligand-binding domain
    • Høyer-Hansen G, Rønne E, Solberg H, et al. Urokinase plasminogen activator cleaves its cell surface receptor releasing the ligand-binding domain. J Biol Chem 1992; 267: 18224-9.
    • (1992) J. Biol. Chem. , vol.267 , pp. 18224-18229
    • Høyer-Hansen, G.1    Rønne, E.2    Solberg, H.3
  • 7
    • 0032520886 scopus 로고    scopus 로고
    • Differential expression of a truncated form of the urokinase-type plasminogen-activator receptor in normal and tumor thyroid cells
    • Ragno P, Montuori N, Covelli B, et al. Differential expression of a truncated form of the urokinase-type plasminogen-activator receptor in normal and tumor thyroid cells. Cancer Res 1998; 58: 1315-9.
    • (1998) Cancer Res. , vol.58 , pp. 1315-1319
    • Ragno, P.1    Montuori, N.2    Covelli, B.3
  • 8
    • 0036332150 scopus 로고    scopus 로고
    • Metalloproteases cleave the urokinase-type plasminogen activator receptor in the D1-D2 linker region and expose epitopes not present in the intact soluble receptor
    • Andolfo A, English WR, Resnati M, et al. Metalloproteases cleave the urokinase-type plasminogen activator receptor in the D1-D2 linker region and expose epitopes not present in the intact soluble receptor. Thromb Haemost. 2002; 88: 298-306.
    • (2002) Thromb. Haemost. , vol.88 , pp. 298-306
    • Andolfo, A.1    English, W.R.2    Resnati, M.3
  • 9
    • 0034625509 scopus 로고    scopus 로고
    • Shedding and cleavage of the urokinase receptor (uPAR): Identification and characterisation of uPAR fragments in vitro and in vivo
    • Sidenius N, Sier CF, Blasi F. Shedding and cleavage of the urokinase receptor (uPAR): identification and characterisation of uPAR fragments in vitro and in vivo. FEBS Lett 2000; 475: 52-6.
    • (2000) FEBS Lett. , vol.475 , pp. 52-56
    • Sidenius, N.1    Sier, C.F.2    Blasi, F.3
  • 10
    • 0035874516 scopus 로고    scopus 로고
    • Proteolysis of the urokinase-type plasminogen activator receptor by metalloproteinase-12: Implication for angiogenesis in fibrin matrices
    • Koolwijk P, Sidenius N, Peters E, et al. Proteolysis of the urokinase-type plasminogen activator receptor by metalloproteinase-12: implication for angiogenesis in fibrin matrices. Blood 2001; 97: 3123-31.
    • (2001) Blood , vol.97 , pp. 3123-3131
    • Koolwijk, P.1    Sidenius, N.2    Peters, E.3
  • 11
    • 4444317514 scopus 로고    scopus 로고
    • Plasmin cleaves the juxtamembrane domain and releases truncated species of the urokinase receptor (CD87) from human bronchial epithelial cells
    • Beaufort N, Leduc D, Rousselle JC, et al. Plasmin cleaves the juxtamembrane domain and releases truncated species of the urokinase receptor (CD87) from human bronchial epithelial cells. FEBS Lett 2004; 574: 89-94.
    • (2004) FEBS Lett. , vol.574 , pp. 89-94
    • Beaufort, N.1    Leduc, D.2    Rousselle, J.C.3
  • 12
    • 0029923744 scopus 로고    scopus 로고
    • Proteolytic cleavage of the urokinase receptor substitutes for the agonist-induced chemotactic effect
    • Resnati M, Guttinger M, Valcamonica S, et al. Proteolytic cleavage of the urokinase receptor substitutes for the agonist-induced chemotactic effect. EMBO J 1996; 15: 1572-82.
    • (1996) EMBO J. , vol.15 , pp. 1572-1582
    • Resnati, M.1    Guttinger, M.2    Valcamonica, S.3
  • 13
    • 0037022391 scopus 로고    scopus 로고
    • The fibrinolytic receptor for urokinase activates the G protein-coupled chemotactic receptor FPRL1/LXA4R
    • Resnati M, Pallavicini I, Wang JM, et al. The fibrinolytic receptor for urokinase activates the G protein-coupled chemotactic receptor FPRL1/LXA4R. Proc Natl Acad Sci U S A 2002; 99: 1359-64.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 1359-1364
    • Resnati, M.1    Pallavicini, I.2    Wang, J.M.3
  • 14
    • 0031463337 scopus 로고    scopus 로고
    • A urokinase-sensitive region of the human urokinase receptor is responsible for its chemotactic activity
    • Fazioli F, Resnati M, Sidenius N, et al. A urokinase-sensitive region of the human urokinase receptor is responsible for its chemotactic activity. EMBO J 1997; 16: 7279-86.
    • (1997) EMBO J. , vol.16 , pp. 7279-7286
    • Fazioli, F.1    Resnati, M.2    Sidenius, N.3
  • 16
    • 0037622867 scopus 로고    scopus 로고
    • The urokinase plasminogen activator receptor in the regulation of the actin cytoskeleton and cell motility
    • Kjøller L. The urokinase plasminogen activator receptor in the regulation of the actin cytoskeleton and cell motility. Biol Chem 2002; 383: 5-19.
    • (2002) Biol. Chem. , vol.383 , pp. 5-19
    • Kjøller, L.1
  • 17
    • 0028567891 scopus 로고
    • Expression of the receptor for urokinase-type plasminogen activator in normal and neoplastic blood cells and hematopoietic tissue
    • Plesner T, Ralfkiaer E, Wittrup M, et al. Expression of the receptor for urokinase-type plasminogen activator in normal and neoplastic blood cells and hematopoietic tissue. Am J Clin Pathol 1994; 102: 835-41.
    • (1994) Am. J. Clin. Pathol. , vol.102 , pp. 835-841
    • Plesner, T.1    Ralfkiaer, E.2    Wittrup, M.3
  • 18
    • 7844250487 scopus 로고    scopus 로고
    • Expression and functional role of urokinase-type plasminogen activator receptor in normal and acute leukaemic cells
    • Lanza F, Castoldi GL, Castagnari B, et al. Expression and functional role of urokinase-type plasminogen activator receptor in normal and acute leukaemic cells. Br J Haematol 1998; 103: 110-23.
    • (1998) Br. J. Haematol. , vol.103 , pp. 110-123
    • Lanza, F.1    Castoldi, G.L.2    Castagnari, B.3
  • 19
    • 0032910575 scopus 로고    scopus 로고
    • Blast cell-surface and plasma soluble urokinase receptor in acute leukemia patients: Relationship to classification and response to therapy
    • Mustjoki S, Alitalo R, Stephens RW, et al. Blast cell-surface and plasma soluble urokinase receptor in acute leukemia patients: relationship to classification and response to therapy. Thromb Haemost 1999; 81: 705-10.
    • (1999) Thromb. Haemost. , vol.81 , pp. 705-710
    • Mustjoki, S.1    Alitalo, R.2    Stephens, R.W.3
  • 20
    • 0033047130 scopus 로고    scopus 로고
    • Plasminogen activation in human leukemia and in normal hematopoietic cells
    • Mustjoki S, Alitalo R, Stephens RW, et al. Plasminogen activation in human leukemia and in normal hematopoietic cells. APMIS 1999; 107: 144-9.
    • (1999) APMIS , vol.107 , pp. 144-149
    • Mustjoki, S.1    Alitalo, R.2    Stephens, R.W.3
  • 21
    • 0030811592 scopus 로고    scopus 로고
    • Vitronectin binding to urokinase receptor in human breast cancer
    • Carriero MV, Del Vecchio S, Franco P, et al. Vitronectin binding to urokinase receptor in human breast cancer. Clin Cancer Res 1997; 3: 1299-308.
    • (1997) Clin. Cancer Res. , vol.3 , pp. 1299-1308
    • Carriero, M.V.1    Del Vecchio, S.2    Franco, P.3
  • 22
    • 0032578687 scopus 로고    scopus 로고
    • Cancer cells overexpress mRNA of urokinase-type plasminogen activator, its receptor and inhibitors in human non-small-cell lung cancer tissue: Analysis by Northern blotting and in situ hybridization
    • Morita S, Sato A, Hayakawa H, et al. Cancer cells overexpress mRNA of urokinase-type plasminogen activator, its receptor and inhibitors in human non-small-cell lung cancer tissue: analysis by Northern blotting and in situ hybridization. Int J Cancer 1998; 78: 286-92.
    • (1998) Int. J. Cancer , vol.78 , pp. 286-292
    • Morita, S.1    Sato, A.2    Hayakawa, H.3
  • 23
    • 0025853770 scopus 로고
    • Urokinase-type plasminogen activator is expressed in stromal cells and its receptor in cancer cells at invasive foci in human colon adenocarcinomas
    • Pyke C, Kristensen P, Ralfkiaer E, et al. Urokinase-type plasminogen activator is expressed in stromal cells and its receptor in cancer cells at invasive foci in human colon adenocarcinomas. Am J Pathol 1991; 138: 1059-67.
    • (1991) Am. J. Pathol. , vol.138 , pp. 1059-1067
    • Pyke, C.1    Kristensen, P.2    Ralfkiaer, E.3
  • 24
    • 0032524046 scopus 로고    scopus 로고
    • Expression of urokinase-type plasminogen activator (u-PA), u-PA receptor, and tissue-type PA messenger RNAs in human hepatocellular carcinoma
    • De Petro G, Tavian D, Copeta A, et al. Expression of urokinase-type plasminogen activator (u-PA), u-PA receptor, and tissue-type PA messenger RNAs in human hepatocellular carcinoma. Cancer Res 1998; 58: 2234-9.
    • (1998) Cancer Res. , vol.58 , pp. 2234-2239
    • De Petro, G.1    Tavian, D.2    Copeta, A.3
  • 25
    • 0032529230 scopus 로고    scopus 로고
    • A urokinase receptor mRNA binding protein-mRNA interaction regulates receptor expression and function in human pleural mesothelioma cells
    • Shetty S, Idell S. A urokinase receptor mRNA binding protein-mRNA interaction regulates receptor expression and function in human pleural mesothelioma cells. Arch Biochem Biophys 1998; 356: 265-79.
    • (1998) Arch. Biochem. Biophys. , vol.356 , pp. 265-279
    • Shetty, S.1    Idell, S.2
  • 26
    • 0032188909 scopus 로고    scopus 로고
    • Enhanced expression of urokinase receptor induced through the tissue factor-factor VIIa pathway in human pancreatic cancer
    • Taniguchi T, Kakkar AK, Tuddenham EG, et al. Enhanced expression of urokinase receptor induced through the tissue factor-factor VIIa pathway in human pancreatic cancer. Cancer Res 1998; 58: 4461-7.
    • (1998) Cancer Res. , vol.58 , pp. 4461-4467
    • Taniguchi, T.1    Kakkar, A.K.2    Tuddenham, E.G.3
  • 27
    • 0027959035 scopus 로고
    • Expression and localization of urokinase-type plasminogen activator receptor in human gliomas
    • Yamamoto M, Sawaya R, Mohanam S, et al. Expression and localization of urokinase-type plasminogen activator receptor in human gliomas. Cancer Res 1994; 54: 5016-20.
    • (1994) Cancer Res. , vol.54 , pp. 5016-5020
    • Yamamoto, M.1    Sawaya, R.2    Mohanam, S.3
  • 28
    • 0038364216 scopus 로고    scopus 로고
    • The urokinase plasminogen activator system in cancer: Recent advances and implication for prognosis and therapy
    • Sidenius N, Blasi F. The urokinase plasminogen activator system in cancer: recent advances and implication for prognosis and therapy. Cancer Metastasis Rev 2003; 22: 205-22.
    • (2003) Cancer Metastasis Rev. , vol.22 , pp. 205-222
    • Sidenius, N.1    Blasi, F.2
  • 29
    • 0035721955 scopus 로고    scopus 로고
    • Role of the matrix metalloproteinase and plasminogen activator-plasmin systems in angiogenesis
    • Pepper MS. Role of the matrix metalloproteinase and plasminogen activator-plasmin systems in angiogenesis. Arterioscler Thromb Vasc Biol 2001; 21: 1104-17.
    • (2001) Arterioscler. Thromb. Vasc. Biol. , vol.21 , pp. 1104-1117
    • Pepper, M.S.1
  • 30
    • 0034648765 scopus 로고    scopus 로고
    • Angiogenesis in cancer and other diseases
    • Carmeliet P, Jain RK. Angiogenesis in cancer and other diseases. Nature 2000; 407: 249-57.
    • (2000) Nature , vol.407 , pp. 249-257
    • Carmeliet, P.1    Jain, R.K.2
  • 31
    • 0035653288 scopus 로고    scopus 로고
    • Vessels of death or life
    • Jain RK, Carmeliet PF. Vessels of death or life. Sci Am 2001; 285: 38-45.
    • (2001) Sci. Am. , vol.285 , pp. 38-45
    • Jain, R.K.1    Carmeliet, P.F.2
  • 32
    • 0029993450 scopus 로고    scopus 로고
    • Role of the INK4a locus in tumor suppression and cell mortality
    • Serrano M, Lee H, Chin L, et al. Role of the INK4a locus in tumor suppression and cell mortality. Cell 1996; 85: 27-37.
    • (1996) Cell , vol.85 , pp. 27-37
    • Serrano, M.1    Lee, H.2    Chin, L.3
  • 33
    • 0036725322 scopus 로고    scopus 로고
    • Genome-wide retroviral insertional tagging of genes involved in cancer in Cdkn2a-deficient mice
    • Lund AH, Turner G, Trubetskoy A, et al. Genome-wide retroviral insertional tagging of genes involved in cancer in Cdkn2a-deficient mice. Nat Genet 2002; 32: 160-5.
    • (2002) Nat. Genet. , vol.32 , pp. 160-165
    • Lund, A.H.1    Turner, G.2    Trubetskoy, A.3
  • 34
    • 0033583761 scopus 로고    scopus 로고
    • Plasma urokinase receptor levels in patients with colorectal cancer: Relationship to prognosis
    • Stephens RW, Nielsen HJ, Christensen IJ, et al. Plasma urokinase receptor levels in patients with colorectal cancer: relationship to prognosis. J Natl Cancer Inst 1999; 91: 869-74.
    • (1999) J. Natl. Cancer Inst. , vol.91 , pp. 869-874
    • Stephens, R.W.1    Nielsen, H.J.2    Christensen, I.J.3
  • 35
    • 0028885643 scopus 로고
    • Individual development and uPA-receptor expression of disseminated tumour cells in bone marrow: A reference to early systemic disease in solid cancer
    • Heiss MM, Allgayer H, Gruetzner KU, et al. Individual development and uPA-receptor expression of disseminated tumour cells in bone marrow: a reference to early systemic disease in solid cancer. Nat Med 1995; 1: 1035-9.
    • (1995) Nat. Med. , vol.1 , pp. 1035-1039
    • Heiss, M.M.1    Allgayer, H.2    Gruetzner, K.U.3
  • 36
    • 0030984295 scopus 로고    scopus 로고
    • Urokinase plasminogen activator receptor (uPA-R): One potential characteristic of metastatic phenotypes in minimal residual tumor disease
    • Allgayer H, Heiss MM, Riesenberg R, et al. Urokinase plasminogen activator receptor (uPA-R): one potential characteristic of metastatic phenotypes in minimal residual tumor disease. Cancer Res 1997; 57: 1394-9.
    • (1997) Cancer Res. , vol.57 , pp. 1394-1399
    • Allgayer, H.1    Heiss, M.M.2    Riesenberg, R.3
  • 38
    • 0001453577 scopus 로고    scopus 로고
    • Urokinase receptor antagonists inhibit angiogenesis and primary tumor growth in syngeneic mice
    • Min HY, Doyle LV, Vitt CR, et al. Urokinase receptor antagonists inhibit angiogenesis and primary tumor growth in syngeneic mice. Cancer Res 1996; 56: 2428-33.
    • (1996) Cancer Res. , vol.56 , pp. 2428-2433
    • Min, H.Y.1    Doyle, L.V.2    Vitt, C.R.3
  • 39
    • 0034906667 scopus 로고    scopus 로고
    • Adenovirus-mediated antisense urokinase-type plasminogen activator receptor gene transfer reduces tumor cell invasion and metastasis in non-small cell lung cancer cell lines
    • Lakka SS, Rajagopal R, Rajan MK, et al. Adenovirus-mediated antisense urokinase-type plasminogen activator receptor gene transfer reduces tumor cell invasion and metastasis in non-small cell lung cancer cell lines. Clin Cancer Res 2001; 7: 1087-93.
    • (2001) Clin. Cancer Res. , vol.7 , pp. 1087-1093
    • Lakka, S.S.1    Rajagopal, R.2    Rajan, M.K.3
  • 40
    • 0035833983 scopus 로고    scopus 로고
    • Peptide-derived antagonists of the urokinase receptor. affinity maturation by combinatorial chemistry, identification of functional epitopes, and inhibitory effect on cancer cell intravasation
    • Ploug M, Ostergaard S, Gardsvoll H, et al. Peptide-derived antagonists of the urokinase receptor. affinity maturation by combinatorial chemistry, identification of functional epitopes, and inhibitory effect on cancer cell intravasation. Biochemistry 2001; 40: 12157-68.
    • (2001) Biochemistry , vol.40 , pp. 12157-12168
    • Ploug, M.1    Ostergaard, S.2    Gardsvoll, H.3
  • 41
    • 0031908852 scopus 로고    scopus 로고
    • Structure and biological activity of the extracellular matrix
    • Aumailley M, Gayraud B. Structure and biological activity of the extracellular matrix. J Mol Med 1998; 76: 253-65.
    • (1998) J. Mol. Med. , vol.76 , pp. 253-265
    • Aumailley, M.1    Gayraud, B.2
  • 42
    • 0038362684 scopus 로고    scopus 로고
    • Cell signaling events: A view from the matrix
    • Ramirez F, Rifkin DB. Cell signaling events: a view from the matrix. Matrix Biol 2003; 22: 101-7.
    • (2003) Matrix Biol. , vol.22 , pp. 101-107
    • Ramirez, F.1    Rifkin, D.B.2
  • 43
    • 0033848986 scopus 로고    scopus 로고
    • Matrix metalloproteinases effectors of development and normal physiology
    • Vu TH., Werb Z. Matrix metalloproteinases effectors of development and normal physiology. Genes Dev 2000; 14: 2123-33.
    • (2000) Genes Dev. , vol.14 , pp. 2123-2133
    • Vu, T.H.1    Werb, Z.2
  • 44
    • 0034650486 scopus 로고    scopus 로고
    • Cell surface-localized matrix metalloproteinase-9 proteolytically activates TGF-beta and promotes tumor invasion and angiogenesis
    • Yu Q, Stamenkovic I. Cell surface-localized matrix metalloproteinase-9 proteolytically activates TGF-beta and promotes tumor invasion and angiogenesis. Genes Dev 2000; 14: 163-76.
    • (2000) Genes Dev. , vol.14 , pp. 163-176
    • Yu, Q.1    Stamenkovic, I.2
  • 45
    • 0023916551 scopus 로고
    • Proteolytic activation of latent transforming growth factor-beta from fibroblast-conditioned medium
    • Lyons RM, Keski-Oja J, Moses HL. Proteolytic activation of latent transforming growth factor-beta from fibroblast-conditioned medium. J Cell Biol 1988; 106: 1659-65.
    • (1988) J. Cell Biol. , vol.106 , pp. 1659-1665
    • Lyons, R.M.1    Keski-Oja, J.2    Moses, H.L.3
  • 46
    • 0029876376 scopus 로고    scopus 로고
    • The degradation of human endothelial cell-derived perlecan and release of bound basic fibroblast growth factor by stromelysin, collagenase, plasmin, and heparanases
    • Whitelock JM, Murdoch AD, Iozzo RV et al. The degradation of human endothelial cell-derived perlecan and release of bound basic fibroblast growth factor by stromelysin, collagenase, plasmin, and heparanases. J Biol Chem 1996; 271: 10079-86.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10079-10086
    • Whitelock, J.M.1    Murdoch, A.D.2    Iozzo, R.V.3
  • 47
    • 0035188727 scopus 로고    scopus 로고
    • How matrix metalloproteinases regulate cell behavior
    • Sternlicht MD, Werb Z. How matrix metalloproteinases regulate cell behavior. Annu Rev Cell Dev Biol 2001; 17: 463-516.
    • (2001) Annu. Rev. Cell Dev. Biol. , vol.17 , pp. 463-516
    • Sternlicht, M.D.1    Werb, Z.2
  • 48
    • 0027077443 scopus 로고
    • Extracellular proteolytic cleavage by urokinase is required for activation of hepatocyte growth factor/scatter factor
    • Naldini L, Tamagnone L, Vigna E, et al. Extracellular proteolytic cleavage by urokinase is required for activation of hepatocyte growth factor/scatter factor. EMBO J 1992; 11: 4825-33.
    • (1992) EMBO J. , vol.11 , pp. 4825-4833
    • Naldini, L.1    Tamagnone, L.2    Vigna, E.3
  • 49
    • 0028912590 scopus 로고
    • Biological activation of pro-HGF (hepatocyte growth factor) by urokinase is controlled by a stoichiometric reaction
    • Naldini L, Vigna E, Bardelli A, et al. Biological activation of pro-HGF (hepatocyte growth factor) by urokinase is controlled by a stoichiometric reaction. J Biol Chem 1995; 270: 603-11.
    • (1995) J. Biol. Chem. , vol.270 , pp. 603-611
    • Naldini, L.1    Vigna, E.2    Bardelli, A.3
  • 50
    • 0027761342 scopus 로고
    • Activation of hepatocyte growth factor by the plasminogen activators uPA and tPA
    • Mars WM, Zarnegar R, Michalopoulos GK. Activation of hepatocyte growth factor by the plasminogen activators uPA and tPA. Am J Pathol 1993; 143: 949-58.
    • (1993) Am. J. Pathol. , vol.143 , pp. 949-958
    • Mars, W.M.1    Zarnegar, R.2    Michalopoulos, G.K.3
  • 51
    • 0025310993 scopus 로고
    • Characterization of the activation of latent TGF-β by co-cultures of endothelial cells and pericytes or smooth muscle cells: A self-regulating system
    • Sato Y, Tsuboi R, Lyons RM, et al. Characterization of the activation of latent TGF-β by co-cultures of endothelial cells and pericytes or smooth muscle cells: a self-regulating system. J Cell Biol 1990; 111: 757-63.
    • (1990) J. Cell Biol. , vol.111 , pp. 757-763
    • Sato, Y.1    Tsuboi, R.2    Lyons, R.M.3
  • 52
    • 0028984569 scopus 로고
    • Characterization of latent TGF-beta activation by murine peritoneal macrophages
    • Nunes I, Shapiro RL, Rifkin DB. Characterization of latent TGF-beta activation by murine peritoneal macrophages. J Immunol 1995; 155: 1450-9.
    • (1995) J. Immunol. , vol.155 , pp. 1450-1459
    • Nunes, I.1    Shapiro, R.L.2    Rifkin, D.B.3
  • 53
    • 0028268212 scopus 로고
    • Requirement for receptor-bound urokinase in plasmin-dependent cellular conversion of latent TGF-beta to TGF-beta
    • Odekon LE, Blasi F, Rifkin DB. Requirement for receptor-bound urokinase in plasmin-dependent cellular conversion of latent TGF-beta to TGF-beta. J Cell Physiol 1994; 158: 398-407.
    • (1994) J. Cell Physiol. , vol.158 , pp. 398-407
    • Odekon, L.E.1    Blasi, F.2    Rifkin, D.B.3
  • 54
    • 0006335227 scopus 로고    scopus 로고
    • Elevated serum levels of transforming growth factor-1 in patients with colorectal carcinoma: Its association with tumor progression and its significant decrease after curative surgical resection
    • Shim KS, Kim KH, Han WS, et al. Elevated serum levels of transforming growth factor-1 in patients with colorectal carcinoma: its association with tumor progression and its significant decrease after curative surgical resection. Cancer 1999; 85: 554-61.
    • (1999) Cancer , vol.85 , pp. 554-561
    • Shim, K.S.1    Kim, K.H.2    Han, W.S.3
  • 55
    • 0030598681 scopus 로고    scopus 로고
    • TGF-β1 inhibits the formation of benign skin tumors, but enhances progression to invasive spindle carcinomas in transgenic mice
    • Cui W, Fowlis DJ, Bryson S, et al. TGF-β1 inhibits the formation of benign skin tumors, but enhances progression to invasive spindle carcinomas in transgenic mice. Cell 1996; 86: 531-42.
    • (1996) Cell , vol.86 , pp. 531-542
    • Cui, W.1    Fowlis, D.J.2    Bryson, S.3
  • 56
    • 0033604556 scopus 로고    scopus 로고
    • Plasminogen-related growth factor and semaphorin receptors: A gene superfamily controlling invasive growth
    • Comoglio PM, Tamagnone L, Boccaccio C. Plasminogen-related growth factor and semaphorin receptors: a gene superfamily controlling invasive growth. Exp Cell Res 1999; 253: 88-99.
    • (1999) Exp. Cell Res. , vol.253 , pp. 88-99
    • Comoglio, P.M.1    Tamagnone, L.2    Boccaccio, C.3
  • 57
    • 0035031701 scopus 로고    scopus 로고
    • Hepatocyte growth factor/scatter factor is a motogen for interneurons migrating from the ventral to dorsal telencephalon
    • Powell EM, Mars WM, Levitt P. Hepatocyte growth factor/scatter factor is a motogen for interneurons migrating from the ventral to dorsal telencephalon. Neuron 2001; 30: 79-89.
    • (2001) Neuron , vol.30 , pp. 79-89
    • Powell, E.M.1    Mars, W.M.2    Levitt, P.3
  • 58
    • 0037439943 scopus 로고    scopus 로고
    • Genetic disruption of cortical interneuron development causes region- and GABA cell type-specific deficits, epilepsy, and behavioral dysfunction
    • Powell EM, Campbell DB, Stanwood GD, et al. Genetic disruption of cortical interneuron development causes region- and GABA cell type-specific deficits, epilepsy, and behavioral dysfunction. J Neurosci 2003; 23: 622-31.
    • (2003) J. Neurosci. , vol.23 , pp. 622-631
    • Powell, E.M.1    Campbell, D.B.2    Stanwood, G.D.3
  • 59
    • 0037686249 scopus 로고    scopus 로고
    • Activated c-Met signals through PI3K with dramatic effects on cytoskeletal functions in small cell lung cancer
    • Maulik G, Madhiwala P, Brooks S, et al. Activated c-Met signals through PI3K with dramatic effects on cytoskeletal functions in small cell lung cancer. J Cell Mol Med 2002; 6: 539-53.
    • (2002) J. Cell Mol. Med. , vol.6 , pp. 539-553
    • Maulik, G.1    Madhiwala, P.2    Brooks, S.3
  • 60
    • 0034282829 scopus 로고    scopus 로고
    • Urokinase-type plasminogen activator and its receptor synergize to promote pathogenic proteolysis
    • Zhou HM, Nichols A, Meda P, et al. Urokinase-type plasminogen activator and its receptor synergize to promote pathogenic proteolysis. EMBO J 2000; 19: 4817-26.
    • (2000) EMBO J. , vol.19 , pp. 4817-4826
    • Zhou, H.M.1    Nichols, A.2    Meda, P.3
  • 61
    • 2442714126 scopus 로고    scopus 로고
    • Plasminogen mediates the pathological effects of urokinase-type plasminogen activator overexpression
    • Bolon I, Zhou HM, Charron Y, et al. Plasminogen mediates the pathological effects of urokinase-type plasminogen activator overexpression. Am J Pathol 2004; 164: 2299-304.
    • (2004) Am. J. Pathol. , vol.164 , pp. 2299-2304
    • Bolon, I.1    Zhou, H.M.2    Charron, Y.3
  • 62
    • 0018160581 scopus 로고
    • Characteristics of chemically transformed mouse epidermal cells in vitro and in vivo
    • Fusenig NE, Amer SM, Boukamp P, et al. Characteristics of chemically transformed mouse epidermal cells in vitro and in vivo. Bull Cancer 1978; 65: 271-9.
    • (1978) Bull. Cancer , vol.65 , pp. 271-279
    • Fusenig, N.E.1    Amer, S.M.2    Boukamp, P.3
  • 63
    • 0030701960 scopus 로고    scopus 로고
    • Halting angiogenesis suppresses carcinoma cell invasion
    • Skobe M, Rockwell P, Goldstein N, et al. Halting angiogenesis suppresses carcinoma cell invasion. Nat Med 1997; 3: 1222-7.
    • (1997) Nat. Med. , vol.3 , pp. 1222-1227
    • Skobe, M.1    Rockwell, P.2    Goldstein, N.3
  • 64
    • 0031902286 scopus 로고    scopus 로고
    • Absence of host plasminogen activator inhibitor 1 prevents cancer invasion and vascularization
    • Bajou K, Noel A, Gerard RD, et al. Absence of host plasminogen activator inhibitor 1 prevents cancer invasion and vascularization. Nat Med 1998; 4: 923-8.
    • (1998) Nat. Med. , vol.4 , pp. 923-928
    • Bajou, K.1    Noel, A.2    Gerard, R.D.3
  • 65
    • 0035911151 scopus 로고    scopus 로고
    • The plasminogen activator inhibitor PAI-1 controls in vivo tumor vascularization by interaction with proteases, not vitronectin. Implications for antiangiogenic strategies
    • Bajou K, Masson V, Gerard RD, et al. The plasminogen activator inhibitor PAI-1 controls in vivo tumor vascularization by interaction with proteases, not vitronectin. Implications for antiangiogenic strategies. J Cell Biol 2001; 152: 777-84.
    • (2001) J. Cell Biol. , vol.152 , pp. 777-784
    • Bajou, K.1    Masson, V.2    Gerard, R.D.3
  • 66
    • 0023223148 scopus 로고
    • The receptor-binding sequence of urokinase. A biological function for the growth-factor module of proteases
    • Appella E, Robinson EA, Ullrich SJ, et al. The receptor-binding sequence of urokinase. A biological function for the growth-factor module of proteases. J Biol Chem 1987; 262: 4437-40.
    • (1987) J. Biol. Chem. , vol.262 , pp. 4437-4440
    • Appella, E.1    Robinson, E.A.2    Ullrich, S.J.3
  • 67
    • 0025543131 scopus 로고
    • An amino-terminal fragment of urokinase isolated from a prostate cancer cell line (PC-3) is mitogenic for osteoblast-like cells
    • Rabbani SA, Desjardins J, Bell AW, et al. An amino-terminal fragment of urokinase isolated from a prostate cancer cell line (PC-3) is mitogenic for osteoblast-like cells. Biochem Biophys Res Commun 1990; 173: 1058-64.
    • (1990) Biochem. Biophys. Res. Commun. , vol.173 , pp. 1058-1064
    • Rabbani, S.A.1    Desjardins, J.2    Bell, A.W.3
  • 68
    • 0026643491 scopus 로고
    • Structural requirements for the growth factor activity of the amino-terminal domain of urokinase
    • Rabbani SA, Mazar AP, Bernier SM, et al. Structural requirements for the growth factor activity of the amino-terminal domain of urokinase. J Biol Chem 1992; 267: 14151-6.
    • (1992) J. Biol. Chem. , vol.267 , pp. 14151-14156
    • Rabbani, S.A.1    Mazar, A.P.2    Bernier, S.M.3
  • 69
    • 0030855023 scopus 로고    scopus 로고
    • Induction in human osteoblastic cells (SaOS2) of the early response genes fos, jun, and myc by the amino terminal fragment (ATF) of urokinase
    • Rabbani SA, Gladu J, Mazar AP, et al. Induction in human osteoblastic cells (SaOS2) of the early response genes fos, jun, and myc by the amino terminal fragment (ATF) of urokinase. J Cell Physiol 1997; 172: 137-45.
    • (1997) J. Cell Physiol. , vol.172 , pp. 137-145
    • Rabbani, S.A.1    Gladu, J.2    Mazar, A.P.3
  • 70
    • 0033824172 scopus 로고    scopus 로고
    • Urokinase receptor and integrin partnership: Coordination of signaling for cell adhesion, migration and growth
    • Ossowski L, Aguirre-Ghiso JA. Urokinase receptor and integrin partnership: coordination of signaling for cell adhesion, migration and growth. Curr Opin Cell Biol 2000; 12: 613-20.
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 613-620
    • Ossowski, L.1    Aguirre-Ghiso, J.A.2
  • 71
    • 0037379794 scopus 로고    scopus 로고
    • ERK(MAPK) activity as a determinant of tumor growth and dormancy; regulation by p38(SAPK)
    • Aguirre-Ghiso JA, Estrada Y, Liu D, et al. ERK(MAPK) activity as a determinant of tumor growth and dormancy; regulation by p38(SAPK). Cancer Res 2003; 63: 1684-95.
    • (2003) Cancer Res. , vol.63 , pp. 1684-1695
    • Aguirre-Ghiso, J.A.1    Estrada, Y.2    Liu, D.3
  • 72
    • 0033590636 scopus 로고    scopus 로고
    • Constitutive activation of the 41-/43-kDa mitogen-activated protein kinase signaling pathway in human tumors
    • Hoshino R, Chatani Y, Yamori T, et al. Constitutive activation of the 41-/43-kDa mitogen-activated protein kinase signaling pathway in human tumors. Oncogene 1999; 18: 813-22.
    • (1999) Oncogene , vol.18 , pp. 813-822
    • Hoshino, R.1    Chatani, Y.2    Yamori, T.3
  • 73
    • 0034671847 scopus 로고    scopus 로고
    • The p38 pathway provides negative feedback for Ras proliferative signaling
    • Chen G, Hitomi M, Han J, et al. The p38 pathway provides negative feedback for Ras proliferative signaling. J Biol Chem 2000, 275: 38973-80.
    • (2000) J. Biol. Chem. , vol.275 , pp. 38973-38980
    • Chen, G.1    Hitomi, M.2    Han, J.3
  • 74
    • 0036596352 scopus 로고    scopus 로고
    • EGFR is a transducer of the urokinase receptor initiated signal that is required for in vivo growth of a human carcinoma
    • Liu D, Aguirre Ghiso J, Estrada Y, et al. EGFR is a transducer of the urokinase receptor initiated signal that is required for in vivo growth of a human carcinoma. Cancer Cell 2002; 1: 445-57.
    • (2002) Cancer Cell , vol.1 , pp. 445-457
    • Liu, D.1    Aguirre Ghiso, J.2    Estrada, Y.3
  • 75
    • 0035172910 scopus 로고    scopus 로고
    • Urokinase receptor and fibronectin regulate the ERK(MAPK) to p38(MAPK) activity ratios that determine carcinoma cell proliferation or dormancy in vivo
    • Aguirre-Ghiso JA, Liu D, Mignatti A, et al. Urokinase receptor and fibronectin regulate the ERK(MAPK) to p38(MAPK) activity ratios that determine carcinoma cell proliferation or dormancy in vivo. Mol Biol Cell 2001; 12: 863-79.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 863-879
    • Aguirre-Ghiso, J.A.1    Liu, D.2    Mignatti, A.3
  • 76
    • 0029148763 scopus 로고
    • Involvement of a mitogen-activated protein kinase signaling pathway in the regulation of urokinase promoter activity by c-Haras
    • Lengyel E, Stepp E, Gum R, et al. Involvement of a mitogen-activated protein kinase signaling pathway in the regulation of urokinase promoter activity by c-Haras. J Biol Chem 1995; 270: 23007-12.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23007-23012
    • Lengyel, E.1    Stepp, E.2    Gum, R.3
  • 77
    • 0029809873 scopus 로고    scopus 로고
    • Requirement of an upstream AP-1 motif for the constitutive and phorbol ester-inducible expression of the urokinase-type plasminogen activator receptor gene
    • Lengyel E, Wang H, Stepp E, et al. Requirement of an upstream AP-1 motif for the constitutive and phorbol ester-inducible expression of the urokinase-type plasminogen activator receptor gene. J Biol Chem 1996; 271: 23176-84.
    • (1996) J. Biol. Chem. , vol.271 , pp. 23176-23184
    • Lengyel, E.1    Wang, H.2    Stepp, E.3
  • 78
    • 0030996974 scopus 로고    scopus 로고
    • Elevated urokinase-type plasminogen activator receptor expression in a colon cancer cell line is due to a constitutively activated extracellular signal-regulated kinase-1-dependent signaling cascade
    • Lengyel E, Wang H, Gum R, et al. Elevated urokinase-type plasminogen activator receptor expression in a colon cancer cell line is due to a constitutively activated extracellular signal-regulated kinase-1-dependent signaling cascade. Oncogene 1997; 14: 2563-73.
    • (1997) Oncogene , vol.14 , pp. 2563-2573
    • Lengyel, E.1    Wang, H.2    Gum, R.3
  • 79
    • 0002460807 scopus 로고    scopus 로고
    • Tumor dormancy induced by downregulation of urokinase receptor in human carcinoma involves integrin and MAPK signaling
    • Aguirre Ghiso JA, Kovalski K, et al. Tumor dormancy induced by downregulation of urokinase receptor in human carcinoma involves integrin and MAPK signaling. J Cell Biol 1999; 147: 89-104.
    • (1999) J. Cell Biol. , vol.147 , pp. 89-104
    • Aguirre Ghiso, J.A.1    Kovalski, K.2
  • 80
    • 0346736507 scopus 로고    scopus 로고
    • The cleavage of the urokinase receptor regulates its multiple functions
    • Montuori N, Carriero MV, Salzano S, et al. The cleavage of the urokinase receptor regulates its multiple functions. J Biol Chem 2002; 277: 46932-9.
    • (2002) J. Biol. Chem. , vol.277 , pp. 46932-46939
    • Montuori, N.1    Carriero, M.V.2    Salzano, S.3
  • 81
    • 0033059340 scopus 로고    scopus 로고
    • Cellular glycosylphosphatidylinositol-specific phospholipase D regulates urokinase receptor shedding and cell surface expression
    • Wilhelm OG, Wilhelm S, Escott GM, et al. Cellular glycosylphosphatidylinositol-specific phospholipase D regulates urokinase receptor shedding and cell surface expression. J Cell Physiol 1999; 180: 225-35.
    • (1999) J. Cell Physiol. , vol.180 , pp. 225-235
    • Wilhelm, O.G.1    Wilhelm, S.2    Escott, G.M.3
  • 82
    • 0027314980 scopus 로고
    • An alternatively spliced variant of mRNA for the human receptor for urokinase plasminogen activator
    • Pyke C, Eriksen J, Solberg H, et al. An alternatively spliced variant of mRNA for the human receptor for urokinase plasminogen activator. FEBS Lett 1993; 326: 69-74.
    • (1993) FEBS Lett. , vol.326 , pp. 69-74
    • Pyke, C.1    Eriksen, J.2    Solberg, H.3
  • 83
    • 0030788411 scopus 로고    scopus 로고
    • The urokinase-type plasminogen activator system in cancer metastasis: A review
    • Andreasen PA, Kjøller L, Christensen L, et al. The urokinase-type plasminogen activator system in cancer metastasis: a review. Int J Cancer 1997; 72: 1-22.
    • (1997) Int. J. Cancer , vol.72 , pp. 1-22
    • Andreasen, P.A.1    Kjøller, L.2    Christensen, L.3
  • 84
    • 0036547696 scopus 로고    scopus 로고
    • Urokinase-type plasminogen activator: A potent marker of metastatic potential in human cancers
    • Duffy MJ. Urokinase-type plasminogen activator: a potent marker of metastatic potential in human cancers. Biochem Soc Trans 2002; 30: 207-10.
    • (2002) Biochem. Soc. Trans. , vol.30 , pp. 207-210
    • Duffy, M.J.1
  • 85
    • 0039770451 scopus 로고    scopus 로고
    • Reduction of breast carcinoma tumor growth and lung colonization by overexpression of the soluble urokinase-type plasminogen activator receptor (CD87)
    • Kruger A, Soeltl R, Lutz V, et al. Reduction of breast carcinoma tumor growth and lung colonization by overexpression of the soluble urokinase-type plasminogen activator receptor (CD87). Cancer Gene Ther 2000; 7: 292-9.
    • (2000) Cancer Gene Ther. , vol.7 , pp. 292-299
    • Kruger, A.1    Soeltl, R.2    Lutz, V.3
  • 86
    • 0034930530 scopus 로고    scopus 로고
    • High level synthesis of recombinant soluble urokinase receptor (CD87) by ovarian cancer cells reduces intraperitoneal tumor growth and spread in nude mice
    • Lutz V, Reuning U, Kruger A, et al. High level synthesis of recombinant soluble urokinase receptor (CD87) by ovarian cancer cells reduces intraperitoneal tumor growth and spread in nude mice. Biol Chem 2001; 382: 789-98.
    • (2001) Biol. Chem. , vol.382 , pp. 789-798
    • Lutz, V.1    Reuning, U.2    Kruger, A.3
  • 87
    • 0344875558 scopus 로고    scopus 로고
    • Soluble urokinase-type plasminogen activator receptor inhibits cancer cell growth and invasion by direct urokinase-independent effects on cell signaling
    • Jo M, Thomas KS, Wu L, et al. Soluble urokinase-type plasminogen activator receptor inhibits cancer cell growth and invasion by direct urokinase-independent effects on cell signaling. J Biol Chem 2003; 278: 46692-8.
    • (2003) J. Biol. Chem. , vol.278 , pp. 46692-46698
    • Jo, M.1    Thomas, K.S.2    Wu, L.3


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