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Volumn 57, Issue 14, 1997, Pages 3016-3025

Human ornithine decarboxylase-overproducing NIH3T3 cells induce rapidly growing, highly vascularized tumors in nude mice

Author keywords

[No Author keywords available]

Indexed keywords

ANGIOGENIC FACTOR; ORNITHINE DECARBOXYLASE; POLYAMINE; THROMBOSPONDIN;

EID: 0030834335     PISSN: 00085472     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (127)

References (85)
  • 2
    • 0023881236 scopus 로고
    • Polyamine metabolism and its importance in neoplastic cell growth and as target for chemotherapy
    • Pegg, A. Polyamine metabolism and its importance in neoplastic cell growth and as target for chemotherapy. Cancer Res., 48: 759-774, 1988.
    • (1988) Cancer Res. , vol.48 , pp. 759-774
    • Pegg, A.1
  • 3
    • 0025873423 scopus 로고
    • Polyamines: From molecular biology to clinical applications
    • Jänne, J., Alhonen, L., and Leinonen, P. Polyamines: from molecular biology to clinical applications. Ann. Med., 23: 241-259, 1991.
    • (1991) Ann. Med. , vol.23 , pp. 241-259
    • Jänne, J.1    Alhonen, L.2    Leinonen, P.3
  • 4
    • 0029455991 scopus 로고
    • Ornithine decarboxylase as a target for chemoprevention
    • Pegg, A., Shantz, L., and Coleman, C. Ornithine decarboxylase as a target for chemoprevention. J. Cell. Biochem., 22 (Suppl.): 132-138, 1995.
    • (1995) J. Cell. Biochem. , vol.22 , Issue.SUPPL. , pp. 132-138
    • Pegg, A.1    Shantz, L.2    Coleman, C.3
  • 5
    • 0027202387 scopus 로고
    • v-src: Delineation of molecular events relevant for the transformed phenotype
    • v-src: delineation of molecular events relevant for the transformed phenotype. J. Cell Biol., 122: 903-914, 1993.
    • (1993) J. Cell Biol. , vol.122 , pp. 903-914
    • Hölttä, E.1    Auvinen, M.2    Andersson, L.C.3
  • 6
    • 0024463314 scopus 로고
    • Activation of chimeric EGF-R/neu tyrosine kinase induces the fos/jun transcription factor complex, glucose transporter, and ornithine decarboxylase
    • Sistonen, L., Hölttä, E., Lehväslaiho, H., Lehtola, L., and Alitalo, K. Activation of chimeric EGF-R/neu tyrosine kinase induces the fos/jun transcription factor complex, glucose transporter, and ornithine decarboxylase. J. Cell Biol., 109: 1911-1919, 1989.
    • (1989) J. Cell Biol. , vol.109 , pp. 1911-1919
    • Sistonen, L.1    Hölttä, E.2    Lehväslaiho, H.3    Lehtola, L.4    Alitalo, K.5
  • 7
    • 0023886318 scopus 로고
    • The mechanism of ornithine decarboxylase deregulation in c-Ha-ras oncogene-transformed NIH3T3 cells
    • Hölttä, E., Sistonen, L., and Alitalo, K. The mechanism of ornithine decarboxylase deregulation in c-Ha-ras oncogene-transformed NIH3T3 cells. J. Biol. Chem., 263: 4500-4507, 1988.
    • (1988) J. Biol. Chem. , vol.263 , pp. 4500-4507
    • Hölttä, E.1    Sistonen, L.2    Alitalo, K.3
  • 8
    • 0026683752 scopus 로고
    • Ornithine decarboxylase activity is critical for cell transformation
    • Auvinen, M., Paasinen, A., Andersson, L. C., and Hölttä, E. Ornithine decarboxylase activity is critical for cell transformation. Nature (Lond.), 360: 355-358, 1992.
    • (1992) Nature (Lond.) , vol.360 , pp. 355-358
    • Auvinen, M.1    Paasinen, A.2    Andersson, L.C.3    Hölttä, E.4
  • 9
    • 0027263467 scopus 로고
    • Transformation of NIH3T3 cells by ornithine decarboxylase overexpression
    • Moshier, J., Dosescu, J., Skunca, M., and Luk, G. Transformation of NIH3T3 cells by ornithine decarboxylase overexpression. Cancer Res., 53: 2618-2622, 1993.
    • (1993) Cancer Res. , vol.53 , pp. 2618-2622
    • Moshier, J.1    Dosescu, J.2    Skunca, M.3    Luk, G.4
  • 10
    • 0028271504 scopus 로고
    • Overproduction of ornithine decarboxylase caused by relief of translational repression is associated with neoplastic transformation
    • Shantz, L., and Pegg, A. Overproduction of ornithine decarboxylase caused by relief of translational repression is associated with neoplastic transformation. Cancer Res., 54: 2313-2316, 1994.
    • (1994) Cancer Res. , vol.54 , pp. 2313-2316
    • Shantz, L.1    Pegg, A.2
  • 11
    • 0028963615 scopus 로고
    • Role of ornithine decarboxylase in epidermal tumorigenesis
    • Clifford, A., Morgan, D., Yuspa, S., Soler, A., and Gilmour, S. Role of ornithine decarboxylase in epidermal tumorigenesis. Cancer Res., 55: 1680-1686, 1995.
    • (1995) Cancer Res. , vol.55 , pp. 1680-1686
    • Clifford, A.1    Morgan, D.2    Yuspa, S.3    Soler, A.4    Gilmour, S.5
  • 12
    • 0029050287 scopus 로고
    • Increased frequency of spontaneous skin tumors in transgenic mice which overexpress ornithine decarboxylase
    • Megosh, L., Gilmour, S., Rosson, D., Soler, A., Blessing, M., Sawicki, J., and O'Brien, T. Increased frequency of spontaneous skin tumors in transgenic mice which overexpress ornithine decarboxylase. Cancer Res., 55: 4205-4209, 1995.
    • (1995) Cancer Res. , vol.55 , pp. 4205-4209
    • Megosh, L.1    Gilmour, S.2    Rosson, D.3    Soler, A.4    Blessing, M.5    Sawicki, J.6    O'Brien, T.7
  • 13
  • 14
    • 0027240106 scopus 로고
    • Direct transcriptional stimulation of the ornithine decarboxylase gene by Fos in PC12 but not in fibroblasts
    • Wrighton, C., and Busslinger, M. Direct transcriptional stimulation of the ornithine decarboxylase gene by Fos in PC12 but not in fibroblasts. Mol. Cell. Biol., 13: 4657-4669, 1993.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 4657-4669
    • Wrighton, C.1    Busslinger, M.2
  • 15
    • 0026639806 scopus 로고
    • Angiogenesis
    • Folkman, J., and Shing, Y. Angiogenesis, J. Biol. Chem., 267: 10931-10934, 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 10931-10934
    • Folkman, J.1    Shing, Y.2
  • 16
    • 0030576517 scopus 로고    scopus 로고
    • Patterns and emerging mechanisms of the angiogenic switch during tumorigenesis
    • Hanahan, D., and Folkman, J. Patterns and emerging mechanisms of the angiogenic switch during tumorigenesis. Cell, 86: 353-364, 1996.
    • (1996) Cell , vol.86 , pp. 353-364
    • Hanahan, D.1    Folkman, J.2
  • 17
    • 0028114985 scopus 로고
    • The implications of angiogenesis for the biology and therapy of cancer metastasis
    • Fidler, I., and Ellis, L. The implications of angiogenesis for the biology and therapy of cancer metastasis. Cell, 79: 185-188, 1994.
    • (1994) Cell , vol.79 , pp. 185-188
    • Fidler, I.1    Ellis, L.2
  • 18
    • 0026504737 scopus 로고
    • Monitoring the uptake and metabolism of amini analogues of polyamines in cultured cells by high performance liquid chromatography
    • Hyvönen, T., Keinänen, T., Khomutov, A., Khomutov, R., and Eloranta, T. Monitoring the uptake and metabolism of amini analogues of polyamines in cultured cells by high performance liquid chromatography. J. Chromatogr., 574: 17-21, 1992.
    • (1992) J. Chromatogr. , vol.574 , pp. 17-21
    • Hyvönen, T.1    Keinänen, T.2    Khomutov, A.3    Khomutov, R.4    Eloranta, T.5
  • 20
    • 0023198682 scopus 로고
    • Complete amino acid sequence of human ornithine decarboxylase deduced from complementary DNA
    • NY
    • Hickok, N., Seppänen, P., Gunsalus, P., and Jänne, O. A. Complete amino acid sequence of human ornithine decarboxylase deduced from complementary DNA. DNA (NY), 6: 179-187, 1987.
    • (1987) DNA , vol.6 , pp. 179-187
    • Hickok, N.1    Seppänen, P.2    Gunsalus, P.3    Jänne, O.A.4
  • 21
    • 1842334849 scopus 로고
    • Two ornithine decarboxylase mRNA species in mouse kidney arise from size heterogeneity at their 3′termini
    • Hickok, N., Seppänen, P., Kontula, P., Jänne, P., Bardin, C., and Jänne, O. A. Two ornithine decarboxylase mRNA species in mouse kidney arise from size heterogeneity at their 3′termini. Proc. Natl. Acad. Sci. USA, 81: 594-598, 1986.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 594-598
    • Hickok, N.1    Seppänen, P.2    Kontula, P.3    Jänne, P.4    Bardin, C.5    Jänne, O.A.6
  • 24
    • 0025966492 scopus 로고
    • Nuclear colocolization of cellular and viral Myc proteins with HSP70 in Myc-overexpressing cells
    • Koskinen, P., Sistonen, L., Evan, G., Morimoto, R., and Alitalo, K. Nuclear colocolization of cellular and viral Myc proteins with HSP70 in Myc-overexpressing cells. J. Virol., 65: 842-851, 1991.
    • (1991) J. Virol. , vol.65 , pp. 842-851
    • Koskinen, P.1    Sistonen, L.2    Evan, G.3    Morimoto, R.4    Alitalo, K.5
  • 25
    • 0026601537 scopus 로고
    • Alternative forms of Max can act either as enhancers or suppressors of cotransformation by c-Myc and Ras
    • Washington DC
    • Mäkelä, T., Koskinen, P., Västrik, I., and Alitalo, K. Alternative forms of Max can act either as enhancers or suppressors of cotransformation by c-Myc and Ras. Science (Washington DC), 256: 373-377, 1992.
    • (1992) Science , vol.256 , pp. 373-377
    • Mäkelä, T.1    Koskinen, P.2    Västrik, I.3    Alitalo, K.4
  • 26
    • 0027408096 scopus 로고
    • Mad: A heterodimeric partner for Max that antagonizes Myc transcriptional activity
    • Ayer, D., Kretzner, L., and Eisenman, R. Mad: a heterodimeric partner for Max that antagonizes Myc transcriptional activity. Cell, 72: 211-222, 1993.
    • (1993) Cell , vol.72 , pp. 211-222
    • Ayer, D.1    Kretzner, L.2    Eisenman, R.3
  • 27
    • 0023718397 scopus 로고
    • fos-associated cellular p39 is related to nuclear transcription factor AP-1
    • Sassone-Corsi, P., Lamph, W., Kamps, M., and Verma, I. fos-associated cellular p39 is related to nuclear transcription factor AP-1. Cell, 54: 553-560, 1988.
    • (1988) Cell , vol.54 , pp. 553-560
    • Sassone-Corsi, P.1    Lamph, W.2    Kamps, M.3    Verma, I.4
  • 28
    • 0000558585 scopus 로고
    • A gene activated by growth factors is related to the oncogene v-jun
    • Ryder, K., Lau, L., and Nathans, D. A gene activated by growth factors is related to the oncogene v-jun. Proc. Natl. Acad. Sci. USA, 85: 1487-1491, 1988.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 1487-1491
    • Ryder, K.1    Lau, L.2    Nathans, D.3
  • 30
    • 0022460149 scopus 로고
    • Human endothelial cell growth factor: Cloning, nucleotide sequence, and chromosome localization
    • Washington DC
    • Jaye, M., Howk, R., Burgess, W., Ricca, C., Chiu, I., Ravera, M., O'Brien, S., Modi, W., Maciag, T., and Drohan, W. Human endothelial cell growth factor: cloning, nucleotide sequence, and chromosome localization. Science (Washington DC), 233: 541-545, 1986.
    • (1986) Science , vol.233 , pp. 541-545
    • Jaye, M.1    Howk, R.2    Burgess, W.3    Ricca, C.4    Chiu, I.5    Ravera, M.6    O'Brien, S.7    Modi, W.8    Maciag, T.9    Drohan, W.10
  • 32
    • 0023186114 scopus 로고
    • Isolation of a rearranged human transforming gene following transfection of Kaposi's sarcoma DNA
    • Delli-Bovi, P., and Basilico, C. Isolation of a rearranged human transforming gene following transfection of Kaposi's sarcoma DNA. Proc. Natl. Acad. Sci. USA, 84: 5660-5664, 1987.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 5660-5664
    • Delli-Bovi, P.1    Basilico, C.2
  • 33
    • 0024818355 scopus 로고
    • Vascular endothelial growth factor is a secreted angiogenic mitogen
    • Washington DC
    • Leung, D., Cachianes, G., Kuang, W-J., Goeddel, D., and Ferrara, N. Vascular endothelial growth factor is a secreted angiogenic mitogen. Science (Washington DC), 246: 1306-1309, 1989.
    • (1989) Science , vol.246 , pp. 1306-1309
    • Leung, D.1    Cachianes, G.2    Kuang, W.-J.3    Goeddel, D.4    Ferrara, N.5
  • 34
    • 18744438097 scopus 로고
    • RFLPs for transforming growth factor α (TGFA) gene at 2p13
    • Murray, J., Buetow, K., and Bell, G. RFLPs for transforming growth factor α (TGFA) gene at 2p13. Nucleic Acids Res., 14: 7126-7131, 1986.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 7126-7131
    • Murray, J.1    Buetow, K.2    Bell, G.3
  • 35
    • 0022373618 scopus 로고
    • Human transforming growth factor-β complementary DNA sequence and expression in normal and transformed cells
    • Derynck, R., Jarret, J., Chen, E., Eaton, D., Bell, J., Assoian, R., Roberts, A., Sporn, M., and Goeddel, D. Human transforming growth factor-β complementary DNA sequence and expression in normal and transformed cells. Nature (Lond.), 316: 701-705, 1985.
    • (1985) Nature (Lond.) , vol.316 , pp. 701-705
    • Derynck, R.1    Jarret, J.2    Chen, E.3    Eaton, D.4    Bell, J.5    Assoian, R.6    Roberts, A.7    Sporn, M.8    Goeddel, D.9
  • 38
    • 0026052391 scopus 로고
    • Isolation of a human placenta cDNA coding for a protein related to the vascular permeability factor
    • Maglione, D., Guerriero, V., Viglietto, G., Delli-Bovi, P., and Persico, G. Isolation of a human placenta cDNA coding for a protein related to the vascular permeability factor. Proc. Natl. Acad. Sci. USA, 88: 9267-9271, 1991.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 9267-9271
    • Maglione, D.1    Guerriero, V.2    Viglietto, G.3    Delli-Bovi, P.4    Persico, G.5
  • 39
    • 0025824738 scopus 로고
    • Identification of a fibroblast-derived epithelial morphogen as a hepatocyte growth factor
    • Montesano, R., Matsumoto, K., Nakamura, T., and Orci, L. Identification of a fibroblast-derived epithelial morphogen as a hepatocyte growth factor. Cell, 67: 901-908, 1991.
    • (1991) Cell , vol.67 , pp. 901-908
    • Montesano, R.1    Matsumoto, K.2    Nakamura, T.3    Orci, L.4
  • 40
    • 0026703137 scopus 로고
    • Characterization of mouse thrombospondin 2 sequence and expression during cell growth and development
    • Laherty, C., O'Rourke, K., Wolf, F., Katz, R., Seldin, M., and Dixit, V. Characterization of mouse thrombospondin 2 sequence and expression during cell growth and development. J. Biol. Chem., 267: 3274-3281, 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 3274-3281
    • Laherty, C.1    O'Rourke, K.2    Wolf, F.3    Katz, R.4    Seldin, M.5    Dixit, V.6
  • 42
    • 0025032508 scopus 로고
    • Cloning and expression of two distinct high-affinity receptors cross-reacting with acidic and basic fibroblast growth factors
    • Dionne, C., Crumley, G., Bellot, F., Kaplow, J., Searforss, G., Ruta, M., Burgess, W., Jaye, M., and Schlessinger, J. Cloning and expression of two distinct high-affinity receptors cross-reacting with acidic and basic fibroblast growth factors. EMBO J., 9: 2685-2692, 1990.
    • (1990) EMBO J. , vol.9 , pp. 2685-2692
    • Dionne, C.1    Crumley, G.2    Bellot, F.3    Kaplow, J.4    Searforss, G.5    Ruta, M.6    Burgess, W.7    Jaye, M.8    Schlessinger, J.9
  • 44
    • 0025259592 scopus 로고
    • Nucleotide sequence and expression of a novel human receptor-type tyrosine kinase (flt) related to the fms family
    • Shibuya, M., Yamagachi, S., Yamane, A., Ikeda, T., Tojo, A., Matsushime, H., and Sato, M. Nucleotide sequence and expression of a novel human receptor-type tyrosine kinase (flt) related to the fms family. Oncogene, 5: 519-524, 1990.
    • (1990) Oncogene , vol.5 , pp. 519-524
    • Shibuya, M.1    Yamagachi, S.2    Yamane, A.3    Ikeda, T.4    Tojo, A.5    Matsushime, H.6    Sato, M.7
  • 46
    • 0022996811 scopus 로고
    • Complete primary structure and homology to an oncogene transformation-induced rat protein
    • Goldberg, G., Wilhelm, S., Kronberger, A., Bauer, E., Grant, G., and Eisen, A. Complete primary structure and homology to an oncogene transformation-induced rat protein. J. Biol. Chem., 261: 6600-6605, 1986.
    • (1986) J. Biol. Chem. , vol.261 , pp. 6600-6605
    • Goldberg, G.1    Wilhelm, S.2    Kronberger, A.3    Bauer, E.4    Grant, G.5    Eisen, A.6
  • 47
    • 0025952928 scopus 로고
    • Complete structure of human gene for 92-kDa type IV collagenase: Divergent regulation of expression for the 92-kDa and 72-kDa enzyme genes in HT-1080 cells
    • Huhtala, P., Tuuttila, A., Chow, L., Lohi, J., Keski-Oja, J., and Tryggvason, K. Complete structure of human gene for 92-kDa type IV collagenase: divergent regulation of expression for the 92-kDa and 72-kDa enzyme genes in HT-1080 cells. J. Biol. Chem., 266: 16485-16490, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 16485-16490
    • Huhtala, P.1    Tuuttila, A.2    Chow, L.3    Lohi, J.4    Keski-Oja, J.5    Tryggvason, K.6
  • 48
    • 0023919959 scopus 로고
    • H-ras oncogene transformed human bronchial cells (TBE-1) secrete a single metalloproteinase capable of degrading basement membrane collagen
    • Collier, I., Wilhelm, S., Eisen, A., Maremer, B., Grant, G., Selzer, J., Kronberger, A., He, C., Bauer, E., and Goldberg, G. H-ras oncogene transformed human bronchial cells (TBE-1) secrete a single metalloproteinase capable of degrading basement membrane collagen. J. Biol. Chem., 263: 6600-6605, 1988.
    • (1988) J. Biol. Chem. , vol.263 , pp. 6600-6605
    • Collier, I.1    Wilhelm, S.2    Eisen, A.3    Maremer, B.4    Grant, G.5    Selzer, J.6    Kronberger, A.7    He, C.8    Bauer, E.9    Goldberg, G.10
  • 51
    • 0030055680 scopus 로고    scopus 로고
    • Regulation of membrane-type matrix metalloproteinase-1 expression by growth factors and phorbol 12-myristate 13-acetate
    • Lohi, J., Lehti, K., Westermarck, J., Kähäri, V-M., and Keski-Oja, J. Regulation of membrane-type matrix metalloproteinase-1 expression by growth factors and phorbol 12-myristate 13-acetate. Eur. J. Biochem., 219: 239-247, 1996.
    • (1996) Eur. J. Biochem. , vol.219 , pp. 239-247
    • Lohi, J.1    Lehti, K.2    Westermarck, J.3    Kähäri, V.-M.4    Keski-Oja, J.5
  • 52
    • 0023689701 scopus 로고
    • Structural study of long arm fragments of laminin: Evidence for repetitive C-terminal sequences in the A-chain, not present in the B-chain
    • Deutzman, R., Huber, J., Schmetz, K., Oberbäumer, I., and Hartl, L. Structural study of long arm fragments of laminin: evidence for repetitive C-terminal sequences in the A-chain, not present in the B-chain. Eur. J. Biochem., 177: 35-45, 1988.
    • (1988) Eur. J. Biochem. , vol.177 , pp. 35-45
    • Deutzman, R.1    Huber, J.2    Schmetz, K.3    Oberbäumer, I.4    Hartl, L.5
  • 53
    • 0022871153 scopus 로고
    • New pUC-derived expression vectors for rapid construction of cDNA libraries
    • Amst.
    • Obermäuer, I. New pUC-derived expression vectors for rapid construction of cDNA libraries. Gene (Amst.), 49: 81-91, 1986.
    • (1986) Gene , vol.49 , pp. 81-91
    • Obermäuer, I.1
  • 55
    • 0030296982 scopus 로고    scopus 로고
    • FGF-2 inhibits apoptosis in human teratocarcinoma cells during differentiation on collagen substratum
    • Alanko, T., Tienari, J., Lehtonen, E., and Saksela, O. FGF-2 inhibits apoptosis in human teratocarcinoma cells during differentiation on collagen substratum. Exp. Cell Res., 228: 306-312.
    • Exp. Cell Res. , vol.228 , pp. 306-312
    • Alanko, T.1    Tienari, J.2    Lehtonen, E.3    Saksela, O.4
  • 56
    • 0030026897 scopus 로고    scopus 로고
    • A novel vascular endothelial growth factor, VEGF-C, is a ligand for the Flt4 (VEGF-R3) and KDR (VEGF-R2) receptor tyrosine kinases
    • Joukov, V., Pajusola, K., Kaipainen, A., Chilov, D., Lahtinen, I., Kukk, E., Saksela, O., Kalkkinen, N., and Alitalo, K. A novel vascular endothelial growth factor, VEGF-C, is a ligand for the Flt4 (VEGF-R3) and KDR (VEGF-R2) receptor tyrosine kinases. EMBO J., 15: 101-110, 1996.
    • (1996) EMBO J. , vol.15 , pp. 101-110
    • 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
  • 57
    • 0024362217 scopus 로고
    • Polyamines differentially modulate the transcription of growth-associated genes in human colon carcinoma
    • Celano, P., Baylin, S., and Casero, R. Polyamines differentially modulate the transcription of growth-associated genes in human colon carcinoma. J. Biol. Chem., 264: 8922-8927, 1989.
    • (1989) J. Biol. Chem. , vol.264 , pp. 8922-8927
    • Celano, P.1    Baylin, S.2    Casero, R.3
  • 58
    • 0027991439 scopus 로고
    • Activation of the proto-oncogene c-myc and c-fos by c-ras: Involvement of polyamines
    • Tabib, A., and Bachrach, U. Activation of the proto-oncogene c-myc and c-fos by c-ras: involvement of polyamines. Biochem. Biophys. Res. Commun., 202: 720-727, 1994.
    • (1994) Biochem. Biophys. Res. Commun. , vol.202 , pp. 720-727
    • Tabib, A.1    Bachrach, U.2
  • 59
    • 0028016495 scopus 로고
    • Ornithine decarboxylase is a mediator of c-Myc induced apoptosis
    • Packham, G., and Cleveland, J. Ornithine decarboxylase is a mediator of c-Myc induced apoptosis. Mol. Cell. Biol., 14: 5741-5747, 1994.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 5741-5747
    • Packham, G.1    Cleveland, J.2
  • 60
    • 0028822437 scopus 로고
    • Induction of apoptosis by excessive polyamine accumulation in ornithine decarboxylase overproducing LI210 cells
    • Poulin, R., Pelletier, G., and Pegg, A. Induction of apoptosis by excessive polyamine accumulation in ornithine decarboxylase overproducing LI210 cells. Biochem. J., 34: 723-727, 1995.
    • (1995) Biochem. J. , vol.34 , pp. 723-727
    • Poulin, R.1    Pelletier, G.2    Pegg, A.3
  • 61
    • 0026337295 scopus 로고
    • Tumor suppressor genes
    • Washington DC
    • Weinberg, R. A. Tumor suppressor genes. Science (Washington DC), 254: 1138-1146, 1991.
    • (1991) Science , vol.254 , pp. 1138-1146
    • Weinberg, R.A.1
  • 62
    • 0027326586 scopus 로고
    • The tumor suppressor genes
    • Levine, A. J. The tumor suppressor genes. Annu. Rev. Biochem., 62: 623-651, 1993.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 623-651
    • Levine, A.J.1
  • 63
    • 0025343230 scopus 로고
    • Signal transduction by receptors with tyrosine kinase activity
    • Ullrich, A., and Schlessinger, J. Signal transduction by receptors with tyrosine kinase activity. Cell, 61: 203-212, 1990.
    • (1990) Cell , vol.61 , pp. 203-212
    • Ullrich, A.1    Schlessinger, J.2
  • 64
    • 0028824340 scopus 로고
    • Ornithine decarboxylase transformation of NIH3T3 cells is mediated by altered growth factor receptor activity
    • Moshier, J., Malecka-Panas, E., Geng, H., Dosescu, J., Tureaud, J., Skunca, M., and Majumdar, A. Ornithine decarboxylase transformation of NIH3T3 cells is mediated by altered growth factor receptor activity. Cancer Res., 55: 5358-5365, 1995.
    • (1995) Cancer Res. , vol.55 , pp. 5358-5365
    • Moshier, J.1    Malecka-Panas, E.2    Geng, H.3    Dosescu, J.4    Tureaud, J.5    Skunca, M.6    Majumdar, A.7
  • 65
    • 0027990414 scopus 로고
    • A novel signaling molecule, p130, forms stable complexes in vivo with c-Crk and v-Src in a tyrosine-phosphorylation-dependent manner
    • Sakai, R., Iwamatsu, A., Hirano, N., Ogawa, S., Tanaka, T., Mano, H., Yazaki, Y., and Hirai, H. A novel signaling molecule, p130, forms stable complexes in vivo with c-Crk and v-Src in a tyrosine-phosphorylation-dependent manner. EMBO J., 13: 3748-3756, 1994.
    • (1994) EMBO J. , vol.13 , pp. 3748-3756
    • Sakai, R.1    Iwamatsu, A.2    Hirano, N.3    Ogawa, S.4    Tanaka, T.5    Mano, H.6    Yazaki, Y.7    Hirai, H.8
  • 66
    • 0023236992 scopus 로고
    • Increase of urokinase type plasminogen activator gene expression in human lung and breast carcinomas
    • Sappino, A., Busso, N., Belin, D., and Vassali, J. Increase of urokinase type plasminogen activator gene expression in human lung and breast carcinomas. Cancer Res., 47: 4043-4046, 1987.
    • (1987) Cancer Res. , vol.47 , pp. 4043-4046
    • Sappino, A.1    Busso, N.2    Belin, D.3    Vassali, J.4
  • 67
    • 0027333411 scopus 로고
    • Tumor cell interactions with the extracellular matrix during invasion and metastasis
    • Stetler-Stevenson, W., Axnavoorian, S., and Liotta, E. Tumor cell interactions with the extracellular matrix during invasion and metastasis. Annu. Rev. Cell Biol., 9: 541-573, 1993.
    • (1993) Annu. Rev. Cell Biol. , vol.9 , pp. 541-573
    • Stetler-Stevenson, W.1    Axnavoorian, S.2    Liotta, E.3
  • 68
    • 0028291737 scopus 로고
    • A matrix metalloproteinase expressed on the surface of invasive tumor cells
    • Sato, H., Takino, T., Okada, Y., Shinagawa, A., Yamamoto, E., and Seiki, M. A matrix metalloproteinase expressed on the surface of invasive tumor cells. Nature (Lond.), 370: 61-65, 1994.
    • (1994) Nature (Lond.) , vol.370 , pp. 61-65
    • Sato, H.1    Takino, T.2    Okada, Y.3    Shinagawa, A.4    Yamamoto, E.5    Seiki, M.6
  • 69
    • 0028929803 scopus 로고
    • Angiogenesis in cancer, vascular, rheumatoid and other disease
    • Folkman, J. Angiogenesis in cancer, vascular, rheumatoid and other disease. Nat. Med., 1: 27-31, 1995.
    • (1995) Nat. Med. , vol.1 , pp. 27-31
    • Folkman, J.1
  • 70
    • 0027968231 scopus 로고
    • Basal lamina assembly
    • Yurchenco, P., and O'Rear, J. Basal lamina assembly. Curr. Biol., 6: 674-681, 1994.
    • (1994) Curr. Biol. , vol.6 , pp. 674-681
    • Yurchenco, P.1    O'Rear, J.2
  • 71
    • 0024549349 scopus 로고
    • Induction of angiogenesis during the transition from hyperplasia to neoplasia
    • Folkman, J., Watson, K., Ingber, D., and Hanahan, D. Induction of angiogenesis during the transition from hyperplasia to neoplasia. Nature (Lond.), 339: 58-61, 1989.
    • (1989) Nature (Lond.) , vol.339 , pp. 58-61
    • Folkman, J.1    Watson, K.2    Ingber, D.3    Hanahan, D.4
  • 72
    • 0027197246 scopus 로고
    • Recombinant fibroblast growth factor-1 promotes intimal hyperplasia and angiogenesis in arteries in vivo
    • Nabel, E., Yang, Z-Y., Plautz, G., Forough, R., Zhan, X., Haudenschild, C., Maciag, T., and Nabel, G. Recombinant fibroblast growth factor-1 promotes intimal hyperplasia and angiogenesis in arteries in vivo. Nature (Lond.), 362: 844-846, 1993.
    • (1993) Nature (Lond.) , vol.362 , pp. 844-846
    • Nabel, E.1    Yang, Z.-Y.2    Plautz, G.3    Forough, R.4    Zhan, X.5    Haudenschild, C.6    Maciag, T.7    Nabel, G.8
  • 73
    • 0027197245 scopus 로고
    • Inhibition of vascular endothelial growth factor-induced angiogenesis suppresses tumor growth in vivo
    • Kim, J., Li, B., Winer, J., Armanini, M., Gillett, N., Phillips, H., and Ferrara, N. Inhibition of vascular endothelial growth factor-induced angiogenesis suppresses tumor growth in vivo. Nature (Lond.), 362: 841-844, 1993.
    • (1993) Nature (Lond.) , vol.362 , pp. 841-844
    • Kim, J.1    Li, B.2    Winer, J.3    Armanini, M.4    Gillett, N.5    Phillips, H.6    Ferrara, N.7
  • 74
    • 0000004505 scopus 로고
    • VEGF/VPF: The angiogenesis factor found?
    • Klagsbrun, M., and Soker, S. VEGF/VPF: the angiogenesis factor found? Curr. Biol., 3: 699-701, 1993.
    • (1993) Curr. Biol. , vol.3 , pp. 699-701
    • Klagsbrun, M.1    Soker, S.2
  • 75
    • 0026485002 scopus 로고
    • Vascular endothelial growth factor induced by hypoxia may mediate hypoxia-initiated angiogenesis
    • Schweiki, D., Itin, A., Soffer, D., and Keshet, E. Vascular endothelial growth factor induced by hypoxia may mediate hypoxia-initiated angiogenesis. Nature (Lond.), 359: 843-845, 1992.
    • (1992) Nature (Lond.) , vol.359 , pp. 843-845
    • Schweiki, D.1    Itin, A.2    Soffer, D.3    Keshet, E.4
  • 76
    • 0026446102 scopus 로고
    • Vascular endothelial growth factor is a potential tumor angiogenesis factor in human gliomas in vivo
    • Plate, K., Breier, G., Weich, H., and Risau, W. Vascular endothelial growth factor is a potential tumor angiogenesis factor in human gliomas in vivo. Nature (Lond.), 359: 845-848, 1992.
    • (1992) Nature (Lond.) , vol.359 , pp. 845-848
    • Plate, K.1    Breier, G.2    Weich, H.3    Risau, W.4
  • 77
    • 0026572345 scopus 로고
    • The fms-like tyrosine kinase, a receptor for vascular endothelial growth factor
    • Washington DC
    • Vries, C., Escobedo, J., Ueno, H., Houck, Ferrara, N., and Williams, L. The fms-like tyrosine kinase, a receptor for vascular endothelial growth factor. Science (Washington DC), 255: 989-991, 1992.
    • (1992) Science , vol.255 , pp. 989-991
    • Vries, C.1    Escobedo, J.2    Ueno, H.3    Houck4    Ferrara, N.5    Williams, L.6
  • 78
    • 0027466849 scopus 로고
    • High affinity VEGF binding and developmental expression suggest Flk-1 as a major regulator of vasculogenesis and angiogenesis
    • Millauer, B., Wizigman-Voos, S., Schnurch, H., Martinez, R., Moller, N., Risau, W., and Ullrich, A. High affinity VEGF binding and developmental expression suggest Flk-1 as a major regulator of vasculogenesis and angiogenesis. Cell, 72: 835-846, 1993.
    • (1993) Cell , vol.72 , pp. 835-846
    • Millauer, B.1    Wizigman-Voos, S.2    Schnurch, H.3    Martinez, R.4    Moller, N.5    Risau, W.6    Ullrich, A.7
  • 80
    • 0030025773 scopus 로고    scopus 로고
    • Hypoxia-mediated selection of cells with diminished apoptotic potential in solid tumors
    • Graeber, T., Osmanian, C. Jacks, T., Housman, D., Koch, C., Lowe, S., and Giaccia, A. Hypoxia-mediated selection of cells with diminished apoptotic potential in solid tumors. Nature (Lond.), 379: 88-91, 1996.
    • (1996) Nature (Lond.) , vol.379 , pp. 88-91
    • Graeber, T.1    Osmanian, C.2    Jacks, T.3    Housman, D.4    Koch, C.5    Lowe, S.6    Giaccia, A.7
  • 81
    • 0024503338 scopus 로고
    • Regulation of the activity of a new inhibitor of angiogenesis by a cancer suppressor gene
    • Rastinejad, F., Polverini, P., and Bouck, N. Regulation of the activity of a new inhibitor of angiogenesis by a cancer suppressor gene. Cell, 56: 345-355, 1989.
    • (1989) Cell , vol.56 , pp. 345-355
    • Rastinejad, F.1    Polverini, P.2    Bouck, N.3
  • 82
    • 0025147371 scopus 로고
    • A tumor suppressor-dependent inhibitor of angiogenesis is immunologically and functionally indistiguishable from a fragment of thrombospondin
    • Good, D., Polverini, P., Rastinejad, F., Le Beau, M., Lemons, R., Frazier, W., and Bouck, N. A tumor suppressor-dependent inhibitor of angiogenesis is immunologically and functionally indistiguishable from a fragment of thrombospondin. Proc. Natl. Acad. Sci. USA, 87: 6624-6628, 1990.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 6624-6628
    • Good, D.1    Polverini, P.2    Rastinejad, F.3    Le Beau, M.4    Lemons, R.5    Frazier, W.6    Bouck, N.7
  • 83
    • 0028060380 scopus 로고
    • Control of angiogenesis in fibroblasts by p53 regulation of thrombospondin-1
    • Washington DC
    • Dameron, K., Volpert, O., Tainsky, M., and Bouck, N. Control of angiogenesis in fibroblasts by p53 regulation of thrombospondin-1. Science (Washington DC), 265: 1582-1584, 1994.
    • (1994) Science , vol.265 , pp. 1582-1584
    • Dameron, K.1    Volpert, O.2    Tainsky, M.3    Bouck, N.4
  • 84
    • 1842374819 scopus 로고
    • Polyamines and angiogenesis: Inhibition of tumor angiogenesis by the irreversible inhibitor of ornithine decarboxylase, α-difluoromethylornithine
    • S. H. Goldemberg and I. D. Algranati (eds.). Oxford, United Kingdom: IRL Press
    • Takigawa, M., Enomoto, M., Nishida, Y., Pan, H-O., Kinoshota, A., and Suzuki, F. Polyamines and angiogenesis: inhibition of tumor angiogenesis by the irreversible inhibitor of ornithine decarboxylase, α-difluoromethylornithine. In: S. H. Goldemberg and I. D. Algranati (eds.), The biology and Chemistry of Polyamines, pp. 203-211. Oxford, United Kingdom: IRL Press, 1990.
    • (1990) The Biology and Chemistry of Polyamines , pp. 203-211
    • Takigawa, M.1    Enomoto, M.2    Nishida, Y.3    Pan, H.-O.4    Kinoshota, A.5    Suzuki, F.6
  • 85
    • 0023100851 scopus 로고
    • Antimetastatic activity of DL-α-difluoromethylornithine, an inhibitor of polyamine biosynthesis, in mice
    • Sunkara, P., and Rosenberger, A. Antimetastatic activity of DL-α-difluoromethylornithine, an inhibitor of polyamine biosynthesis, in mice. Cancer Res., 47: 933-935, 1987.
    • (1987) Cancer Res. , vol.47 , pp. 933-935
    • Sunkara, P.1    Rosenberger, A.2


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