메뉴 건너뛰기




Volumn 55, Issue 9, 1995, Pages 1856-1862

Molecular Insights into Cancer Invasion: Strategies for Prevention and Intervention

Author keywords

[No Author keywords available]

Indexed keywords

5 AMINO 1 [3,5 DICHLORO 4 (4 CHLOROBENZOYL)BENZYL] 1H 1,2,3 TRIAZOLE 4 CARBOXAMIDE; BATIMASTAT; CYTOSTATIC AGENT; METALLOPROTEINASE INHIBITOR; TRIAZOLE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 0028944106     PISSN: 00085472     EISSN: 15387445     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (502)

References (92)
  • 1
    • 0028006219 scopus 로고
    • Commentary: rethinking cancer
    • Astrow, A. B. Commentary: rethinking cancer. Lancet, 343: 494–495, 1994.
    • (1994) Lancet , vol.343 , pp. 494-495
    • Astrow, A.B.1
  • 2
    • 0022627586 scopus 로고
    • Progress against cancer?
    • Bailar, J. C., and Smith, E. Progress against cancer? N. Engl. J. Med., 314: 1226–1232, 1986.
    • (1986) N. Engl. J. Med. , vol.314 , pp. 1226-1232
    • Bailar, J.C.1    Smith, E.2
  • 3
    • 0014492997 scopus 로고
    • The study of mammary carcinoma by mammography and whole organ sectioning, early observations
    • Gallager, H. S., and Martin, J. E. The study of mammary carcinoma by mammography and whole organ sectioning, early observations, Cancer (Phila.), 23: 855–866, 1969.
    • (1969) Cancer (Phila.) , vol.23 , pp. 855-866
    • Gallager, H.S.1    Martin, J.E.2
  • 4
    • 0028346953 scopus 로고
    • Progress in cancer chemoprevention: perspectives on agent selection and short-term clinical intervention trials
    • Kelloff, G. J., Boone, C. W., Steele, V., et al. Progress in cancer chemoprevention: perspectives on agent selection and short-term clinical intervention trials. Cancer Res., 54: 2015–2024, 1994.
    • (1994) Cancer Res. , vol.54 , pp. 2015-2024
    • Kelloff, G.J.1    Boone, C.W.2    Steele, V.3
  • 5
    • 0022626427 scopus 로고
    • Geometry, growth rates, and duration of cancer and carcinoma in situ of the breast before detection by screening
    • Spratt, J. S., Greenberg, R. A., and Heuser, L. S. Geometry, growth rates, and duration of cancer and carcinoma in situ of the breast before detection by screening. Cancer Res., 46: 970–974, 1986.
    • (1986) Cancer Res. , vol.46 , pp. 970-974
    • Spratt, J.S.1    Greenberg, R.A.2    Heuser, L.S.3
  • 6
    • 0027141759 scopus 로고
    • Prevention therapy: basic science and the resolution of the cancer problem—presidential address
    • Wattenberg, L. W. Prevention therapy: basic science and the resolution of the cancer problem—presidential address. Cancer Res., 53: 5890–5896, 1993.
    • (1993) Cancer Res. , vol.53 , pp. 5890-5896
    • Wattenberg, L.W.1
  • 7
    • 0028928694 scopus 로고
    • Identical allelic loss on chromosome 1lql3 in microdissected in situ and invasive human breast cancer
    • Zhuang, Z., Merino, M., Chuaqui, R., Liotta, L. A., and Emmert-Buck, M. Identical allelic loss on chromosome 1lql3 in microdissected in situ and invasive human breast cancer. Cancer Res., 55: 467–471, 1995.
    • (1995) Cancer Res. , vol.55 , pp. 467-471
    • Zhuang, Z.1    Merino, M.2    Chuaqui, R.3    Liotta, L.A.4    Emmert-Buck, M.5
  • 8
    • 0019495782 scopus 로고
    • Management and survival of female patients with minimal breast cancer
    • Bedwani, R., Vana, J., Rosner, D., et al. Management and survival of female patients with minimal breast cancer. Cancer (Phila.), 47: 2769–2778, 1981.
    • (1981) Cancer (Phila.) , vol.47 , pp. 2769-2778
    • Bedwani, R.1    Vana, J.2    Rosner, D.3
  • 9
    • 0343285053 scopus 로고
    • Circulating cancer cells
    • L. G. Koss (ed.), Ed. 4, Philadelphia: J. B. Lippincott Company
    • Melamed, M. Circulating cancer cells. In: L. G. Koss (ed.), Diagnostic Cytology and Its Histopathologic Bases, Ed. 4, Vol. 2, pp, 1403–1419. Philadelphia: J. B. Lippincott Company, 1992.
    • (1992) Diagnostic Cytology and Its Histopathologic Bases , vol.2 , pp. 1403-1419
    • Melamed, M.1
  • 10
    • 0016218630 scopus 로고
    • Quantitative relationships of intravascular tumor cells: tumor vessels and pulmonary metastases following tumor implantation
    • Liotta, L. A., Kleinerman, J., and Saidel, G. Quantitative relationships of intravascular tumor cells: tumor vessels and pulmonary metastases following tumor implantation. Cancer Res., 34: 997–1003, 1974.
    • (1974) Cancer Res. , vol.34 , pp. 997-1003
    • Liotta, L.A.1    Kleinerman, J.2    Saidel, G.3
  • 11
    • 85013312416 scopus 로고
    • Tumor angiogenesis: therapeutic implications
    • Folkman, J. Tumor angiogenesis: therapeutic implications. N. Engl. J. Med., 285: 1182–1186, 1971.
    • (1971) N. Engl. J. Med. , vol.285 , pp. 1182-1186
    • Folkman, J.1
  • 12
    • 0026193383 scopus 로고
    • Gene expression, cellular diversification and tumor progression to the metastatic phenotype
    • Nicolson, G. L. Gene expression, cellular diversification and tumor progression to the metastatic phenotype. Bioessays, 13: 337–342, 1991.
    • (1991) Bioessays , vol.13 , pp. 337-342
    • Nicolson, G.L.1
  • 13
    • 0019873814 scopus 로고
    • Partial purification and characterization of a neutral proteinase which cleaves type IV collagen
    • Liotta, L. A., Tryggvason, K., Garbisa, S., Gehron-Robey, P., and Abe, S. Partial purification and characterization of a neutral proteinase which cleaves type IV collagen. Biochemistry, 20: 100–104, 1981.
    • (1981) Biochemistry , vol.20 , pp. 100-104
    • Liotta, L.A.1    Tryggvason, K.2    Garbisa, S.3    Gehron-Robey, P.4    Abe, S.5
  • 14
    • 0020601626 scopus 로고
    • Loss of basement membrane components by invasive tumors but not by their benign counterparts, Lab
    • Barsky, S. H., Siegal, G. P., Jannotta, F., and Liotta L. A. Loss of basement membrane components by invasive tumors but not by their benign counterparts, Lab. Invest., 49: 140–147, 1983.
    • (1983) Invest. , vol.49 , pp. 140-147
    • Barsky, S.H.1    Siegal, G.P.2    Jannotta, F.3    Liotta, L.A.4
  • 15
    • 0025312728 scopus 로고
    • A genetic model for colorectal tumorigenesis
    • Fearon, E. R., and Vogelstein, B. A genetic model for colorectal tumorigenesis. Cell, 61: 759–767, 1990.
    • (1990) Cell , vol.61 , pp. 759-767
    • Fearon, E.R.1    Vogelstein, B.2
  • 16
    • 0026027556 scopus 로고
    • Cancer metastasis and angiogenesis; an imbalance of positive and negative regulation
    • Liotta, L. A., Steeg, P. S., and Stetler-Stevenson, W. G. Cancer metastasis and angiogenesis; an imbalance of positive and negative regulation. Cell, 64: 327–336, 1991.
    • (1991) Cell , vol.64 , pp. 327-336
    • Liotta, L.A.1    Steeg, P.S.2    Stetler-Stevenson, W.G.3
  • 17
    • 0026503656 scopus 로고
    • Contact and adhesive specificities in the associations, migrations, and targeting of cells and axons
    • Hynes, R. O., and Lander, A. D. Contact and adhesive specificities in the associations, migrations, and targeting of cells and axons. Cell, 68: 303–322, 1992.
    • (1992) Cell , vol.68 , pp. 303-322
    • Hynes, R.O.1    Lander, A.D.2
  • 19
    • 0025765115 scopus 로고
    • E-cadherin-mediated cell-cell adhesion prevents invasivenss of human colorectal carcinoma cells
    • Frixen, U. H., Behrens, J., Sachs, M., et al. E-cadherin-mediated cell-cell adhesion prevents invasivenss of human colorectal carcinoma cells. J. Cell Biol., 113: 173–185, 1991.
    • (1991) J. Cell Biol. , vol.113 , pp. 173-185
    • Frixen, U.H.1    Behrens, J.2    Sachs, M.3
  • 20
    • 0019195010 scopus 로고
    • Metastatic potential correlates with enzymatic degradation of basement membrane collagen
    • Liotta, L. A., Tryggvason, K., Garbisa, S., Hart, I., Foltz, C. M., and Shafie, S. Metastatic potential correlates with enzymatic degradation of basement membrane collagen. Nature (Lond.), 284: 67–68, 1980.
    • (1980) Nature (Lond.) , vol.284 , pp. 67-68
    • Liotta, L.A.1    Tryggvason, K.2    Garbisa, S.3    Hart, I.4    Foltz, C.M.5    Shafie, S.6
  • 21
    • 0028276786 scopus 로고
    • Invasiveness and metastasis of NIH 3T3 cells induced by Met-hepatocyte growth factor/scatter factor autocrine stimulation
    • Rong, S., Segal, S., Anver, M., Resau, J. H., and Vande Woude, G. F. Invasiveness and metastasis of NIH 3T3 cells induced by Met-hepatocyte growth factor/scatter factor autocrine stimulation. Proc. Natl. Acad. Sci. USA, 91: 4731–4735, 1994.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 4731-4735
    • Rong, S.1    Segal, S.2    Anver, M.3    Resau, J.H.4    Vande Woude, G.F.5
  • 22
    • 0026787698 scopus 로고
    • Identification, purification, and partial sequence analysis of autotaxin, a novel nrotffity-stimulating protein
    • Stracke, M. L., Krutzsch, H. C., Unsworth, E. J., årestad, A., Cioce, V., Schiffinann, E., and Liotta, L. A. Identification, purification, and partial sequence analysis of autotaxin, a novel nrotffity-stimulating protein. J. Biol. Chem., 267: 2524–2529, 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 2524-2529
    • Stracke, M.L.1    Krutzsch, H.C.2    Unsworth, E.J.3    årestad, A.4    Cioce, V.5    Schiffinann, E.6    Liotta, L.A.7
  • 23
    • 0025728353 scopus 로고
    • Signaling targets for anticancer drug development
    • Powis, G. Signaling targets for anticancer drug development. Trends Pharmacol. Sci., 12: 188–194, 1991.
    • (1991) Trends Pharmacol. Sci. , vol.12 , pp. 188-194
    • Powis, G.1
  • 24
    • 0026915386 scopus 로고
    • Inositol phosphates and Ca2+ entry: toward a proliferation or a simplification
    • Irvine, R. F. Inositol phosphates and Ca2+ entry: toward a proliferation or a simplification, FASEB J., 6: 3085–3091, 1992.
    • (1992) FASEB J. , vol.6 , pp. 3085-3091
    • Irvine, R.F.1
  • 25
    • 0028331587 scopus 로고
    • Farnesyltransferase inhibitors: ras research yields a potential cancer therapeutic
    • Gibbs, J. B., Oliff, A., and Kohl, N. E. Farnesyltransferase inhibitors: ras research yields a potential cancer therapeutic. Cell, 77: 175–178, 1994.
    • (1994) Cell , vol.77 , pp. 175-178
    • Gibbs, J.B.1    Oliff, A.2    Kohl, N.E.3
  • 26
    • 0028009848 scopus 로고
    • Calcium-mediated signal transduction: biology, biochemistry, and therapy
    • Cole, K. A., and Kohn, E. C. Calcium-mediated signal transduction: biology, biochemistry, and therapy. Cancer Metastasis Rev., 13: 33–41, 1994.
    • (1994) Cancer Metastasis Rev. , vol.13 , pp. 33-41
    • Cole, K.A.1    Kohn, E.C.2
  • 27
    • 0028146228 scopus 로고
    • Smooth muscle cell migration and matrix metalloproteinase expression after arterial injury in the rat
    • Bendeck, M. P., Zempo, N., Clowes, A. W., and Reidy, M. A. Smooth muscle cell migration and matrix metalloproteinase expression after arterial injury in the rat. Circ. Res., 75: 539–545, 1994.
    • (1994) Circ. Res. , vol.75 , pp. 539-545
    • Bendeck, M.P.1    Zempo, N.2    Clowes, A.W.3    Reidy, M.A.4
  • 28
    • 0027732212 scopus 로고
    • Tumor angiogenesis: reveiw of current applications in tumor prognostication
    • Weidner, N. Tumor angiogenesis: reveiw of current applications in tumor prognostication. Scmin. Diagn. Pathol., 10: 302–313, 1993.
    • (1993) Scmin. Diagn. Pathol. , vol.10 , pp. 302-313
    • Weidner, N.1
  • 29
    • 0026768210 scopus 로고
    • Coordinated expression of extracellular matrix degrading proteinases and their inhibitors regulates mammary epithelial function during involution
    • Talhouk, R. S., Bisell, M. J., and Werb, Z. Coordinated expression of extracellular matrix degrading proteinases and their inhibitors regulates mammary epithelial function during involution. J. Cell Biol., 118: 1271–1282, 1992.
    • (1992) J. Cell Biol. , vol.118 , pp. 1271-1282
    • Talhouk, R.S.1    Bisell, M.J.2    Werb, Z.3
  • 30
    • 0027362796 scopus 로고
    • Regulated tyrosine phosphorylation at the tips of growth cone filopodia
    • Wu, D.-Y., and Goldberg, D. J. Regulated tyrosine phosphorylation at the tips of growth cone filopodia. J. Cell Biol., 123: 653–664, 1993.
    • (1993) J. Cell Biol. , vol.123 , pp. 653-664
    • Wu, D.-Y.1    Goldberg, D.J.2
  • 31
    • 0025610377 scopus 로고
    • Mechanisms of trophoblast invasiveness and their control: the role of proteases and protease inhibitors
    • Lola, P. K., and Graham, C. H. Mechanisms of trophoblast invasiveness and their control: the role of proteases and protease inhibitors. Cancer Metastasis Rev., 9: 369–380, 1990.
    • (1990) Cancer Metastasis Rev. , vol.9 , pp. 369-380
    • Lola, P.K.1    Graham, C.H.2
  • 32
    • 0021941053 scopus 로고
    • Cancer Metastasis: experimental approaches, theoretical concepts, and impacts for treatment strategies
    • Schirrmacher, V. Cancer Metastasis: experimental approaches, theoretical concepts, and impacts for treatment strategies. Adv. Cancer Res., 43: 1–73, 1985.
    • (1985) Adv. Cancer Res. , vol.43 , pp. 1-73
    • Schirrmacher, V.1
  • 33
    • 0027333420 scopus 로고
    • Life at the leading edge: the formation of cell protrusions
    • Condeelis, J. Life at the leading edge: the formation of cell protrusions. Annu. Rev. Physiol., 9: 411–444, 1993.
    • (1993) Annu. Rev. Physiol. , vol.9 , pp. 411-444
    • Condeelis, J.1
  • 34
    • 0027299745 scopus 로고
    • On the crawling of animal cells
    • Stossel, T. P. On the crawling of animal cells. Science (Washington DC), 260: 1086–1094, 1993.
    • (1993) Science (Washington DC) , vol.260 , pp. 1086-1094
    • Stossel, T.P.1
  • 35
    • 0023261034 scopus 로고
    • Cytokine-induced pseudopodial protrusion is coupled to tumour cell migration
    • Guirguis, R., Margulies, I., Taraboletti, G., and Liotta, L. Cytokine-induced pseudopodial protrusion is coupled to tumour cell migration. Nature (Lond.), 329: 261–263, 1987.
    • (1987) Nature (Lond.) , vol.329 , pp. 261-263
    • Guirguis, R.1    Margulies, I.2    Taraboletti, G.3    Liotta, L.4
  • 36
    • 0028319085 scopus 로고
    • Two phases of pseudopod protrusion in tumor cells revealed by a micropipette
    • Dong, C., Aznavoorian, S., and Liotta, L. A. Two phases of pseudopod protrusion in tumor cells revealed by a micropipette. Microvasc. Res., 47: 55–67, 1994.
    • (1994) Microvasc. Res. , vol.47 , pp. 55-67
    • Dong, C.1    Aznavoorian, S.2    Liotta, L.A.3
  • 37
    • 0026938957 scopus 로고
    • Signal transduction by integrin receptors for extracellular matrix: cooperation and processing of extracellular information
    • Damsky, C. H., and Werb, Z. Signal transduction by integrin receptors for extracellular matrix: cooperation and processing of extracellular information. Curr. Opin. Cell Biol., 4: 772–781, 1992.
    • (1992) Curr. Opin. Cell Biol. , vol.4 , pp. 772-781
    • Damsky, C.H.1    Werb, Z.2
  • 38
    • 0027550662 scopus 로고
    • Urokinase and urokinase receptor: a paracrine/autocrine system regulating cell migration and invasiveness
    • Blasi, F. Urokinase and urokinase receptor: a paracrine/autocrine system regulating cell migration and invasiveness. Bioessays, 15: 105–111, 1993.
    • (1993) Bioessays , vol.15 , pp. 105-111
    • Blasi, F.1
  • 39
    • 0028291737 scopus 로고
    • A matrix metalloproteinase expressed on the surface of invasive tumor cells
    • Sato, H., Takino, T., Yasunori, O., Cao, J., Shinagawa, E. Y., 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    Yasunori, O.3    Cao, J.4    Shinagawa, E.Y.5    Seiki, M.6
  • 40
    • 0027438302 scopus 로고
    • v-Src activates the expression of 92-kDa type IV collagenase gene through the AP-1 site and the GT box homologous to retinoblastoma control elements
    • Sato, H., Kita, M., and Seiki, M. v-Src activates the expression of 92-kDa type IV collagenase gene through the AP-1 site and the GT box homologous to retinoblastoma control elements. J. Biol. Chem., 268: 23460–23468, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 23460-23468
    • Sato, H.1    Kita, M.2    Seiki, M.3
  • 41
    • 0024556819 scopus 로고
    • Expression of human recombinant plasminogen activators enhances invasion and experimental metastasis of H-ras-transformed NIH 3T3 cells
    • Axelrod, J. H., Reich, R., and Mishkin, R. Expression of human recombinant plasminogen activators enhances invasion and experimental metastasis of H-ras-transformed NIH 3T3 cells. Mol. Cell. Biol., 9: 2133–2141, 1989.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 2133-2141
    • Axelrod, J.H.1    Reich, R.2    Mishkin, R.3
  • 42
    • 0025690427 scopus 로고
    • Cathepsin D: a protease involved in breast cancer metastasis
    • Rochefort, H., Capony, F., and Garcia, M. Cathepsin D: a protease involved in breast cancer metastasis. Cancer Metastasis Rev., 9: 321–331, 1990.
    • (1990) Cancer Metastasis Rev. , vol.9 , pp. 321-331
    • Rochefort, H.1    Capony, F.2    Garcia, M.3
  • 43
  • 45
    • 0025613301 scopus 로고
    • Influence of organ environment on extracellular matrix degradative activity and metastasis of human colon carcinoma cells
    • Nakajima, M., Morikawa, K., Fabra, A., et al. Influence of organ environment on extracellular matrix degradative activity and metastasis of human colon carcinoma cells. J. Natl. Cancer Inst., 82: 1890–1898, 1990.
    • (1990) J. Natl. Cancer Inst. , vol.82 , pp. 1890-1898
    • Nakajima, M.1    Morikawa, K.2    Fabra, A.3
  • 46
    • 0022969477 scopus 로고
    • Tumor invasion through the human amniotic membrane: requirement for a proteinase cascade
    • Mignatti, P., Robbins, E., and Rifkin, D. B. Tumor invasion through the human amniotic membrane: requirement for a proteinase cascade. Cell, 47: 487–498, 1986.
    • (1986) Cell , vol.47 , pp. 487-498
    • Mignatti, P.1    Robbins, E.2    Rifkin, D.B.3
  • 47
    • 0020416872 scopus 로고
    • Effect of the natural protease inhibitors and a chemoattractant on tumor invasion in vitro
    • Thorgeirsson, U. P., Liotta, L. A., Kalebic, T., et al. Effect of the natural protease inhibitors and a chemoattractant on tumor invasion in vitro. J. Natl. Cancer Inst., 69: 1049–1054, 1982.
    • (1982) J. Natl. Cancer Inst. , vol.69 , pp. 1049-1054
    • Thorgeirsson, U.P.1    Liotta, L.A.2    Kalebic, T.3
  • 48
    • 0025230509 scopus 로고
    • Metalloproteinases and their inhibitors in matrix remodeling
    • Matrisian, L. M. Metalloproteinases and their inhibitors in matrix remodeling. Trends Genet., 6: 121–125, 1990.
    • (1990) Trends Genet. , vol.6 , pp. 121-125
    • Matrisian, L.M.1
  • 49
    • 0024330327 scopus 로고
    • SV40-transformed human lung fibroblasts secrete a 92-kDa type IV collagenase which is identical to that secreted by normal human macrophages
    • Wilhelm, S. M., Collier, I. E., Marmer, B. L., et al. SV40-transformed human lung fibroblasts secrete a 92-kDa type IV collagenase which is identical to that secreted by normal human macrophages. J. Biol. Chem., 264: 17213–17221, 1989.
    • (1989) J. Biol. Chem. , vol.264 , pp. 17213-17221
    • Wilhelm, S.M.1    Collier, I.E.2    Marmer, B.L.3
  • 50
    • 0021232779 scopus 로고
    • Identification of the procollagen IV cleavage products produced by a specific tumor collagenase
    • Fessler, L., Duncan, K., and Tryggvason, K. Identification of the procollagen IV cleavage products produced by a specific tumor collagenase. J. Biol. Chem., 259: 9783–9789, 1984.
    • (1984) J. Biol. Chem. , vol.259 , pp. 9783-9789
    • Fessler, L.1    Duncan, K.2    Tryggvason, K.3
  • 51
    • 0024394212 scopus 로고
    • Tissue inhibitor of metalloproteinase (TIMP-2): a new member of the metalloproteinase inhibitor family
    • Stetler-Stevenson, W. G., Krutzsch, H. C., and Liotta, L. A. Tissue inhibitor of metalloproteinase (TIMP-2): a new member of the metalloproteinase inhibitor family. J. Biol. Chem., 264: 17374–17378, 1989.
    • (1989) J. Biol. Chem. , vol.264 , pp. 17374-17378
    • Stetler-Stevenson, W.G.1    Krutzsch, H.C.2    Liotta, L.A.3
  • 52
    • 0006506596 scopus 로고
    • Human 72-kilodalton type IV collagenase forms a complex with a tissue inhibitor of metalloproteinases designated TIMP-2
    • Goldberg, G. I., Marmer, B. L., Grant, G. A., et al. Human 72-kilodalton type IV collagenase forms a complex with a tissue inhibitor of metalloproteinases designated TIMP-2. Proc. Natl. Acad. Sci. USA, 86: 8207–8211, 1989.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 8207-8211
    • Goldberg, G.I.1    Marmer, B.L.2    Grant, G.A.3
  • 53
    • 0024325265 scopus 로고
    • Purification and characterization of two related but distinct metalloproteinase inhibitors secreted by bovine aortic endothelial cells
    • DeClerck, Y. A., Yean, T. D., Ratzkin, B. J., et al. Purification and characterization of two related but distinct metalloproteinase inhibitors secreted by bovine aortic endothelial cells. J. Biol. Chem., 264: 17445–17453, 1989.
    • (1989) J. Biol. Chem. , vol.264 , pp. 17445-17453
    • DeClerck, Y.A.1    Yean, T.D.2    Ratzkin, B.J.3
  • 54
    • 0019422999 scopus 로고
    • An inhibitor of collagenase from human amniotic fluid: purification, characterization, and action on metalloproteinases
    • Murphy, G., Cawston, T., and Reynolds, J. An inhibitor of collagenase from human amniotic fluid: purification, characterization, and action on metalloproteinases. Biochem. J., 195: 167–173, 1981.
    • (1981) Biochem. J. , vol.195 , pp. 167-173
    • Murphy, G.1    Cawston, T.2    Reynolds, J.3
  • 55
    • 0025816440 scopus 로고
    • Preferential inhibition of 72 kDa and 92 kDa gelatinases by TIMP-2
    • Howard, E. W., Bullen, E. C., and Banda, M. J. Preferential inhibition of 72 kDa and 92 kDa gelatinases by TIMP-2. J. Biol. Chem., 266: 13070–13075, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 13070-13075
    • Howard, E.W.1    Bullen, E.C.2    Banda, M.J.3
  • 56
    • 0024344882 scopus 로고
    • Expression of type IV collagenase and procollagen genes and its correlation with the tumorigenic, invasive and metastatic abilities of oncogene-transformed human bronchial epithelial cells
    • Ura, H., Bonfil, R. D., Reich, R., et al. Expression of type IV collagenase and procollagen genes and its correlation with the tumorigenic, invasive and metastatic abilities of oncogene-transformed human bronchial epithelial cells. Cancer Res., 49: 4615–4622, 1989.
    • (1989) Cancer Res. , vol.49 , pp. 4615-4622
    • Ura, H.1    Bonfil, R.D.2    Reich, R.3
  • 57
    • 0025262040 scopus 로고
    • Immunohistologic distribution of type IV collagenase in normal, benign, and malignant breast tissue
    • Monteagudo, C., Merino, M., San Juan, J., et al. Immunohistologic distribution of type IV collagenase in normal, benign, and malignant breast tissue. Am. J. Pathol., 136: 585–592, 1990.
    • (1990) Am. J. Pathol. , vol.136 , pp. 585-592
    • Monteagudo, C.1    Merino, M.2    San Juan, J.3
  • 58
    • 0025924794 scopus 로고
    • Increased expression of the 72 kDa type IV collagenase in human colonic adenocarcinoma
    • Levy, A., Cioce, V., Sobel, M. E., et al. Increased expression of the 72 kDa type IV collagenase in human colonic adenocarcinoma. Cancer Res., 51: 439–444, 1991.
    • (1991) Cancer Res. , vol.51 , pp. 439-444
    • Levy, A.1    Cioce, V.2    Sobel, M.E.3
  • 59
    • 0023696675 scopus 로고
    • Inhibition by recombinant tissue inhibitor of metalloproteinases of human amnion invasion and lung colonization by murine B16 F10 melanoma cells
    • Schultz, R. M., Silberman, S., Persky, B., et al. Inhibition by recombinant tissue inhibitor of metalloproteinases of human amnion invasion and lung colonization by murine B16 F10 melanoma cells. Cancer Res., 48: 5539–5545, 1988.
    • (1988) Cancer Res. , vol.48 , pp. 5539-5545
    • Schultz, R.M.1    Silberman, S.2    Persky, B.3
  • 60
    • 0024593647 scopus 로고
    • Antisense RNA-induced reduction in murine TIMP level confers oncogenicity on Swiss 3T3
    • Khokha, R., Waterhouse, P., Yagel, S., et al. Antisense RNA-induced reduction in murine TIMP level confers oncogenicity on Swiss 3T3. Science (Washington DC), 243: 947–950, 1989.
    • (1989) Science (Washington DC) , vol.243 , pp. 947-950
    • Khokha, R.1    Waterhouse, P.2    Yagel, S.3
  • 61
  • 62
    • 0026573378 scopus 로고
    • Inhibition of invasion and metastasis in cells transfected with an inhibitor of metalloproteinases
    • DeClerck, Y. A., Perez, N., Shimada, H., et al. Inhibition of invasion and metastasis in cells transfected with an inhibitor of metalloproteinases. Cancer Res., 52: 701–708, 1992.
    • (1992) Cancer Res. , vol.52 , pp. 701-708
    • DeClerck, Y.A.1    Perez, N.2    Shimada, H.3
  • 63
    • 0024504371 scopus 로고
    • In vitro angiogenesis on the human amniotic membrane: requirement for basic fibroblast growth factor-induced proteinases
    • Mignatti, P., Tsuboi, R., Robbins, E., and Rifkin, D. In vitro angiogenesis on the human amniotic membrane: requirement for basic fibroblast growth factor-induced proteinases. J. Cell Biol., 108: 671–682, 1989.
    • (1989) J. Cell Biol. , vol.108 , pp. 671-682
    • Mignatti, P.1    Tsuboi, R.2    Robbins, E.3    Rifkin, D.4
  • 64
    • 0027030103 scopus 로고
    • Eight synthetic inhibitors of bacterial and mammalian interstitial collagenases
    • Schwartz, M. A., and Van Wart, H. E. Eight synthetic inhibitors of bacterial and mammalian interstitial collagenases. Prog. Med. Chem., 29: 271–334, 1992.
    • (1992) Prog. Med. Chem. , vol.29 , pp. 271-334
    • Schwartz, M.A.1    Van Wart, H.E.2
  • 65
    • 0024493129 scopus 로고
    • The activation of human type IV collagenase proenzyme
    • Sequence identification of the major converstion product following orangomercurial activation.
    • Stetler-Stevenson, W. G., Krutzsch, H. C., Wacher, M. P., Margulies, I. M. K., and Liotta, L. A. The activation of human type IV collagenase proenzyme. Sequence identification of the major converstion product following orangomercurial activation. J. Biol. Chem., 264: 1353–1356, 1989.
    • (1989) J. Biol. Chem. , vol.264 , pp. 1353-1356
    • Stetler-Stevenson, W.G.1    Krutzsch, H.C.2    Wacher, M.P.3    Margulies, I.M.K.4    Liotta, L.A.5
  • 66
    • 0026762677 scopus 로고
    • Inhibition of tumor cell invasion by a highly conserved peptide sequence form the matrix metalloproteinase enzyme pro-segment
    • Melchiori, A., Albini, A., Ray, J. M., et al Inhibition of tumor cell invasion by a highly conserved peptide sequence form the matrix metalloproteinase enzyme pro-segment. Cancer Res., 52: 2353–2356, 1992.
    • (1992) Cancer Res. , vol.52 , pp. 2353-2356
    • Melchiori, A.1    Albini, A.2    Ray, J.M.3
  • 67
    • 0028004639 scopus 로고
    • Potent peptide inhibitors of stromelysin based on the prodomain region of matrix metalloproteinases
    • Fotouhi, N., Lugo, A., Visnick, M., Lusch, L., Walsky, R., Coffey, J. W., and Hanglow, A. C. Potent peptide inhibitors of stromelysin based on the prodomain region of matrix metalloproteinases. J. Biol. Chem., 269: 30227–30231, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30227-30231
    • Fotouhi, N.1    Lugo, A.2    Visnick, M.3    Lusch, L.4    Walsky, R.5    Coffey, J.W.6    Hanglow, A.C.7
  • 68
    • 0027994031 scopus 로고
    • Matrix metalloproteinase inhibitor BB-94 (Batimastat) inhibits human colon tumor growth and spread in a patient-like orthotopic model in nude mice
    • Wang, X., Fu, X., Brown, P. D., Crimmin, M. J., and Hoffman, R. M. Matrix metalloproteinase inhibitor BB-94 (Batimastat) inhibits human colon tumor growth and spread in a patient-like orthotopic model in nude mice. Cancer Res., 54: 4726–472S, 1994.
    • (1994) Cancer Res. , vol.54 , pp. 4726-472S
    • Wang, X.1    Fu, X.2    Brown, P.D.3    Crimmin, M.J.4    Hoffman, R.M.5
  • 69
    • 0028341420 scopus 로고
    • Inhibition of retinal growth cone activity by specific metalloproeinase inhibitors in vitro
    • Sheffield, J. B., Krasnopolsky, V., and Dehlinger, E. Inhibition of retinal growth cone activity by specific metalloproeinase inhibitors in vitro. Dev., Dynamics, 200: 79–88, 1994.
    • (1994) Dev., Dynamics , vol.200 , pp. 79-88
    • Sheffield, J.B.1    Krasnopolsky, V.2    Dehlinger, E.3
  • 70
    • 0027956746 scopus 로고
    • Inhibition of angiogenesis by the matrix metalloprotease inhibitor N-[2R-2-(hydroxamidocar-bonymethyl)-4-methylpentanoyl)]-L-tryptophan methylamide
    • Galardy, R., Grobelney, D., Foellmer, H. G., and Fernandez, L. A. Inhibition of angiogenesis by the matrix metalloprotease inhibitor N-[2R-2-(hydroxamidocar-bonymethyl)-4-methylpentanoyl)]-L-tryptophan methylamide. Cancer Res., 54: 4715–4718, 1994.
    • (1994) Cancer Res. , vol.54 , pp. 4715-4718
    • Galardy, R.1    Grobelney, D.2    Foellmer, H.G.3    Fernandez, L.A.4
  • 71
    • 0027251836 scopus 로고
    • A synthetic matrix metalloproteinase inhibitor decreases tumor burden and prolongs survival of mice bearing human ovarian carcinoma xenografts
    • Davies, B., Brown, P. D., East, N., Criinmin, M. J., and Balkwill, F. R. A synthetic matrix metalloproteinase inhibitor decreases tumor burden and prolongs survival of mice bearing human ovarian carcinoma xenografts. Cancer Res., 53: 2087–2091, 1993.
    • (1993) Cancer Res. , vol.53 , pp. 2087-2091
    • Davies, B.1    Brown, P.D.2    East, N.3    Criinmin, M.J.4    Balkwill, F.R.5
  • 72
    • 0023942517 scopus 로고
    • Growth factor receptor kinases
    • Yarden, Y., and Urlich, A. Growth factor receptor kinases. Annu. Rev. Biochem., 57: 443–478, 1988.
    • (1988) Annu. Rev. Biochem. , vol.57 , pp. 443-478
    • Yarden, Y.1    Urlich, A.2
  • 73
    • 0027439698 scopus 로고
    • Regulatory mechanism of 92 kDa type IV collagenase gene expression which is associated with invasiveness of tumor cell
    • Sato, H., and Seiki, M. Regulatory mechanism of 92 kDa type IV collagenase gene expression which is associated with invasiveness of tumor cell. Oncogene, 8: 385–405, 1993.
    • (1993) Oncogene , vol.8 , pp. 385-405
    • Sato, H.1    Seiki, M.2
  • 74
    • 0027665766 scopus 로고
    • Negative growth selection against rodent fibroblasts targeted for genetic inhibition of farnesyl transferase
    • Prendergast, G. C., Davide, J. P., Krai, A., Diehl, R., Gibbs, J. B., Omer, C. A., and Kohl, N. E. Negative growth selection against rodent fibroblasts targeted for genetic inhibition of farnesyl transferase. Cell Growth & Differ., 4: 707–713, 1993.
    • (1993) Cell Growth & Differ. , vol.4 , pp. 707-713
    • Prendergast, G.C.1    Davide, J.P.2    Krai, A.3    Diehl, R.4    Gibbs, J.B.5    Omer, C.A.6    Kohl, N.E.7
  • 75
    • 0027014526 scopus 로고
    • Drugs active against growth factor and oncogene phosphatidylinositol signaling pathways
    • Powis, G. Drugs active against growth factor and oncogene phosphatidylinositol signaling pathways. Semin. Cancer Biol., 3: 343–350, 1992.
    • (1992) Semin. Cancer Biol. , vol.3 , pp. 343-350
    • Powis, G.1
  • 76
    • 0027536464 scopus 로고
    • Protein kinase C: a novel target for inhibiting gastric cancer invasion
    • Schwartz, G. K., Jiang, J., Kelsen, D., and Albino, A. P. Protein kinase C: a novel target for inhibiting gastric cancer invasion. J. Natl. Cancer Inst, 85: 402–407, 1993.
    • (1993) J. Natl. Cancer Inst , vol.85 , pp. 402-407
    • Schwartz, G.K.1    Jiang, J.2    Kelsen, D.3    Albino, A.P.4
  • 77
    • 0025344028 scopus 로고
    • TGF-βl inhibition of transin/stromelysin gene expression is mediated through a fos binding sequence
    • Kerr, L. D., Miller, D. B., and Matrisian, L. M. TGF-βl inhibition of transin/stromelysin gene expression is mediated through a fos binding sequence. Cell, 61: 267–278, 1990.
    • (1990) Cell , vol.61 , pp. 267-278
    • Kerr, L.D.1    Miller, D.B.2    Matrisian, L.M.3
  • 78
    • 0025012854 scopus 로고
    • L651582, a novel antiproliferative and antimetastasis agent
    • Kohn, E. C., and Liotta, L. A. L651582, a novel antiproliferative and antimetastasis agent. J. Natl. Cancer Inst., 82: 54–60, 1990.
    • (1990) J. Natl. Cancer Inst. , vol.82 , pp. 54-60
    • Kohn, E.C.1    Liotta, L.A.2
  • 79
    • 0026740712 scopus 로고
    • In vivo efficacy of a novel inhibitor of selected signal transduction pathways including calcium, arachidonate, and inositol phosphates
    • Kohn, E. C., Sandeen, M. A., and Liotta, L. A. In vivo efficacy of a novel inhibitor of selected signal transduction pathways including calcium, arachidonate, and inositol phosphates. Cancer Res., 52: 3208–3212, 1992.
    • (1992) Cancer Res. , vol.52 , pp. 3208-3212
    • Kohn, E.C.1    Sandeen, M.A.2    Liotta, L.A.3
  • 80
    • 0028040432 scopus 로고
    • Calcium influx regulates matrix metalloproteinase-2 (72 kDa type IV collagenase, gelatinase A) expression
    • Kohn, E. C., Jacobs, W., Kim, Y. S., Alessandro, R., Stetler-Stevenson, W. G., and Liotta, L. A. Calcium influx regulates matrix metalloproteinase-2 (72 kDa type IV collagenase, gelatinase A) expression. J. Biol. Chem., 269: 21505–21511, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 21505-21511
    • Kohn, E.C.1    Jacobs, W.2    Kim, Y.S.3    Alessandro, R.4    Stetler-Stevenson, W.G.5    Liotta, L.A.6
  • 81
    • 0028205812 scopus 로고
    • Stucture-function analysis of signal and growth inhibition by carboxyamido-triazole, CAI
    • Kohn, E. C., Felder, C. C., Jacobs, W., Holmes, K. A., Day, A., Freer, R., and Liotta, L. A. Stucture-function analysis of signal and growth inhibition by carboxyamido-triazole, CAI. Cancer Res., 54: 935–942, 1994.
    • (1994) Cancer Res. , vol.54 , pp. 935-942
    • Kohn, E.C.1    Felder, C.C.2    Jacobs, W.3    Holmes, K.A.4    Day, A.5    Freer, R.6    Liotta, L.A.7
  • 83
    • 0027503305 scopus 로고
    • Muscarinic receptor-mediated tyrosine phosphorylation of phospholipase C-y: an alternative mechanism for cholinergic-induced phosphoinositide breakdown
    • Gusovsky, F., Lueders, J. E., Kohn, E. C., and Felder, C. C. Muscarinic receptor-mediated tyrosine phosphorylation of phospholipase C-y: an alternative mechanism for cholinergic-induced phosphoinositide breakdown. J. Biol. Chem., 268: 7768–7772, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 7768-7772
    • Gusovsky, F.1    Lueders, J.E.2    Kohn, E.C.3    Felder, C.C.4
  • 84
    • 0025772585 scopus 로고
    • The antiproliferative and antimetastatic compound L651582 inhibits muscarinic acetylcholine receptor-stimulated calcium influx and arachidonic acid release
    • Felder, C. C., Ma, A. L., Liotta, L. A., and Kohn, E. C. The antiproliferative and antimetastatic compound L651582 inhibits muscarinic acetylcholine receptor-stimulated calcium influx and arachidonic acid release. J. Pharmacol. Exp. Ther., 257: 967–971, 1991.
    • (1991) J. Pharmacol. Exp. Ther. , vol.257 , pp. 967-971
    • Felder, C.C.1    Ma, A.L.2    Liotta, L.A.3    Kohn, E.C.4
  • 85
    • 0024503541 scopus 로고
    • Tyrosine protein kinase activity of the EGF receptor is required to induce activation of receptor-operated calcium channels
    • Chapron, Y., Cochet, C., Crouzy, S., Jullien, T., Keramidas, M., and Verdetti, J. Tyrosine protein kinase activity of the EGF receptor is required to induce activation of receptor-operated calcium channels. Biochem. Biophys. Res. Commun., 158: 527–533, 1989.
    • (1989) Biochem. Biophys. Res. Commun. , vol.158 , pp. 527-533
    • Chapron, Y.1    Cochet, C.2    Crouzy, S.3    Jullien, T.4    Keramidas, M.5    Verdetti, J.6
  • 86
    • 0028274104 scopus 로고
    • Phosphoinositides and calcium as regulators of cellular actin assembly and disassembly
    • Janney, P. A. Phosphoinositides and calcium as regulators of cellular actin assembly and disassembly. Annu. Rev. Physiol., 56: 169–191, 1994.
    • (1994) Annu. Rev. Physiol. , vol.56 , pp. 169-191
    • Janney, P.A.1
  • 88
    • 0027521847 scopus 로고
    • Pathways of ras function: connections to the actin cytoskeleton
    • Prendergast, G. C., and Gibbs, J. B. Pathways of ras function: connections to the actin cytoskeleton. Adv. Cancer Res., 62: 19–64, 1993.
    • (1993) Adv. Cancer Res. , vol.62 , pp. 19-64
    • Prendergast, G.C.1    Gibbs, J.B.2
  • 90
    • 0027380135 scopus 로고
    • Reexpression of røi-encoded oncoprotein counteracts the tumor-suppressing but not the metastasis-suppressing function of E1A
    • Yu, D., Shi, D., Scanlon, M., and Hung, M. C. Reexpression of røi-encoded oncoprotein counteracts the tumor-suppressing but not the metastasis-suppressing function of E1A. Cancer Res., 53: 5784–5790, 1993.
    • (1993) Cancer Res. , vol.53 , pp. 5784-5790
    • Yu, D.1    Shi, D.2    Scanlon, M.3    Hung, M.C.4
  • 91
    • 0027406756 scopus 로고
    • Protein-tyrosine kinase p72syk is activated by thrombin and is negatively regulated through Cpa2+ regulation in platelets
    • Tanaguchi, T., Kitagawea, H., Yasue, S., et al. Protein-tyrosine kinase p72syk is activated by thrombin and is negatively regulated through Cpa2+ regulation in platelets. J. Biol. Chem., 268: 2277–2279, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 2277-2279
    • Tanaguchi, T.1    Kitagawea, H.2    Yasue, S.3
  • 92
    • 0026806502 scopus 로고
    • Type IV collagen stimulates an increase in intracellular calcium: potential role in tumor cell motility
    • Savarese, D. M. F., Russell, J. T., Fatatis, A., and Liotta, L. A. Type IV collagen stimulates an increase in intracellular calcium: potential role in tumor cell motility. J. Biol. Chem., 267: 21928–21935, 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 21928-21935
    • Savarese, D.M.F.1    Russell, J.T.2    Fatatis, A.3    Liotta, L.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.