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Volumn , Issue , 2010, Pages 53-76

Matrix Metalloproteinases and their Inhibitors - Friend or Foe

Author keywords

Invasive and metastatic activities of cancer cells contributing morbidity and mortality; Mammalian family of matrix metalloproteinases; Matrilysins, MMP 7 and MMP 26 roles in degradation and processing of ECM and non ECM proteins; Matrix metalloproteinases and their inhibitors friend or foe; MMP impact on tumor microenvironment and growth; Modulating change within physiologic and tumor microenvironment matrix metalloproteinases (MMPs) and tissue inhibitors of matrix metalloproteinases (TIMPs); Pleiotropic nature of MMPs diversity of functions in cancer progression; Targets and substrates of MMP action cellular or extracellular; Tissue inhibitors of matrix metalloproteinases; Tumor associated fibroblasts role in cancer progression and angiogenesis

Indexed keywords


EID: 84863674581     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9780470669891.ch4     Document Type: Chapter
Times cited : (3)

References (135)
  • 2
    • 0030454231 scopus 로고    scopus 로고
    • Rescue of mammary epithelial cell apoptosis and entactin degradation by a tissue inhibitor of metalloproteinases-1 transgene
    • Alexander, C.M., Howard, E.W., Bissell, M.J., and Werb, Z. (1996) Rescue of mammary epithelial cell apoptosis and entactin degradation by a tissue inhibitor of metalloproteinases-1 transgene. Journal of Cell Biology, 135, 1669-1677.
    • (1996) Journal of Cell Biology , vol.135 , pp. 1669-1677
    • Alexander, C.M.1    Howard, E.W.2    Bissell, M.J.3    Werb, Z.4
  • 3
    • 0025238632 scopus 로고
    • Inhibition of collagenolytic activity and metastasis of tumor cells by a recombinant human tissue inhibitor of metalloproteinases
    • Alvarez, O.A., Carmichael, D.F., and Declerck, Y.A. (1990) Inhibition of collagenolytic activity and metastasis of tumor cells by a recombinant human tissue inhibitor of metalloproteinases. Journal of National Cancer Institute, 82, 589-595.
    • (1990) Journal of National Cancer Institute , vol.82 , pp. 589-595
    • Alvarez, O.A.1    Carmichael, D.F.2    Declerck, Y.A.3
  • 4
    • 0032508675 scopus 로고    scopus 로고
    • TNF-alpha converting enzyme (TACE) is inhibited by TIMP-3
    • Amour, A., Slocombe, P.M., Webster, A. et al. (1998) TNF-alpha converting enzyme (TACE) is inhibited by TIMP-3. FEBS Letters, 435, 39-44.
    • (1998) FEBS Letters , vol.435 , pp. 39-44
    • Amour, A.1    Slocombe, P.M.2    Webster, A.3
  • 6
    • 0141731300 scopus 로고    scopus 로고
    • Dual stromelysin-3 function during natural mouse mammary tumor virus-ras tumor progression
    • Andarawewa, K.L., Boulay, A., Masson, R. et al. (2003) Dual stromelysin-3 function during natural mouse mammary tumor virus-ras tumor progression. Cancer Research, 63, 5844-5849.
    • (2003) Cancer Research , vol.63 , pp. 5844-5849
    • Andarawewa, K.L.1    Boulay, A.2    Masson, R.3
  • 7
    • 70350029581 scopus 로고    scopus 로고
    • Neutrophil MMP-9 proenzyme, unencumbered by TIMP-1, undergoes efficient activation in vivo and catalytically induces angiogenesis via a basic fibroblast growth factor (FGF-2)/FGFR-2 pathway
    • Ardi, V.C., Van Den Steen, P.E., Opdenakker, G. et al. (2009) Neutrophil MMP-9 proenzyme, unencumbered by TIMP-1, undergoes efficient activation in vivo and catalytically induces angiogenesis via a basic fibroblast growth factor (FGF-2)/FGFR-2 pathway. The Journal of Biological Chemistry, 284, 25854-25866.
    • (2009) The Journal of Biological Chemistry , vol.284 , pp. 25854-25866
    • Ardi, V.C.1    Van Den Steen, P.E.2    Opdenakker, G.3
  • 9
    • 0032974030 scopus 로고    scopus 로고
    • Inhibition of invasion and induction of apoptotic cell death of cancer cell lines by overexpression of TIMP-3
    • Baker, A.H., George, S.J., Zaltsman, A.B. et al. (1999) Inhibition of invasion and induction of apoptotic cell death of cancer cell lines by overexpression of TIMP-3. British Journal of Cancer, 79, 1347-1355.
    • (1999) British Journal of Cancer , vol.79 , pp. 1347-1355
    • Baker, A.H.1    George, S.J.2    Zaltsman, A.B.3
  • 10
    • 0141482154 scopus 로고    scopus 로고
    • Matrix metalloproteinases (MMP9 and MMP2) induce the release of vascular endothelial growth factor (VEGF) by ovarian carcinoma cells: implications for ascites formation
    • Belotti, D., Paganoni, P., Manenti, L. et al. (2003) Matrix metalloproteinases (MMP9 and MMP2) induce the release of vascular endothelial growth factor (VEGF) by ovarian carcinoma cells: implications for ascites formation. Cancer Research, 63, 5224-5229.
    • (2003) Cancer Research , vol.63 , pp. 5224-5229
    • Belotti, D.1    Paganoni, P.2    Manenti, L.3
  • 11
    • 72449139066 scopus 로고    scopus 로고
    • MMP-9 (gelatinase B) expression is associated with disease-free survival and disease-specific survival in colorectal cancer patients
    • Bendardaf, R., Buhmeida, A., Hilska, M. et al. (2010) MMP-9 (gelatinase B) expression is associated with disease-free survival and disease-specific survival in colorectal cancer patients. Cancer Investigation, 28, 38-43.
    • (2010) Cancer Investigation , vol.28 , pp. 38-43
    • Bendardaf, R.1    Buhmeida, A.2    Hilska, M.3
  • 12
    • 0000391746 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 triggers the angiogenic switch during carcinogenesis
    • Bergers, G., Brekken, R., Mcmahon, G. et al. (2000) Matrix metalloproteinase-9 triggers the angiogenic switch during carcinogenesis. Nature Cell Biology, 2, 737-744.
    • (2000) Nature Cell Biology , vol.2 , pp. 737-744
    • Bergers, G.1    Brekken, R.2    Mcmahon, G.3
  • 14
    • 0036350763 scopus 로고    scopus 로고
    • MMP-2 and TIMP-1 are derived from, not in response to, pancreatic cancer
    • Bloomston, M., Shafii, A., Zervos, E.E. et al. (2002) MMP-2 and TIMP-1 are derived from, not in response to, pancreatic cancer. Journal of Surgical Research, 102, 35-38.
    • (2002) Journal of Surgical Research , vol.102 , pp. 35-38
    • Bloomston, M.1    Shafii, A.2    Zervos, E.E.3
  • 16
    • 0034667462 scopus 로고    scopus 로고
    • Treatment of colorectal liver metastases by adenoviral transfer of tissue inhibitor of metalloproteinases-2 into the liver tissue
    • Brand, K., Baker, A.H., Perez-Canto, A. et al. (2000) Treatment of colorectal liver metastases by adenoviral transfer of tissue inhibitor of metalloproteinases-2 into the liver tissue. Cancer Research, 60, 5723-5730.
    • (2000) Cancer Research , vol.60 , pp. 5723-5730
    • Brand, K.1    Baker, A.H.2    Perez-Canto, A.3
  • 17
    • 0034615550 scopus 로고    scopus 로고
    • Tissue inhibitors of metalloproteinases: evolution, structure and function
    • Brew, K., Dinakarpandian, D., and Nagase, H. (2000) Tissue inhibitors of metalloproteinases: evolution, structure and function. Biochimica et Biophysica Acta, 1477, 267-283.
    • (2000) Biochimica et Biophysica Acta , vol.1477 , pp. 267-283
    • Brew, K.1    Dinakarpandian, D.2    Nagase, H.3
  • 18
    • 0035913171 scopus 로고    scopus 로고
    • Inhibition of Wilms' tumor growth by intramuscular administration of tissue inhibitor of metalloproteinases-4 plasmid DNA
    • Celiker, M.Y., Wang, M., Atsidaftos, E. et al. (2001) Inhibition of Wilms' tumor growth by intramuscular administration of tissue inhibitor of metalloproteinases-4 plasmid DNA. Oncogene, 20, 4337-4343.
    • (2001) Oncogene , vol.20 , pp. 4337-4343
    • Celiker, M.Y.1    Wang, M.2    Atsidaftos, E.3
  • 19
    • 0028850519 scopus 로고
    • Metalloproteinase inhibition and erythroid potentiation are independent activities of tissue inhibitor of metalloproteinases-1
    • Chesler, L., Golde, D.W., Bersch, N., and Johnson, M.D. (1995) Metalloproteinase inhibition and erythroid potentiation are independent activities of tissue inhibitor of metalloproteinases-1. Blood, 86, 4506-4515.
    • (1995) Blood , vol.86 , pp. 4506-4515
    • Chesler, L.1    Golde, D.W.2    Bersch, N.3    Johnson, M.D.4
  • 20
    • 0029035551 scopus 로고
    • Tissue inhibitor of metalloproteinase- 2 stimulates fibroblast proliferation via a cAMP-dependent mechanism
    • Corcoran, M.L. and Stetler-Stevenson, W.G. (1995) Tissue inhibitor of metalloproteinase- 2 stimulates fibroblast proliferation via a cAMP-dependent mechanism. The Journal of Biological Chemistry, 270, 13453-13459.
    • (1995) The Journal of Biological Chemistry , vol.270 , pp. 13453-13459
    • Corcoran, M.L.1    Stetler-Stevenson, W.G.2
  • 21
    • 0032534596 scopus 로고    scopus 로고
    • Matrix metalloproteinases generate angiostatin: effects on neovascularization
    • Cornelius, L.A., Nehring, L.C., Harding, E. et al. (1998) Matrix metalloproteinases generate angiostatin: effects on neovascularization. Journal of Immunology, 161, 6845-6852.
    • (1998) Journal of Immunology , vol.161 , pp. 6845-6852
    • Cornelius, L.A.1    Nehring, L.C.2    Harding, E.3
  • 22
    • 0037192458 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitors and cancer: trials and tribulations
    • Coussens, L.M., Fingleton, B., and Matrisian, L.M. (2002) Matrix metalloproteinase inhibitors and cancer: trials and tribulations. Science, 295, 2387-2392.
    • (2002) Science , vol.295 , pp. 2387-2392
    • Coussens, L.M.1    Fingleton, B.2    Matrisian, L.M.3
  • 23
    • 0034721666 scopus 로고    scopus 로고
    • MMP-9 supplied by bone marrow-derived cells contributes to skin carcinogenesis
    • Coussens, L.M., Tinkle, C.L., Hanahan, D., and Werb, Z. (2000) MMP-9 supplied by bone marrow-derived cells contributes to skin carcinogenesis. Cell, 103, 481-490.
    • (2000) Cell , vol.103 , pp. 481-490
    • Coussens, L.M.1    Tinkle, C.L.2    Hanahan, D.3    Werb, Z.4
  • 25
    • 0033019235 scopus 로고    scopus 로고
    • MMP-2 and TIMP-2 expression correlates with poor prognosis in cervical carcinoma-a clinicopathologic study using immunohistochemistry and mRNA in situ hybridization
    • Davidson, B., Goldberg, I., Kopolovic, J. et al. (1999) MMP-2 and TIMP-2 expression correlates with poor prognosis in cervical carcinoma-a clinicopathologic study using immunohistochemistry and mRNA in situ hybridization. Gynecologic Oncology, 73, 372-382.
    • (1999) Gynecologic Oncology , vol.73 , pp. 372-382
    • Davidson, B.1    Goldberg, I.2    Kopolovic, J.3
  • 26
    • 41949117906 scopus 로고    scopus 로고
    • Extracellular matrix mediates a molecular balance between vascular morphogenesis and regression
    • Davis, G.E. and Senger, D.R. (2008) Extracellular matrix mediates a molecular balance between vascular morphogenesis and regression. Current Opinion in Hematology, 15, 197-203.
    • (2008) Current Opinion in Hematology , vol.15 , pp. 197-203
    • Davis, G.E.1    Senger, D.R.2
  • 27
    • 34247341829 scopus 로고    scopus 로고
    • Proteomics discovery of metalloproteinase substrates in the cellular context by iTRAQ labeling reveals a diverse MMP-2 substrate degradome
    • Dean, R.A. and Overall, C.M. (2007) Proteomics discovery of metalloproteinase substrates in the cellular context by iTRAQ labeling reveals a diverse MMP-2 substrate degradome. Molecular and Cellular Proteomics, 6, 611-623.
    • (2007) Molecular and Cellular Proteomics , vol.6 , pp. 611-623
    • Dean, R.A.1    Overall, C.M.2
  • 30
    • 77049108176 scopus 로고    scopus 로고
    • Pleiotropic roles of matrix metalloproteinases in tumor angiogenesis: contrasting, overlapping and compensatory functions
    • Deryugina, E.I. and Quigley, J.P. (2010) Pleiotropic roles of matrix metalloproteinases in tumor angiogenesis: contrasting, overlapping and compensatory functions. Biochimica et Biophysica Acta, 1803 (1), 103-20.
    • (2010) Biochimica et Biophysica Acta , vol.1803 , Issue.1 , pp. 103-20
    • Deryugina, E.I.1    Quigley, J.P.2
  • 31
    • 0037081306 scopus 로고    scopus 로고
    • Up-regulation of vascular endothelial growth factor by membrane-type 1 matrix metalloproteinase stimulates human glioma xenograft growth and angiogenesis
    • Deryugina, E.I., Soroceanu, L., and Strongin, A.Y. (2002) Up-regulation of vascular endothelial growth factor by membrane-type 1 matrix metalloproteinase stimulates human glioma xenograft growth and angiogenesis. Cancer Research, 62, 580-588.
    • (2002) Cancer Research , vol.62 , pp. 580-588
    • Deryugina, E.I.1    Soroceanu, L.2    Strongin, A.Y.3
  • 32
    • 0022382006 scopus 로고
    • Sequence of human tissue inhibitor of metalloproteinases and its identity to erythroid-potentiating activity
    • Docherty, A.J., Lyons, A., Smith, B.J. et al. (1985) Sequence of human tissue inhibitor of metalloproteinases and its identity to erythroid-potentiating activity. Nature, 318, 66-69.
    • (1985) Nature , vol.318 , pp. 66-69
    • Docherty, A.J.1    Lyons, A.2    Smith, B.J.3
  • 33
    • 0036512208 scopus 로고    scopus 로고
    • New functions for the matrix metalloproteinases in cancer progression
    • Egeblad, M. and Werb, Z. (2002) New functions for the matrix metalloproteinases in cancer progression. Nature Reviews Cancer, 2, 161-174.
    • (2002) Nature Reviews Cancer , vol.2 , pp. 161-174
    • Egeblad, M.1    Werb, Z.2
  • 35
    • 77149137406 scopus 로고    scopus 로고
    • Matrix metalloproteinases: evolution, gene regulation and functional analysis in mouse models
    • Fanjul-Fernandez, M., Folgueras, A.R., Cabrera, S., and Lopez-Otin, C. (2010) Matrix metalloproteinases: evolution, gene regulation and functional analysis in mouse models. Biochimica et Biophysica Acta, 1803 (1), 3-19.
    • (2010) Biochimica et Biophysica Acta , vol.1803 , Issue.1 , pp. 3-19
    • Fanjul-Fernandez, M.1    Folgueras, A.R.2    Cabrera, S.3    Lopez-Otin, C.4
  • 36
    • 0032816628 scopus 로고    scopus 로고
    • Inhibition of endothelial cell migration by gene transfer of tissue inhibitor of metalloproteinases-1
    • Fernandez, H.A., Kallenbach, K., Seghezzi, G. et al. (1999) Inhibition of endothelial cell migration by gene transfer of tissue inhibitor of metalloproteinases-1. Journal of Surgical Research, 82, 156-162.
    • (1999) Journal of Surgical Research , vol.82 , pp. 156-162
    • Fernandez, H.A.1    Kallenbach, K.2    Seghezzi, G.3
  • 37
    • 84900056200 scopus 로고    scopus 로고
    • MMP inhibitor clinical trials-the past present, and future in
    • (eds D. Edwards G. Hoyer-Hansen F. Blasi and B.F. Sloane) Springer New York
    • Fingleton, B. (2008) MMP inhibitor clinical trials-the past, present, and future, in The Cancer Degradome (eds D. Edwards, G. Hoyer-Hansen, F. Blasi and B.F. Sloane), Springer, New York, pp. 759-785.
    • (2008) The Cancer Degradome , pp. 759-785
    • Fingleton, B.1
  • 38
    • 10344220521 scopus 로고    scopus 로고
    • Endogenous angiogenesis inhibitors
    • Folkman, J. (2004) Endogenous angiogenesis inhibitors. APMIS, 112, 496-507.
    • (2004) APMIS , vol.112 , pp. 496-507
    • Folkman, J.1
  • 40
    • 0028057613 scopus 로고
    • Disruption of epithelial cell-matrix interactions induces apoptosis
    • Frisch, S.M. and Francis, H. (1994) Disruption of epithelial cell-matrix interactions induces apoptosis. Journal of Cell Biology, 124, 619-626.
    • (1994) Journal of Cell Biology , vol.124 , pp. 619-626
    • Frisch, S.M.1    Francis, H.2
  • 41
    • 1642354112 scopus 로고    scopus 로고
    • ADAMTS4 (aggrecanase-1) activation on the cell surface involves C-terminal cleavage by glycosylphosphatidyl inositol-anchored membrane type 4-matrix metalloproteinase and binding of the activated proteinase to chondroitin sulfate and heparan sulfate on syndecan-1
    • Gao, G., Plaas, A., Thompson, V.P. et al. (2004) ADAMTS4 (aggrecanase-1) activation on the cell surface involves C-terminal cleavage by glycosylphosphatidyl inositol-anchored membrane type 4-matrix metalloproteinase and binding of the activated proteinase to chondroitin sulfate and heparan sulfate on syndecan-1. The Journal of Biological Chemistry, 279, 10042-10051.
    • (2004) The Journal of Biological Chemistry , vol.279 , pp. 10042-10051
    • Gao, G.1    Plaas, A.2    Thompson, V.P.3
  • 42
    • 76549092128 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 functions as a tumor suppressor in colitis-associated cancer
    • Garg, P., Sarma, D., Jeppsson, S. et al. (2010) Matrix metalloproteinase-9 functions as a tumor suppressor in colitis-associated cancer. Cancer Research, 70, 792-801.
    • (2010) Cancer Research , vol.70 , pp. 792-801
    • Garg, P.1    Sarma, D.2    Jeppsson, S.3
  • 44
    • 17144437129 scopus 로고    scopus 로고
    • Mouse macrophage metalloelastase gene transfer into a murine melanoma suppresses primary tumor growth by halting angiogenesis
    • Gorrin-Rivas, M.J., Arii, S., Furutani, M. et al. (2000) Mouse macrophage metalloelastase gene transfer into a murine melanoma suppresses primary tumor growth by halting angiogenesis. Clinical Cancer Research, 6, 1647-1654.
    • (2000) Clinical Cancer Research , vol.6 , pp. 1647-1654
    • Gorrin-Rivas, M.J.1    Arii, S.2    Furutani, M.3
  • 46
    • 0032529290 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinase (TIMP)-1 induces differentiation and an antiapoptotic phenotype in germinal center B cells.
    • Guedez, L., Courtemanch, L., and Stetler-Stevenson, M. (1998a) Tissue inhibitor of metalloproteinase (TIMP)-1 induces differentiation and an antiapoptotic phenotype in germinal center B cells. Blood, 92, 1342-1349.
    • (1998) Blood , vol.92 , pp. 1342-1349
    • Guedez, L.1    Courtemanch, L.2    Stetler-Stevenson, M.3
  • 47
    • 0032407788 scopus 로고    scopus 로고
    • In vitro suppression of programmed cell death of B cells by tissue inhibitor of metalloproteinases-1
    • Guedez, L., Stetler-Stevenson, W.G., Wolff, L. et al. (1998b) In vitro suppression of programmed cell death of B cells by tissue inhibitor of metalloproteinases-1. Journal of Clinical Investigation, 102, 2002-2010.
    • (1998) Journal of Clinical Investigation , vol.102 , pp. 2002-2010
    • Guedez, L.1    Stetler-Stevenson, W.G.2    Wolff, L.3
  • 48
    • 0035066974 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinase- 1 alters the tumorigenicity of Burkitt's lymphoma via divergent effects on tumor growth and angiogenesis
    • Guedez, L.,Mcmarlin, A.J., Kingma, D.W. et al. (2001) Tissue inhibitor of metalloproteinase- 1 alters the tumorigenicity of Burkitt's lymphoma via divergent effects on tumor growth and angiogenesis. American Journal of Pathology, 158, 1207-1215.
    • (2001) American Journal of Pathology , vol.158 , pp. 1207-1215
    • Guedez, L.1    Mcmarlin, A.J.2    Kingma, D.W.3
  • 49
    • 42349115927 scopus 로고    scopus 로고
    • Matrix metalloproteinase-8 functions as a metastasis suppressor through modulation of tumor cell adhesion and invasion
    • Gutierrez-Fernandez, A., Fueyo, A., Folgueras, A.R. et al. (2008) Matrix metalloproteinase-8 functions as a metastasis suppressor through modulation of tumor cell adhesion and invasion. Cancer Research, 68, 2755-2763.
    • (2008) Cancer Research , vol.68 , pp. 2755-2763
    • Gutierrez-Fernandez, A.1    Fueyo, A.2    Folgueras, A.R.3
  • 50
    • 0035110730 scopus 로고    scopus 로고
    • Overexpression of membrane-type matrix metalloproteinase-1 gene induces mammary gland abnormalities and adenocarcinoma in transgenic mice
    • Ha, H.Y., Moon, H.B., Nam, M.S. et al. (2001) Overexpression of membrane-type matrix metalloproteinase-1 gene induces mammary gland abnormalities and adenocarcinoma in transgenic mice. Cancer Research, 61, 984-990.
    • (2001) Cancer Research , vol.61 , pp. 984-990
    • Ha, H.Y.1    Moon, H.B.2    Nam, M.S.3
  • 51
    • 0028132867 scopus 로고
    • Cell growth-promoting activity of tissue inhibitor of metalloproteinases-2 (TIMP-2)
    • Hayakawa, T., Yamashita, K., Ohuchi, E., and Shinagawa, A. (1994) Cell growth-promoting activity of tissue inhibitor of metalloproteinases-2 (TIMP-2). Journal of Cell Science, 107 (Pt 9), 2373-2379.
    • (1994) Journal of Cell Science , vol.107 PT. 9 , pp. 2373-2379
    • Hayakawa, T.1    Yamashita, K.2    Ohuchi, E.3    Shinagawa, A.4
  • 52
    • 0033675417 scopus 로고    scopus 로고
    • Increased expression of tissue inhibitor ofmetalloproteinases type 1 (TIMP-1) in amore tumourigenic colon cancer cell line
    • Hewitt, R.E., Brown, K.E., Corcoran, M., and Stetler-Stevenson, W.G. (2000) Increased expression of tissue inhibitor ofmetalloproteinases type 1 (TIMP-1) in amore tumourigenic colon cancer cell line. Journal of Pathology, 192, 455-459.
    • (2000) Journal of Pathology , vol.192 , pp. 455-459
    • Hewitt, R.E.1    Brown, K.E.2    Corcoran, M.3    Stetler-Stevenson, W.G.4
  • 53
    • 33645323807 scopus 로고    scopus 로고
    • Imaging specific cell-surface proteolytic activity in single living cells
    • Hobson, J.P., Liu, S., Rono, B. et al. (2006) Imaging specific cell-surface proteolytic activity in single living cells. Nature Methods, 3, 259-261.
    • (2006) Nature Methods , vol.3 , pp. 259-261
    • Hobson, J.P.1    Liu, S.2    Rono, B.3
  • 54
    • 0034904186 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans: heavy hitters in the angiogenesis arena
    • Iozzo, R.V. and San Antonio, J.D. (2001) Heparan sulfate proteoglycans: heavy hitters in the angiogenesis arena. Journal of Clinical Investigation, 108, 349-355.
    • (2001) Journal of Clinical Investigation , vol.108 , pp. 349-355
    • Iozzo, R.V.1    San Antonio, J.D.2
  • 55
    • 28444454893 scopus 로고    scopus 로고
    • MT1-MMP: a potent modifier of pericellular microenvironment
    • Itoh, Y. and Seiki,M. (2006) MT1-MMP: a potent modifier of pericellular microenvironment. Journal of Cellular Physiology, 206, 1-8.
    • (2006) Journal of Cellular Physiology , vol.206 , pp. 1-8
    • Itoh, Y.1    Seiki, M.2
  • 56
    • 0035866816 scopus 로고    scopus 로고
    • Stimulation of mammary tumorigenesis by systemic tissue inhibitor of matrix metalloproteinase 4 gene delivery
    • Jiang, Y., Wang, M., Celiker, M.Y. et al. (2001) Stimulation of mammary tumorigenesis by systemic tissue inhibitor of matrix metalloproteinase 4 gene delivery. Cancer Research, 61, 2365-2370.
    • (2001) Cancer Research , vol.61 , pp. 2365-2370
    • Jiang, Y.1    Wang, M.2    Celiker, M.Y.3
  • 57
    • 0032835899 scopus 로고    scopus 로고
    • Expression of MMP-2 and MMP-9, their inhibitors, and the activator MT1-MMP in primary breast carcinomas
    • Jones, J.L., Glynn, P., and Walker, R.A. (1999) Expression of MMP-2 and MMP-9, their inhibitors, and the activator MT1-MMP in primary breast carcinomas. Journal of Pathology, 189, 161-168.
    • (1999) Journal of Pathology , vol.189 , pp. 161-168
    • Jones, J.L.1    Glynn, P.2    Walker, R.A.3
  • 58
    • 0034001460 scopus 로고    scopus 로고
    • Expression of tissue inhibitors of metalloproteinases (TIMPs) in gastric cancer
    • Joo, Y.E., Seo, K.S., Kim, H.S. et al. (2000) Expression of tissue inhibitors of metalloproteinases (TIMPs) in gastric cancer. Digestive Diseases and Science, 45, 114-121.
    • (2000) Digestive Diseases and Science , vol.45 , pp. 114-121
    • Joo, Y.E.1    Seo, K.S.2    Kim, H.S.3
  • 59
    • 33744940015 scopus 로고    scopus 로고
    • Earlier onset of tumoral angiogenesis in matrix metalloproteinase-19-deficient mice
    • Jost, M., Folgueras, A.R., Frerart, F. et al. (2006) Earlier onset of tumoral angiogenesis in matrix metalloproteinase-19-deficient mice. Cancer Research, 66, 5234-5241.
    • (2006) Cancer Research , vol.66 , pp. 5234-5241
    • Jost, M.1    Folgueras, A.R.2    Frerart, F.3
  • 60
    • 33748371637 scopus 로고    scopus 로고
    • Identification of CD63 as a tissue inhibitor of metalloproteinase-1 interacting cell surface protein
    • Jung, K.K., Liu, X.W., Chirco, R. et al. (2006) Identification of CD63 as a tissue inhibitor of metalloproteinase-1 interacting cell surface protein. EMBO Journal, 25, 3934-3942.
    • (2006) EMBO Journal , vol.25 , pp. 3934-3942
    • Jung, K.K.1    Liu, X.W.2    Chirco, R.3
  • 61
    • 0037805549 scopus 로고    scopus 로고
    • Basement membranes: structure, assembly and role in tumour angiogenesis
    • Kalluri, R. (2003) Basement membranes: structure, assembly and role in tumour angiogenesis. Nature Reviews Cancer, 3, 422-433.
    • (2003) Nature Reviews Cancer , vol.3 , pp. 422-433
    • Kalluri, R.1
  • 62
    • 0036772138 scopus 로고    scopus 로고
    • Metalloelastase (MMP-12) expression by tumour cells in squamous cell carcinoma of the vulva correlates with invasiveness, while that by macrophages predicts better outcome
    • Kerkela, E., Ala-Aho, R., Klemi, P. et al. (2002) Metalloelastase (MMP-12) expression by tumour cells in squamous cell carcinoma of the vulva correlates with invasiveness, while that by macrophages predicts better outcome. Journal of Pathology, 198, 258-269.
    • (2002) Journal of Pathology , vol.198 , pp. 258-269
    • Kerkela, E.1    Ala-Aho, R.2    Klemi, P.3
  • 63
    • 0028140295 scopus 로고
    • Suppression of the tumorigenic and metastatic abilities of murine B16-F10 melanoma cells in vivo by the overexpression of the tissue inhibitor of the metalloproteinases-1
    • Khokha, R. (1994) Suppression of the tumorigenic and metastatic abilities of murine B16-F10 melanoma cells in vivo by the overexpression of the tissue inhibitor of the metalloproteinases-1. Journal of the National Cancer Institute, 86, 299-304.
    • (1994) Journal of the National Cancer Institute , vol.86 , pp. 299-304
    • Khokha, R.1
  • 64
    • 0024593647 scopus 로고
    • Antisense RNA-induced reduction in murine TIMP levels confers oncogenicity on Swiss 3T3 cells
    • Khokha, R., Waterhouse, P., Yagel, S. et al. (1989) Antisense RNA-induced reduction in murine TIMP levels confers oncogenicity on Swiss 3T3 cells. Science, 243, 947-950.
    • (1989) Science , vol.243 , pp. 947-950
    • Khokha, R.1    Waterhouse, P.2    Yagel, S.3
  • 65
    • 0025744001 scopus 로고
    • Tissue inhibitor of metalloproteinases-1 (TIMP-1) RNA is expressed at elevated levels in malignant non- Hodgkin's lymphomas
    • Kossakowska, A.E., Urbanski, S.J., and Edwards, D.R. (1991) Tissue inhibitor of metalloproteinases-1 (TIMP-1) RNA is expressed at elevated levels in malignant non- Hodgkin's lymphomas. Blood, 77, 2475-2481.
    • (1991) Blood , vol.77 , pp. 2475-2481
    • Kossakowska, A.E.1    Urbanski, S.J.2    Edwards, D.R.3
  • 66
    • 59949092806 scopus 로고    scopus 로고
    • Functional genetic mouse models: promising tools for investigation of the proteolytic internet
    • Kruger, A. (2009) Functional genetic mouse models: promising tools for investigation of the proteolytic internet. Biological Chemistry, 390, 91-97.
    • (2009) Biological Chemistry , vol.390 , pp. 91-97
    • Kruger, A.1
  • 67
    • 59849109742 scopus 로고    scopus 로고
    • TIMP-1 binding to proMMP-9/CD44 complex localized at the cell surface promotes erythroid cell survival
    • Lambert, E., Bridoux, L., Devy, J. et al. (2009) TIMP-1 binding to proMMP-9/CD44 complex localized at the cell surface promotes erythroid cell survival. International Journal of Biochemistry and Cell Biology, 41, 1102-1115.
    • (2009) International Journal of Biochemistry and Cell Biology , vol.41 , pp. 1102-1115
    • Lambert, E.1    Bridoux, L.2    Devy, J.3
  • 69
    • 22344437713 scopus 로고    scopus 로고
    • Processing of VEGF-A by matrix metalloproteinases regulates bioavailability and vascular patterning in tumors
    • Lee, S., Jilani, S.M., Nikolova, G.V. et al. (2005) Processing of VEGF-A by matrix metalloproteinases regulates bioavailability and vascular patterning in tumors. Journal of Cell Biology, 169, 681-691.
    • (2005) Journal of Cell Biology , vol.169 , pp. 681-691
    • Lee, S.1    Jilani, S.M.2    Nikolova, G.V.3
  • 70
    • 0034749944 scopus 로고    scopus 로고
    • Matrix metalloproteinases: multifunctional effectors of inflammation in multiple sclerosis and bacterial meningitis
    • Leppert, D., Lindberg, R.L., Kappos, L., and Leib, S.L. (2001) Matrix metalloproteinases: multifunctional effectors of inflammation in multiple sclerosis and bacterial meningitis. Brain Research: Brain Research Reviews, 36, 249-257.
    • (2001) Brain Research: Brain Research Reviews , vol.36 , pp. 249-257
    • Leppert, D.1    Lindberg, R.L.2    Kappos, L.3    Leib, S.L.4
  • 71
    • 31544441610 scopus 로고    scopus 로고
    • Distinct role of macrophages in different tumor microenvironments
    • Lewis, C.E. and Pollard, J.W. (2006) Distinct role of macrophages in different tumor microenvironments. Cancer Research, 66, 605-612.
    • (2006) Cancer Research , vol.66 , pp. 605-612
    • Lewis, C.E.1    Pollard, J.W.2
  • 72
    • 0033572494 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinase-1 inhibits apoptosis of human breast epithelial cells
    • Li, G., Fridman, R., and Kim, H.R. (1999) Tissue inhibitor of metalloproteinase-1 inhibits apoptosis of human breast epithelial cells. Cancer Research, 59, 6267-6275.
    • (1999) Cancer Research , vol.59 , pp. 6267-6275
    • Li, G.1    Fridman, R.2    Kim, H.R.3
  • 73
    • 0141993985 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinase-1 protects human breast epithelial cells against intrinsic apoptotic cell death via the focal adhesion kinase/phosphatidylinositol 3-kinase and MAPK signaling pathway
    • Liu, X.W., Bernardo, M.M., Fridman, R., and Kim, H.R. (2003) Tissue inhibitor of metalloproteinase-1 protects human breast epithelial cells against intrinsic apoptotic cell death via the focal adhesion kinase/phosphatidylinositol 3-kinase and MAPK signaling pathway. The Journal of Biological Chemistry, 278, 40364-40372.
    • (2003) The Journal of Biological Chemistry , vol.278 , pp. 40364-40372
    • Liu, X.W.1    Bernardo, M.M.2    Fridman, R.3    Kim, H.R.4
  • 74
    • 13444311544 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinase-1 protects human breast epithelial cells from extrinsic cell death: a potential oncogenic activity of tissue inhibitor of metalloproteinase-1
    • Liu, X.W., Taube, M.E., Jung, K.K. et al. (2005) Tissue inhibitor of metalloproteinase-1 protects human breast epithelial cells from extrinsic cell death: a potential oncogenic activity of tissue inhibitor of metalloproteinase-1. Cancer Research, 65, 898-906.
    • (2005) Cancer Research , vol.65 , pp. 898-906
    • Liu, X.W.1    Taube, M.E.2    Jung, K.K.3
  • 75
    • 34648815810 scopus 로고    scopus 로고
    • Emerging roles of proteases in tumour suppression
    • Lopez-Otin, C. and Matrisian, L.M. (2007) Emerging roles of proteases in tumour suppression. Nature Reviews Cancer, 7, 800-808.
    • (2007) Nature Reviews Cancer , vol.7 , pp. 800-808
    • Lopez-Otin, C.1    Matrisian, L.M.2
  • 76
    • 0032211804 scopus 로고    scopus 로고
    • ECM signalling: orchestrating cell behaviour and misbehaviour
    • Lukashev, M.E. and Werb, Z. (1998) ECM signalling: orchestrating cell behaviour and misbehaviour. Trends in Cell Biology, 8, 437-441.
    • (1998) Trends in Cell Biology , vol.8 , pp. 437-441
    • Lukashev, M.E.1    Werb, Z.2
  • 77
    • 31744445961 scopus 로고    scopus 로고
    • Matrix metalloproteinases (MMPs) in health and disease: an overview
    • Malemud, C.J. (2006) Matrix metalloproteinases (MMPs) in health and disease: an overview. Frontiers in Bioscience, 11, 1696-1701.
    • (2006) Frontiers in Bioscience , vol.11 , pp. 1696-1701
    • Malemud, C.J.1
  • 78
    • 36148994693 scopus 로고    scopus 로고
    • The other side of MMPs: protective roles in tumor progression
    • Martin, M.D. and Matrisian, L.M. (2007) The other side of MMPs: protective roles in tumor progression. Cancer and Metastasis Reviews, 26, 717-724.
    • (2007) Cancer and Metastasis Reviews , vol.26 , pp. 717-724
    • Martin, M.D.1    Matrisian, L.M.2
  • 79
    • 0030051305 scopus 로고    scopus 로고
    • Transfection of an invasive human astrocytoma cell line with a TIMP-1 cDNA: modulation of astrocytoma invasive potential
    • Matsuzawa, K., Fukuyama, K., Hubbard, S.L. et al. (1996) Transfection of an invasive human astrocytoma cell line with a TIMP-1 cDNA: modulation of astrocytoma invasive potential. Journal of Neuropathology and Experimental Neurology, 55, 88-96.
    • (1996) Journal of Neuropathology and Experimental Neurology , vol.55 , pp. 88-96
    • Matsuzawa, K.1    Fukuyama, K.2    Hubbard, S.L.3
  • 80
    • 0032963210 scopus 로고    scopus 로고
    • High levels of tissue inhibitor of metalloproteinase-1 predict poor outcome in patients with breast cancer
    • Mccarthy, K., Maguire, T., Mcgreal, G. et al. (1999) High levels of tissue inhibitor of metalloproteinase-1 predict poor outcome in patients with breast cancer. International Journal of Cancer, 84, 44-48.
    • (1999) International Journal of Cancer , vol.84 , pp. 44-48
    • Mccarthy, K.1    Maguire, T.2    Mcgreal, G.3
  • 81
    • 0033047083 scopus 로고    scopus 로고
    • Expression and prognostic significance of metalloproteinases and their tissue inhibitors in patients with small-cell lung cancer
    • Michael, M., Babic, B., Khokha, R. et al. (1999) Expression and prognostic significance of metalloproteinases and their tissue inhibitors in patients with small-cell lung cancer. Journal of Clinical Oncology, 17, 1802-1808.
    • (1999) Journal of Clinical Oncology , vol.17 , pp. 1802-1808
    • Michael, M.1    Babic, B.2    Khokha, R.3
  • 82
    • 0027851841 scopus 로고
    • Erythroid potentiating activity of tissue inhibitor of metalloproteinases on the differentiation of erythropoietin-responsive mouse erythroleukemia cell line, ELM-I-1-3, is closely related to its cell growth potentiating activity
    • Murate, T., Yamashita, K., Ohashi, H. et al. (1993) Erythroid potentiating activity of tissue inhibitor of metalloproteinases on the differentiation of erythropoietin-responsive mouse erythroleukemia cell line, ELM-I-1-3, is closely related to its cell growth potentiating activity. Experimental Hematology, 21, 169-176.
    • (1993) Experimental Hematology , vol.21 , pp. 169-176
    • Murate, T.1    Yamashita, K.2    Ohashi, H.3
  • 83
    • 0027383944 scopus 로고
    • Tissue inhibitor of metalloproteinases-2 inhibits bFGF-induced human microvascular endothelial cell proliferation
    • Murphy, A.N., Unsworth, E.J., and Stetler-Stevenson, W.G. (1993) Tissue inhibitor of metalloproteinases-2 inhibits bFGF-induced human microvascular endothelial cell proliferation. Journal of Cellular Physiology, 157, 351-358.
    • (1993) Journal of Cellular Physiology , vol.157 , pp. 351-358
    • Murphy, A.N.1    Unsworth, E.J.2    Stetler-Stevenson, W.G.3
  • 84
    • 0025944065 scopus 로고
    • The N-terminal domain of tissue inhibitor of metalloproteinases retains metalloproteinase inhibitory activity
    • Murphy, G., Houbrechts, A., Cockett, M.I. et al. (1991) The N-terminal domain of tissue inhibitor of metalloproteinases retains metalloproteinase inhibitory activity. Biochemistry, 30, 8097-8102.
    • (1991) Biochemistry , vol.30 , pp. 8097-8102
    • Murphy, G.1    Houbrechts, A.2    Cockett, M.I.3
  • 85
    • 0027301930 scopus 로고
    • TIMP-2, a growth-stimulatory protein from SV40- transformed human fibroblasts
    • Nemeth, J.A. and Goolsby, C.L. (1993) TIMP-2, a growth-stimulatory protein from SV40- transformed human fibroblasts. Experimental Cell Research, 207, 376-382.
    • (1993) Experimental Cell Research , vol.207 , pp. 376-382
    • Nemeth, J.A.1    Goolsby, C.L.2
  • 86
    • 0033631262 scopus 로고    scopus 로고
    • Suppression of metastasis by tissue inhibitor of metalloproteinase-1 in a newly established human oral squamous cell carcinoma cell line
    • Nii, M., Kayada, Y., Yoshiga, K. et al. (2000) Suppression of metastasis by tissue inhibitor of metalloproteinase-1 in a newly established human oral squamous cell carcinoma cell line. International Journal of Oncology, 16, 119-124.
    • (2000) International Journal of Oncology , vol.16 , pp. 119-124
    • Nii, M.1    Kayada, Y.2    Yoshiga, K.3
  • 87
    • 0023721660 scopus 로고
    • In vivo effect of human erythroid-potentiating activity on hematopoiesis in mice
    • Niskanen, E., Gasson, J.C., Teates, C.D., and Golde, D.W. (1988) In vivo effect of human erythroid-potentiating activity on hematopoiesis in mice. Blood, 72, 806-810.
    • (1988) Blood , vol.72 , pp. 806-810
    • Niskanen, E.1    Gasson, J.C.2    Teates, C.D.3    Golde, D.W.4
  • 88
    • 20144379162 scopus 로고    scopus 로고
    • Endogenous inhibitors of angiogenesis
    • Nyberg, P., Xie, L., and Kalluri, R. (2005) Endogenous inhibitors of angiogenesis. Cancer Research, 65, 3967-3979.
    • (2005) Cancer Research , vol.65 , pp. 3967-3979
    • Nyberg, P.1    Xie, L.2    Kalluri, R.3
  • 89
    • 0027970092 scopus 로고
    • Angiostatin: a novel angiogenesis inhibitor that mediates the suppression of metastases by a Lewis lung carcinoma
    • O'Reilly, M.S., Holmgren, L., Shing, Y. et al. (1994) Angiostatin: a novel angiogenesis inhibitor that mediates the suppression of metastases by a Lewis lung carcinoma. Cell, 79, 315-328.
    • (1994) Cell , vol.79 , pp. 315-328
    • O'Reilly, M.S.1    Holmgren, L.2    Shing, Y.3
  • 90
    • 18244367390 scopus 로고    scopus 로고
    • The membrane-anchored MMP inhibitor RECK is a key regulator of extracellular matrix integrity and angiogenesis
    • Oh, J., Takahashi, R., Kondo, S. et al. (2001) The membrane-anchored MMP inhibitor RECK is a key regulator of extracellular matrix integrity and angiogenesis. Cell, 107, 789-800.
    • (2001) Cell , vol.107 , pp. 789-800
    • Oh, J.1    Takahashi, R.2    Kondo, S.3
  • 91
    • 58149288221 scopus 로고    scopus 로고
    • Direct visualization of protease activity on cells migrating in three-dimensions
    • Packard, B.Z., Artym, V.V., Komoriya, A., and Yamada, K.M. (2009) Direct visualization of protease activity on cells migrating in three-dimensions. Matrix Biology, 28, 3-10.
    • (2009) Matrix Biology , vol.28 , pp. 3-10
    • Packard, B.Z.1    Artym, V.V.2    Komoriya, A.3    Yamada, K.M.4
  • 92
    • 60649106195 scopus 로고    scopus 로고
    • Antiangiogenic therapy elicits malignant progression of tumors to increased local invasion and distant metastasis
    • Paez-Ribes, M., Allen, E., Hudock, J. et al. (2009) Antiangiogenic therapy elicits malignant progression of tumors to increased local invasion and distant metastasis. Cancer Cell, 15, 220-231.
    • (2009) Cancer Cell , vol.15 , pp. 220-231
    • Paez-Ribes, M.1    Allen, E.2    Hudock, J.3
  • 94
    • 15444352707 scopus 로고    scopus 로고
    • Angiostatin-converting enzyme activities of human matrilysin (MMP-7) and gelatinase B/type IV collagenase (MMP-9)
    • Patterson, B.C. and Sang, Q.A. (1997) Angiostatin-converting enzyme activities of human matrilysin (MMP-7) and gelatinase B/type IV collagenase (MMP-9). The Journal of Biological Chemistry, 272, 28823-28825.
    • (1997) The Journal of Biological Chemistry , vol.272 , pp. 28823-28825
    • Patterson, B.C.1    Sang, Q.A.2
  • 95
    • 0030904714 scopus 로고    scopus 로고
    • TIMP-3 mRNA expression is regionally increased in moderately and poorly differentiated colorectal adenocarcinoma
    • Powe, D.G., Brough, J.L., Carter, G.I. et al. (1997) TIMP-3 mRNA expression is regionally increased in moderately and poorly differentiated colorectal adenocarcinoma. British Journal of Cancer, 75, 1678-1683.
    • (1997) British Journal of Cancer , vol.75 , pp. 1678-1683
    • Powe, D.G.1    Brough, J.L.2    Carter, G.I.3
  • 97
    • 18144364350 scopus 로고    scopus 로고
    • Fibroblast growth factor/fibroblast growth factor receptor system in angiogenesis
    • Presta, M., Dell'era, P., Mitola, S. et al. (2005) Fibroblast growth factor/fibroblast growth factor receptor system in angiogenesis. Cytokine Growth Factor Reviews, 16, 159-178.
    • (2005) Cytokine Growth Factor Reviews , vol.16 , pp. 159-178
    • Presta, M.1    Dell'era, P.2    Mitola, S.3
  • 98
    • 0037393850 scopus 로고    scopus 로고
    • A novel function for tissue inhibitor of metalloproteinases-3 (TIMP3): inhibition of angiogenesis by blockage of VEGF binding to VEGF receptor-2
    • Qi, J.H., Ebrahem, Q., Moore, N. et al. (2003) A novel function for tissue inhibitor of metalloproteinases-3 (TIMP3): inhibition of angiogenesis by blockage of VEGF binding to VEGF receptor-2. Nature Medicine, 9, 407-415.
    • (2003) Nature Medicine , vol.9 , pp. 407-415
    • Qi, J.H.1    Ebrahem, Q.2    Moore, N.3
  • 99
    • 0033551186 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinases-1 (TIMP-1) binds to the cell surface and translocates to the nucleus of human MCF-7 breast carcinoma cells
    • Ritter, L.M., Garfield, S.H., and Thorgeirsson, U.P. (1999) Tissue inhibitor of metalloproteinases-1 (TIMP-1) binds to the cell surface and translocates to the nucleus of human MCF-7 breast carcinoma cells. Biochemical and Biophysical Research Communications, 257, 494-499.
    • (1999) Biochemical and Biophysical Research Communications , vol.257 , pp. 494-499
    • Ritter, L.M.1    Garfield, S.H.2    Thorgeirsson, U.P.3
  • 100
    • 77149164774 scopus 로고    scopus 로고
    • Matrix metalloproteinases: What do they not do? New substrates and biological roles identified by murine models and proteomics
    • Rodriguez, D., Morrison, C.J., and Overall, C.M. (2010) Matrix metalloproteinases: What do they not do? New substrates and biological roles identified by murine models and proteomics. Biochimica et Biophysica Acta, 1803 (1), 39-54.
    • (2010) Biochimica et Biophysica Acta , vol.1803 , Issue.1 , pp. 39-54
    • Rodriguez, D.1    Morrison, C.J.2    Overall, C.M.3
  • 102
    • 84886024652 scopus 로고    scopus 로고
    • Aggressive growth pattern of H2009 lung carcinoma following TIMP-1 overexpression in CNS metastasis model
    • Rojiani,M.V. and Rojiani, A.M. (2005) Aggressive growth pattern of H2009 lung carcinoma following TIMP-1 overexpression in CNS metastasis model. AACR Meeting Abstracts, Apr 2005, 38.
    • (2005) AACR Meeting Abstracts, Apr , vol.2005 , pp. 38
    • Rojiani, M.V.1    Rojiani, A.M.2
  • 103
    • 84885995609 scopus 로고    scopus 로고
    • Down-regulation of Thrombospondin-1 following TIMP-1 overexpression in lung carcinoma enhances angiogenesis
    • Rojiani, M.V. and Rojiani, A.M. (2006) Down-regulation of Thrombospondin-1 following TIMP-1 overexpression in lung carcinoma enhances angiogenesis. AACR Meeting Abstracts, Apr 2006, 655-656.
    • (2006) AACR Meeting Abstracts, Apr , vol.2006 , pp. 655-656
    • Rojiani, M.V.1    Rojiani, A.M.2
  • 104
    • 0030999633 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinase-1 and tissue inhibitor of metalloproteinase-2 expression in human amnion mesenchymal and epithelial cells
    • Rowe, T.F., King, L.A., Macdonald, P.C., and Casey, M.L. (1997) Tissue inhibitor of metalloproteinase-1 and tissue inhibitor of metalloproteinase-2 expression in human amnion mesenchymal and epithelial cells. American Journal ofObstetrics and Gynecology, 176, 915-921.
    • (1997) American Journal ofObstetrics and Gynecology , vol.176 , pp. 915-921
    • Rowe, T.F.1    King, L.A.2    Macdonald, P.C.3    Casey, M.L.4
  • 105
    • 65249155429 scopus 로고    scopus 로고
    • Protease-dependent versus -independent cancer cell invasion programs: three-dimensional amoeboid movement revisited
    • Sabeh, F., Shimizu-Hirota, R., andWeiss, S.J. (2009) Protease-dependent versus -independent cancer cell invasion programs: three-dimensional amoeboid movement revisited. Journal of Cell Biology, 185, 11-19.
    • (2009) Journal of Cell Biology , vol.185 , pp. 11-19
    • Sabeh, F.1    Shimizu-Hirota, R.2    Weiss, S.J.3
  • 106
    • 28044442504 scopus 로고    scopus 로고
    • Enzymatic remodeling of heparan sulfate proteoglycans within the tumor microenvironment: growth regulation and the prospect of new cancer therapies
    • Sanderson, R.D., Yang, Y., Kelly, T. et al. (2005) Enzymatic remodeling of heparan sulfate proteoglycans within the tumor microenvironment: growth regulation and the prospect of new cancer therapies. Journal of Cellular Biochemistry, 96, 897-905.
    • (2005) Journal of Cellular Biochemistry , vol.96 , pp. 897-905
    • Sanderson, R.D.1    Yang, Y.2    Kelly, T.3
  • 107
    • 0023696675 scopus 로고
    • Inhibition by human recombinant tissue inhibitor ofmetalloproteinases of human amnion invasion and lung colonization by murine B16-F10 melanoma cells
    • Schultz, R.M., Silberman, S., Persky, B. et al. (1988) Inhibition by human recombinant tissue inhibitor ofmetalloproteinases of human amnion invasion and lung colonization by murine B16-F10 melanoma cells. Cancer Research, 48, 5539-5545.
    • (1988) Cancer Research , vol.48 , pp. 5539-5545
    • Schultz, R.M.1    Silberman, S.2    Persky, B.3
  • 108
    • 0036775766 scopus 로고    scopus 로고
    • The cell surface: the stage for matrix metalloproteinase regulation of migration
    • Seiki, M. (2002) The cell surface: the stage for matrix metalloproteinase regulation of migration. Current Opinion in Cell Biology, 14, 624-632.
    • (2002) Current Opinion in Cell Biology , vol.14 , pp. 624-632
    • Seiki, M.1
  • 109
    • 0042197340 scopus 로고    scopus 로고
    • TIMP-2 mediated inhibition of angiogenesis: an MMP-independent mechanism
    • Seo, D.W., Li, H., Guedez, L. et al. (2003) TIMP-2 mediated inhibition of angiogenesis: an MMP-independent mechanism. Cell, 114, 171-180.
    • (2003) Cell , vol.114 , pp. 171-180
    • Seo, D.W.1    Li, H.2    Guedez, L.3
  • 111
    • 0033597726 scopus 로고    scopus 로고
    • The stromal proteinase MMP3/stromelysin-1 promotes mammary carcinogenesis
    • Sternlicht, M.D., Lochter, A., Sympson, C.J. et al. (1999) The stromal proteinase MMP3/stromelysin-1 promotes mammary carcinogenesis. Cell, 98, 137-146.
    • (1999) Cell , vol.98 , pp. 137-146
    • Sternlicht, M.D.1    Lochter, A.2    Sympson, C.J.3
  • 112
    • 0026601513 scopus 로고
    • Tissue inhibitor of metalloproteinase-2 (TIMP-2) has erythroid-potentiating activity
    • Stetler-Stevenson, W.G., Bersch, N., and Golde, D.W. (1992) Tissue inhibitor of metalloproteinase-2 (TIMP-2) has erythroid-potentiating activity. FEBS Letters, 296, 231-234.
    • (1992) FEBS Letters , vol.296 , pp. 231-234
    • Stetler-Stevenson, W.G.1    Bersch, N.2    Golde, D.W.3
  • 113
    • 0033989608 scopus 로고    scopus 로고
    • Localization and quantification of mRNA for matrix metalloproteinase-2 (MMP-2) and tissue inhibitor of matrix metalloproteinase-2 (TIMP-2) in human benign and malignant prostatic tissue
    • Still, K., Robson, C.N., Autzen, P. et al. (2000) Localization and quantification of mRNA for matrix metalloproteinase-2 (MMP-2) and tissue inhibitor of matrix metalloproteinase-2 (TIMP-2) in human benign and malignant prostatic tissue. Prostate, 42, 18-25.
    • (2000) Prostate , vol.42 , pp. 18-25
    • Still, K.1    Robson, C.N.2    Autzen, P.3
  • 114
    • 57649112725 scopus 로고    scopus 로고
    • Deletion of vascular endothelial growth factor in myeloid cells accelerates tumorigenesis
    • Stockmann, C., Doedens, A., Weidemann, A. et al. (2008) Deletion of vascular endothelial growth factor in myeloid cells accelerates tumorigenesis. Nature, 456, 814-818.
    • (2008) Nature , vol.456 , pp. 814-818
    • Stockmann, C.1    Doedens, A.2    Weidemann, A.3
  • 115
    • 0032545643 scopus 로고    scopus 로고
    • TIMP-2 over-expression reduces invasion and angiogenesis and protects B16F10 melanoma cells from apoptosis
    • Valente, P., Fassina, G., Melchiori, A. et al. (1998) TIMP-2 over-expression reduces invasion and angiogenesis and protects B16F10 melanoma cells from apoptosis. International Journal of Cancer, 75, 246-253.
    • (1998) International Journal of Cancer , vol.75 , pp. 246-253
    • Valente, P.1    Fassina, G.2    Melchiori, A.3
  • 116
    • 57749204989 scopus 로고    scopus 로고
    • Blood outgrowth endothelial cells from cord blood and peripheral blood: angiogenesis-related characteristics in vitro
    • Van Beem, R.T., Verloop, R.E., Kleijer, M. et al. (2009) Blood outgrowth endothelial cells from cord blood and peripheral blood: angiogenesis-related characteristics in vitro. Journal of Thrombosis and Haemostasis, 7, 217-226.
    • (2009) Journal of Thrombosis and Haemostasis , vol.7 , pp. 217-226
    • Van Beem, R.T.1    Verloop, R.E.2    Kleijer, M.3
  • 117
    • 42349114587 scopus 로고    scopus 로고
    • Endothelial sprouting and angiogenesis:matrix metalloproteinases in the lead
    • Van Hinsbergh, V.W. and Koolwijk, P. (2008) Endothelial sprouting and angiogenesis:matrix metalloproteinases in the lead. Cardiovascular Research, 78, 203-212.
    • (2008) Cardiovascular Research , vol.78 , pp. 203-212
    • Van Hinsbergh, V.W.1    Koolwijk, P.2
  • 118
    • 0028148301 scopus 로고
    • Enhanced expression of tissue inhibitor of metalloproteinase-2 (TIMP-2) in the stroma of breast carcinomas correlates with tumor recurrence
    • Visscher, D.W., Hoyhtya, M., Ottosen, S.K. et al. (1994) Enhanced expression of tissue inhibitor of metalloproteinase-2 (TIMP-2) in the stroma of breast carcinomas correlates with tumor recurrence. International Journal of Cancer, 59, 339-344.
    • (1994) International Journal of Cancer , vol.59 , pp. 339-344
    • Visscher, D.W.1    Hoyhtya, M.2    Ottosen, S.K.3
  • 119
    • 0030800299 scopus 로고    scopus 로고
    • Inhibition of tumor growth and metastasis of human breast cancer cells transfected with tissue inhibitor of metalloproteinase 4
    • Wang, M., Liu, Y.E., Greene, J. et al. (1997) Inhibition of tumor growth and metastasis of human breast cancer cells transfected with tissue inhibitor of metalloproteinase 4. Oncogene, 14, 2767-2774.
    • (1997) Oncogene , vol.14 , pp. 2767-2774
    • Wang, M.1    Liu, Y.E.2    Greene, J.3
  • 120
    • 0029998873 scopus 로고    scopus 로고
    • Inhibition of metastasis in human gastric cancer cells transfected with tissue inhibitor of metalloproteinase 1 gene in nude mice
    • Watanabe,M., Takahashi, Y., Ohta, T. et al. (1996) Inhibition of metastasis in human gastric cancer cells transfected with tissue inhibitor of metalloproteinase 1 gene in nude mice. Cancer, 77, 1676-1680.
    • (1996) Cancer , vol.77 , pp. 1676-1680
    • Watanabe, M.1    Takahashi, Y.2    Ohta, T.3
  • 121
    • 0033572338 scopus 로고    scopus 로고
    • The generation of endostatin is mediated by elastase
    • Wen, W., Moses, M.A., Wiederschain, D. et al. (1999) The generation of endostatin is mediated by elastase. Cancer Research, 59, 6052-6056.
    • (1999) Cancer Research , vol.59 , pp. 6052-6056
    • Wen, W.1    Moses, M.A.2    Wiederschain, D.3
  • 122
    • 0025341267 scopus 로고
    • Disulphide bond assignment in human tissue inhibitor of metalloproteinases (TIMP)
    • Williamson, R.A.,Marston, F.A., Angal, S. et al. (1990) Disulphide bond assignment in human tissue inhibitor of metalloproteinases (TIMP). Biochemical Journal, 268, 267-274.
    • (1990) Biochemical Journal , vol.268 , pp. 267-274
    • Williamson, R.A.1    Marston, F.A.2    Angal, S.3
  • 123
    • 0028284731 scopus 로고
    • Interferon effect on glycosaminoglycans in mouse glioma in vitro
    • Wiranowska, M. and Naidu, A.K. (1994) Interferon effect on glycosaminoglycans in mouse glioma in vitro. Journal of Neurooncology, 18, 9-17.
    • (1994) Journal of Neurooncology , vol.18 , pp. 9-17
    • Wiranowska, M.1    Naidu, A.K.2
  • 124
    • 77957046739 scopus 로고    scopus 로고
    • Cytokines and extracellular matrix remodeling in the central nervous system in
    • (eds C. Phelps and E.A. Korneva) Elsevier Edinburgh
    • Wiranowska, M., Plaas, A. (2008) Cytokines and extracellular matrix remodeling in the central nervous system, in NeuroImmune Biology (eds C. Phelps and E.A. Korneva), Elsevier, Edinburgh, pp. 167-197.
    • (2008) NeuroImmune Biology , pp. 167-197
    • Wiranowska, M.1    Plaas, A.2
  • 125
    • 0031789663 scopus 로고    scopus 로고
    • The effect of interferon and anti-CD44 antibody on mouse glioma invasiveness in vitro
    • Wiranowska, M., Tresser, N., and Saporta, S. (1998) The effect of interferon and anti-CD44 antibody on mouse glioma invasiveness in vitro. Anticancer Research, 18, 3331-3338.
    • (1998) Anticancer Research , vol.18 , pp. 3331-3338
    • Wiranowska, M.1    Tresser, N.2    Saporta, S.3
  • 126
    • 0034477147 scopus 로고    scopus 로고
    • CD44 expression and MMP-2 secretion by mouse glioma cells: effect of interferon and anti-CD44 antibody
    • Wiranowska, M., Rojiani, A.M., Gottschall, P., Moscinski, L., Johnson, J., and Saporta, S. (2000). CD44 expression and MMP-2 secretion by mouse glioma cells: effect of interferon and anti-CD44 antibody. Anticancer Research, 20, 4301-4306.
    • (2000) Anticancer Research , vol.20 , pp. 4301-4306
    • Wiranowska, M.1    Rojiani, A.M.2    Gottschall, P.3    Moscinski, L.4    Johnson, J.5    Saporta, S.6
  • 127
    • 35448988125 scopus 로고    scopus 로고
    • CD44 adhesion molecule and neuro-glial proteoglycan NG2 as invasive markers of glioma
    • Wiranowska, M., Ladd, S., Smith, S.R., and Gottschall, P.E. (2006) CD44 adhesion molecule and neuro-glial proteoglycan NG2 as invasive markers of glioma. Brain Cell Biology, 35, 159-172.
    • (2006) Brain Cell Biology , vol.35 , pp. 159-172
    • Wiranowska, M.1    Ladd, S.2    Smith, S.R.3    Gottschall, P.E.4
  • 128
    • 0037455576 scopus 로고    scopus 로고
    • Compensation mechanism in tumor cell migration: mesenchymal-amoeboid transition after blocking of pericellular proteolysis
    • Wolf, K.,Mazo, I., Leung, H. et al. (2003) Compensation mechanism in tumor cell migration: mesenchymal-amoeboid transition after blocking of pericellular proteolysis. Journal of Cell Biology, 160, 267-277.
    • (2003) Journal of Cell Biology , vol.160 , pp. 267-277
    • Wolf, K.1    Mazo, I.2    Leung, H.3
  • 129
    • 34547569807 scopus 로고    scopus 로고
    • Multi-step pericellular proteolysis controls the transition from individual to collective cancer cell invasion
    • Wolf, K., Wu, Y.I., Liu, Y. et al. (2007) Multi-step pericellular proteolysis controls the transition from individual to collective cancer cell invasion. Nature Cell Biology, 9, 893-904.
    • (2007) Nature Cell Biology , vol.9 , pp. 893-904
    • Wolf, K.1    Wu, Y.I.2    Liu, Y.3
  • 130
    • 0034746688 scopus 로고    scopus 로고
    • TIMP-1 promotes VEGF-induced neovascularization in the retina
    • Yamada, E., Tobe, T., Yamada, H. et al. (2001) TIMP-1 promotes VEGF-induced neovascularization in the retina. Histology and Histopathology, 16, 87-97.
    • (2001) Histology and Histopathology , vol.16 , pp. 87-97
    • Yamada, E.1    Tobe, T.2    Yamada, H.3
  • 132
    • 0029977663 scopus 로고    scopus 로고
    • Enhanced RNA expression of tissue inhibitor of metalloproteinases-1 (TIMP-1) in human breast cancer
    • Yoshiji, H., Gomez, D.E., and Thorgeirsson, U.P. (1996) Enhanced RNA expression of tissue inhibitor of metalloproteinases-1 (TIMP-1) in human breast cancer. International Journal of Cancer, 69, 131-134.
    • (1996) International Journal of Cancer , vol.69 , pp. 131-134
    • Yoshiji, H.1    Gomez, D.E.2    Thorgeirsson, U.P.3
  • 133
    • 0032484529 scopus 로고    scopus 로고
    • Mammary carcinoma cells over-expressing tissue inhibitor of metalloproteinases-1 show enhanced vascular endothelial growth factor expression
    • Yoshiji, H., Harris, S.R., Raso, E. et al. (1998) Mammary carcinoma cells over-expressing tissue inhibitor of metalloproteinases-1 show enhanced vascular endothelial growth factor expression. International Journal of Cancer, 75, 81-87.
    • (1998) International Journal of Cancer , vol.75 , pp. 81-87
    • Yoshiji, H.1    Harris, S.R.2    Raso, E.3
  • 134
    • 0032926177 scopus 로고    scopus 로고
    • Localization of matrix metalloproteinase 9 to the cell surface provides a mechanism for CD44-mediated tumor invasion
    • Yu, Q. and Stamenkovic, I. (1999) Localization of matrix metalloproteinase 9 to the cell surface provides a mechanism for CD44-mediated tumor invasion. Genes Development, 13, 35-48.
    • (1999) Genes Development , vol.13 , pp. 35-48
    • Yu, Q.1    Stamenkovic, I.2
  • 135
    • 0029079752 scopus 로고
    • Elevated tissue inhibitor of metalloproteinase 1 RNA in colorectal cancer stroma correlates with lymph node and distant metastases
    • Zeng, Z.S., Cohen, A.M., Zhang, Z.F. et al. (1995) Elevated tissue inhibitor of metalloproteinase 1 RNA in colorectal cancer stroma correlates with lymph node and distant metastases. Clinical Cancer Research, 1, 899-906.
    • (1995) Clinical Cancer Research , vol.1 , pp. 899-906
    • Zeng, Z.S.1    Cohen, A.M.2    Zhang, Z.F.3


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