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Volumn 77, Issue 7, 1999, Pages 465-480

Physiological roles of matrix metalloproteinases: Implications for tumor growth and metastasis

Author keywords

Cancer; Cell invasion; Extracellular matrix; Matrix metalloproteinases; Physiology

Indexed keywords

COLLAGENASE; GELATINASE A; GELATINASE B; MATRIX METALLOPROTEINASE; STROMELYSIN;

EID: 0032709474     PISSN: 00084212     EISSN: None     Source Type: Journal    
DOI: 10.1139/y99-055     Document Type: Review
Times cited : (144)

References (144)
  • 1
    • 0027981004 scopus 로고
    • Collagenase during burn wound healing: Influence of a hydrogel dressing and pulsed electrical stimulation
    • Agren, M.S., Engel, M.A., and Mertz, P.M. 1994. Collagenase during burn wound healing: influence of a hydrogel dressing and pulsed electrical stimulation. Plast. Reconstr. Surg. 94: 518-524.
    • (1994) Plast. Reconstr. Surg. , vol.94 , pp. 518-524
    • Agren, M.S.1    Engel, M.A.2    Mertz, P.M.3
  • 2
    • 0028085533 scopus 로고
    • Stromelysin-3 in stromal tissue as a control factor in breast cancer behavior
    • Basset, P., Wolf, C., Rouyer, N., Bellocq, J.P., Rio, M.C., and Chambon, P. 1994. Stromelysin-3 in stromal tissue as a control factor in breast cancer behavior. Cancer, 74(3 Suppl.): 1045-1049.
    • (1994) Cancer , vol.74 , Issue.3 SUPPL. , pp. 1045-1049
    • Basset, P.1    Wolf, C.2    Rouyer, N.3    Bellocq, J.P.4    Rio, M.C.5    Chambon, P.6
  • 4
    • 0030932125 scopus 로고    scopus 로고
    • The AP-1 site and MMP gene regulation: What is all the fuss about?
    • Benbow, U., and Brinckerhoff, C.E. 1997. The AP-1 site and MMP gene regulation: what is all the fuss about? Matrix Biol. 15: 515-526.
    • (1997) Matrix Biol. , vol.15 , pp. 515-526
    • Benbow, U.1    Brinckerhoff, C.E.2
  • 5
    • 0028346025 scopus 로고
    • Direct evidence linking expression of matrix metalloproteinase 9 (92-kDa gelatinase/collagenase) to the metastatic phenotype in transformed rat embryo cells
    • Bernhard, E.J., Gruber, S.B., and Muschel, R.J. 1994. Direct evidence linking expression of matrix metalloproteinase 9 (92-kDa gelatinase/collagenase) to the metastatic phenotype in transformed rat embryo cells. Proc. Natl. Acad. Sci. U.S.A. 91: 4293-4297.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 4293-4297
    • Bernhard, E.J.1    Gruber, S.B.2    Muschel, R.J.3
  • 7
    • 0025286753 scopus 로고
    • Tumor interactions with the vasculature: Angiogenesis and tumor metastasis
    • Blood, C.H., and Zetter, B.R. 1990. Tumor interactions with the vasculature: angiogenesis and tumor metastasis. Biochim. Biophys. Acta, 1032: 89-118.
    • (1990) Biochim. Biophys. Acta , vol.1032 , pp. 89-118
    • Blood, C.H.1    Zetter, B.R.2
  • 8
    • 0026091412 scopus 로고
    • Joint destruction in arthritis: Metalloproteinases in the spotlight
    • Brinckerhoff, C.E. 1991. Joint destruction in arthritis: metalloproteinases in the spotlight. Arthritis Rheum. 34: 1073-1075.
    • (1991) Arthritis Rheum. , vol.34 , pp. 1073-1075
    • Brinckerhoff, C.E.1
  • 10
    • 0010712792 scopus 로고    scopus 로고
    • Disruption of angiogenesis by PEX, a noncatalytic metalloproteinase fragment with integrin binding activity
    • Brooks, P.C., Silletti, S., von Schalscha, T.L., Friedlander, M., and Cheresh, D.A. 1998. Disruption of angiogenesis by PEX, a noncatalytic metalloproteinase fragment with integrin binding activity. Cell, 92: 391-400.
    • (1998) Cell , vol.92 , pp. 391-400
    • Brooks, P.C.1    Silletti, S.2    Von Schalscha, T.L.3    Friedlander, M.4    Cheresh, D.A.5
  • 11
    • 0025035989 scopus 로고
    • Independent expression and cellular processing of Mr 72,000 type IV collagenase and interstitial collagenase in human tumorigenic cell lines
    • Brown, P.D., Levy, A.T., Margulies, I.M., Liotta, L.A., and Stetler-Stevenson, W.G. 1990. Independent expression and cellular processing of Mr 72,000 type IV collagenase and interstitial collagenase in human tumorigenic cell lines. Cancer Res. 50: 6184-6191.
    • (1990) Cancer Res. , vol.50 , pp. 6184-6191
    • Brown, P.D.1    Levy, A.T.2    Margulies, I.M.3    Liotta, L.A.4    Stetler-Stevenson, W.G.5
  • 13
    • 0025168071 scopus 로고
    • Regulation of fibrillar collagen types I and III and basement membrane type IV collagen gene expression in hypertrophied rat myocardium
    • Chapman, D., Weber, K.T., and Eghbali, M. 1990. Regulation of fibrillar collagen types I and III and basement membrane type IV collagen gene expression in hypertrophied rat myocardium. Circ. Res. 67: 787-794.
    • (1990) Circ. Res. , vol.67 , pp. 787-794
    • Chapman, D.1    Weber, K.T.2    Eghbali, M.3
  • 14
    • 0031954519 scopus 로고    scopus 로고
    • Death to a blood vessel, death to a tumor
    • Cheresh, D.A. 1998. Death to a blood vessel, death to a tumor. Nat. Med. 4: 395-396.
    • (1998) Nat. Med. , vol.4 , pp. 395-396
    • Cheresh, D.A.1
  • 15
    • 0026096865 scopus 로고
    • On the structure and chromosome location of the 72- and 92-kDa human type IV collagenase genes
    • Collier, I.E., Brans, G.A.P., Goldberg, G.I., and Gerhard, D.S. 1991. On the structure and chromosome location of the 72- and 92-kDa human type IV collagenase genes. Genomics, 9: 429-434.
    • (1991) Genomics , vol.9 , pp. 429-434
    • Collier, I.E.1    Brans, G.A.P.2    Goldberg, G.I.3    Gerhard, D.S.4
  • 18
    • 0029899015 scopus 로고    scopus 로고
    • Mechanisms controlling the transcription of matrix metalloproteinase genes in normal and neoplastic cells
    • Crawford, H.C., and Matrisian, L.M. 1996. Mechanisms controlling the transcription of matrix metalloproteinase genes in normal and neoplastic cells. Enzyme Protein, 49: 20-37.
    • (1996) Enzyme Protein , vol.49 , pp. 20-37
    • Crawford, H.C.1    Matrisian, L.M.2
  • 19
    • 0025339737 scopus 로고
    • Alpha2-macroglobulin and tissue inhibitor of metalloproteinases: Collagenase inhibitors in human preovulatory ovaries
    • Curry, T.E., Jr., Mann, J.S., Estes, R.S., and Jones P.B.C. 1990. Alpha2-macroglobulin and tissue inhibitor of metalloproteinases: collagenase inhibitors in human preovulatory ovaries. Endocrinology, 127: 63-68.
    • (1990) Endocrinology , vol.127 , pp. 63-68
    • Curry T.E., Jr.1    Mann, J.S.2    Estes, R.S.3    Jones, P.B.C.4
  • 20
    • 0029907622 scopus 로고    scopus 로고
    • The expression of tissue-type plasminogen activator, matrix metalloproteases and endogenous inhibitors in the central nervous system in multiple sclerosis: Comparison of stages in lesion evolution
    • Cuzner, M.L., Gveric, D., Strand, C., Loughlin, A.J., Paemen, L., Opdenakker, G., and Newcombe, J. 1996. The expression of tissue-type plasminogen activator, matrix metalloproteases and endogenous inhibitors in the central nervous system in multiple sclerosis: comparison of stages in lesion evolution. J. Neuropathol. Exp. Neurol. 55: 1194-1204.
    • (1996) J. Neuropathol. Exp. Neurol. , vol.55 , pp. 1194-1204
    • Cuzner, M.L.1    Gveric, D.2    Strand, C.3    Loughlin, A.J.4    Paemen, L.5    Opdenakker, G.6    Newcombe, J.7
  • 21
    • 0026461115 scopus 로고
    • Collagenase expression in the lungs of transgenic mice causes pulmonary emphysema
    • D'Armiento, J., Dalal, S.S., Okada, Y., Berg, R.A., and Chada, K. 1992. Collagenase expression in the lungs of transgenic mice causes pulmonary emphysema. Cell, 71: 955-961.
    • (1992) Cell , vol.71 , pp. 955-961
    • D'Armiento, J.1    Dalal, S.S.2    Okada, Y.3    Berg, R.A.4    Chada, K.5
  • 22
    • 0029122808 scopus 로고
    • Collagenase expression in transgenic mouse skin causes hyperkeratosis and acanthosis and increases susceptibility to tumorigenesis
    • D'Armiento, J., DiColandrea, T., Dalal, S.S., Okada, Y., Huang, M.T., Conney, A.H., and Chada, K. 1995. Collagenase expression in transgenic mouse skin causes hyperkeratosis and acanthosis and increases susceptibility to tumorigenesis. Mol. Cell. Biol. 15: 5732-5739.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 5732-5739
    • D'Armiento, J.1    DiColandrea, T.2    Dalal, S.S.3    Okada, Y.4    Huang, M.T.5    Conney, A.H.6    Chada, K.7
  • 23
    • 0024712236 scopus 로고
    • Evidence for metalloproteinase and metalloproteinase inhibitor imbalance in human osteoarthritic cartilage
    • Dean, D.D., Martel-Pelletier, J., Pelletier, J.P., Howell, D.S., and Woessner, J.F., Jr. 1989. Evidence for metalloproteinase and metalloproteinase inhibitor imbalance in human osteoarthritic cartilage. J. Clin. Invest. 84: 678-685.
    • (1989) J. Clin. Invest. , vol.84 , pp. 678-685
    • Dean, D.D.1    Martel-Pelletier, J.2    Pelletier, J.P.3    Howell, D.S.4    Woessner J.F., Jr.5
  • 24
    • 0029988699 scopus 로고    scopus 로고
    • Increased production of matrix metalloproteinases in enriched astrocyte and mixed hippocampal cultures treated with beta-amyloid peptides
    • Deb, S., and Gottschall, P.E. 1996. Increased production of matrix metalloproteinases in enriched astrocyte and mixed hippocampal cultures treated with beta-amyloid peptides. J. Neurochem. 66: 1641-1647.
    • (1996) J. Neurochem. , vol.66 , pp. 1641-1647
    • Deb, S.1    Gottschall, P.E.2
  • 25
    • 0029999334 scopus 로고    scopus 로고
    • Cooperation between matrix metalloproteinases and the plasminogen activator - Plasmin system in tumor progression
    • DeClerck, Y.A., and Laug, W.E. 1996. Cooperation between matrix metalloproteinases and the plasminogen activator - plasmin system in tumor progression. Enzyme Protein, 49: 72-84.
    • (1996) Enzyme Protein , vol.49 , pp. 72-84
    • DeClerck, Y.A.1    Laug, W.E.2
  • 26
    • 0026573378 scopus 로고
    • Inhibition of invasion and metastasis in cells transfected with an inhibitor of metalloproteinases
    • DeClerck, Y.A., Perez, N., Shimada, H., Boone, T.C., Langley, K.E., and Taylor, S.M. 1992. Inhibition of invasion and metastasis in cells transfected with an inhibitor of metalloproteinases. Cancer Res. 52: 701-708.
    • (1992) Cancer Res. , vol.52 , pp. 701-708
    • DeClerck, Y.A.1    Perez, N.2    Shimada, H.3    Boone, T.C.4    Langley, K.E.5    Taylor, S.M.6
  • 27
    • 0009486526 scopus 로고    scopus 로고
    • Expression of matrix metalloproteinases and their inhibitors in human brain tumors. Anti-cancer proteins and drugs: Structure, function and design
    • In press
    • Delbecchi, L., Beaulieu, E., Mousseau, N., Moudjan, R., Del Maestro, X., and Béliveau, R. 1998. Expression of matrix metalloproteinases and their inhibitors in human brain tumors. Anti-cancer proteins and drugs: structure, function and design. N.Y. Acad. Sci. In press.
    • (1998) N.Y. Acad. Sci.
    • Delbecchi, L.1    Beaulieu, E.2    Mousseau, N.3    Moudjan, R.4    Del Maestro, X.5    Béliveau, R.6
  • 28
    • 0031606328 scopus 로고    scopus 로고
    • Purification and sequencing of a 21 kDa and 25 kDa bovine enamel metalloproteinase
    • Den Besten, P.K., Punzi, J.S., and Li, W. 1998. Purification and sequencing of a 21 kDa and 25 kDa bovine enamel metalloproteinase. Eur. J. Oral Sci. 106(Suppl. 1): 345-349.
    • (1998) Eur. J. Oral Sci. , vol.106 , Issue.SUPPL. 1 , pp. 345-349
    • Den Besten, P.K.1    Punzi, J.S.2    Li, W.3
  • 29
    • 0001125655 scopus 로고    scopus 로고
    • Matrix metalloproteinase-2 activation modulates glioma cell migration
    • Deryugina, E.I., Bourbon, M.A., Luo, G.X., Reisfeld, R.A., and Strongin, A. 1997a. Matrix metalloproteinase-2 activation modulates glioma cell migration. J. Cell Sci. 110: 2473-2482.
    • (1997) J. Cell Sci. , vol.110 , pp. 2473-2482
    • Deryugina, E.I.1    Bourbon, M.A.2    Luo, G.X.3    Reisfeld, R.A.4    Strongin, A.5
  • 30
    • 0030827411 scopus 로고    scopus 로고
    • Tumor cell invasion through matrigel is regulated by activated matrix metalloproteinase-2
    • Deryugina, E.I., Luo, G.X. Reisfeld, R.A., Bourdon, M.A., and Strongin, A. 1997b. Tumor cell invasion through matrigel is regulated by activated matrix metalloproteinase-2. Anticancer Res. 17: 3201-3210.
    • (1997) Anticancer Res. , vol.17 , pp. 3201-3210
    • Deryugina, E.I.1    Luo, G.X.2    Reisfeld, R.A.3    Bourdon, M.A.4    Strongin, A.5
  • 31
    • 0009550145 scopus 로고    scopus 로고
    • Cell surface MT1-MMP and αvβ3 jointly govern the activation of MMP-2 proenzyme by human tumor cells
    • Deryugina, E.I., Reisfeld, R.A., Bourdon, M.A., and Strongin, A. 1998. Cell surface MT1-MMP and αvβ3 jointly govern the activation of MMP-2 proenzyme by human tumor cells. Proc. Am. Assoc. Cancer Res. 39: 82.
    • (1998) Proc. Am. Assoc. Cancer Res. , vol.39 , pp. 82
    • Deryugina, E.I.1    Reisfeld, R.A.2    Bourdon, M.A.3    Strongin, A.4
  • 32
    • 0032448427 scopus 로고    scopus 로고
    • Epidermal expression of collagenase delays wound-healing intransgenic mice
    • Di Colandrea, T., Wang, L., Wille, J., D'Armiento, J., and Chada, K.K. 1998. Epidermal expression of collagenase delays wound-healing intransgenic mice. J. Invest. Dermatol. 111: 1029-1033.
    • (1998) J. Invest. Dermatol. , vol.111 , pp. 1029-1033
    • Di Colandrea, T.1    Wang, L.2    Wille, J.3    D'Armiento, J.4    Chada, K.K.5
  • 33
    • 0030998660 scopus 로고    scopus 로고
    • Macrophage-derived metalloelastase is responsible for the generation of angiostatin in Lewis lung carcinoma
    • Dong, Z., Kumar, R., Yang, X., and Fidler, I.J. 1997. Macrophage-derived metalloelastase is responsible for the generation of angiostatin in Lewis lung carcinoma. Cell, 88: 801-810.
    • (1997) Cell , vol.88 , pp. 801-810
    • Dong, Z.1    Kumar, R.2    Yang, X.3    Fidler, I.J.4
  • 34
    • 6844250127 scopus 로고    scopus 로고
    • Membrane-type matrix metalloproteinases 1 and 2 exhibit broad-spectrum proteolytic capacities comparable to many matrix metalloproteinases
    • d'Ortho, M.P., Will, H., Atkinson, S., Butler, G., Messent, A., Gavrilovic, J., Smith, B., Timpl, R., Zardi, L., and Murphy, G. 1997. Membrane-type matrix metalloproteinases 1 and 2 exhibit broad-spectrum proteolytic capacities comparable to many matrix metalloproteinases. Eur. J. Biochem. 250: 751-757.
    • (1997) Eur. J. Biochem. , vol.250 , pp. 751-757
    • D'Ortho, M.P.1    Will, H.2    Atkinson, S.3    Butler, G.4    Messent, A.5    Gavrilovic, J.6    Smith, B.7    Timpl, R.8    Zardi, L.9    Murphy, G.10
  • 35
    • 0028334568 scopus 로고
    • The prevention of collagen breakdown in bovine nasal cartilage by TIMP, TIMP-2 and a low molecular weight synthetic inhibitor
    • Ellis, A.J., Curry, V.A., Powell, E.K., and Cawston, T.E. 1994. The prevention of collagen breakdown in bovine nasal cartilage by TIMP, TIMP-2 and a low molecular weight synthetic inhibitor. Biochem. Biophys. Res. Commun. 201: 94-101.
    • (1994) Biochem. Biophys. Res. Commun. , vol.201 , pp. 94-101
    • Ellis, A.J.1    Curry, V.A.2    Powell, E.K.3    Cawston, T.E.4
  • 36
    • 0027965584 scopus 로고
    • Correlation between stromelysin-3 mRNA level and outcome of human breast cancer
    • Engel, G., Heselmeyer, K., Auer, G., Bäckdahl, M., Eriksson, E., and Linder, S. 1994. Correlation between stromelysin-3 mRNA level and outcome of human breast cancer. Int. J. Cancer, 58: 830-835.
    • (1994) Int. J. Cancer , vol.58 , pp. 830-835
    • Engel, G.1    Heselmeyer, K.2    Auer, G.3    Bäckdahl, M.4    Eriksson, E.5    Linder, S.6
  • 37
    • 0025369023 scopus 로고
    • Developmental expression of the endogenous TIMP gene and a TIMP-lacZ fusion gene in transgenic mice
    • Flenniken, A.M., and Williams, B.R.G. 1990. Developmental expression of the endogenous TIMP gene and a TIMP-lacZ fusion gene in transgenic mice. Genes Dev. 4: 1094-1106.
    • (1990) Genes Dev. , vol.4 , pp. 1094-1106
    • Flenniken, A.M.1    Williams, B.R.G.2
  • 38
  • 39
    • 0026753677 scopus 로고
    • Domain structure of human 72-kDa gelatinase/type IV collagenase. Characterization of proteolytic activity and identification of the tissue inhibitor of metalloproteinase-2 (TIMP-2) binding regions
    • Fridman, R., Fuerst, T.R., Birb, R.E., Hoyhtya, M., Oelkuct, M., Kraus, S., Komarek, D., Liotta, L.A., Berman, M.L., and Stetler-Stevenson, W.G. 1992. Domain structure of human 72-kDa gelatinase/type IV collagenase. Characterization of proteolytic activity and identification of the tissue inhibitor of metalloproteinase-2 (TIMP-2) binding regions. J. Biol. Chem. 267: 15398-15405.
    • (1992) J. Biol. Chem. , vol.267 , pp. 15398-15405
    • Fridman, R.1    Fuerst, T.R.2    Birb, R.E.3    Hoyhtya, M.4    Oelkuct, M.5    Kraus, S.6    Komarek, D.7    Liotta, L.A.8    Berman, M.L.9    Stetler-Stevenson, W.G.10
  • 40
    • 0031457759 scopus 로고    scopus 로고
    • Regulation and role of myocardial collagen matrix remodelling in hypertensive heart disease
    • Funck, R.C., Wilke, A., Rupp, H., and Brilla, C.G. 1997. Regulation and role of myocardial collagen matrix remodelling in hypertensive heart disease. Adv. Exp. Med. Biol. 432: 35-44.
    • (1997) Adv. Exp. Med. Biol. , vol.432 , pp. 35-44
    • Funck, R.C.1    Wilke, A.2    Rupp, H.3    Brilla, C.G.4
  • 41
    • 0030698670 scopus 로고    scopus 로고
    • L'angiogenèse tumorale: Une nouvelle cible thérapeutique anticancéreuse
    • Gingras, D., and Béliveau, R. 1997. L'angiogenèse tumorale: une nouvelle cible thérapeutique anticancéreuse. M/S, 13: 1428-1435.
    • (1997) M/S , vol.13 , pp. 1428-1435
    • Gingras, D.1    Béliveau, R.2
  • 42
    • 0030717692 scopus 로고    scopus 로고
    • Tissue inhibitors of metalloproteinases: Structure, regulation and biological functions
    • Gomez, D.E., Alonso, D.F., Yoshiji, H., and Thorgeirsson, U.P. 1997. Tissue inhibitors of metalloproteinases: structure, regulation and biological functions. Eur. J. Cell Biol. 74: 111-122.
    • (1997) Eur. J. Cell Biol. , vol.74 , pp. 111-122
    • Gomez, D.E.1    Alonso, D.F.2    Yoshiji, H.3    Thorgeirsson, U.P.4
  • 43
    • 0029806813 scopus 로고    scopus 로고
    • Molecular cloning and characterization of human tissue inhibitor of metalloproteinase 4
    • Greene, J., Wang, M., Liu, Y.E., Raymond, L.A., Rosen, C., and Shi, Y.E. 1996. Molecular cloning and characterization of human tissue inhibitor of metalloproteinase 4. J. Biol. Chem. 271: 30375-30380.
    • (1996) J. Biol. Chem. , vol.271 , pp. 30375-30380
    • Greene, J.1    Wang, M.2    Liu, Y.E.3    Raymond, L.A.4    Rosen, C.5    Shi, Y.E.6
  • 44
    • 0032529030 scopus 로고    scopus 로고
    • Isolation and characterization of two novel metalloproteinase genes linked to the Cdc2L locus on human chromosome 1p36.3
    • Gururajan, R., Grenet, J., Lahti, J.M., and Kidd, V.J. 1998. Isolation and characterization of two novel metalloproteinase genes linked to the Cdc2L locus on human chromosome 1p36.3. Genomics, 15: 101-106.
    • (1998) Genomics , vol.15 , pp. 101-106
    • Gururajan, R.1    Grenet, J.2    Lahti, J.M.3    Kidd, V.J.4
  • 45
    • 0030823772 scopus 로고    scopus 로고
    • Requirement for macrophage elastase for cigarette smoke-induced emphysema in mice
    • Hautamaki, R.D., Kobayashi, D.K., Senior, R.M., and Shapiro, S.D. 1997. Requirement for macrophage elastase for cigarette smoke-induced emphysema in mice. Science (Washington, D.C.), 277: 2002-2004.
    • (1997) Science (Washington, D.C.) , vol.277 , pp. 2002-2004
    • Hautamaki, R.D.1    Kobayashi, D.K.2    Senior, R.M.3    Shapiro, S.D.4
  • 46
    • 0026568011 scopus 로고
    • Growth-promoting activity of tissue inhibitor of metalloproteinase-1 (TIMP-1) for a wide range of cells. A possible new growth factor in serum
    • Hayakawa, T., Yamashita, K., Tanzawa, K., Uchijima, E., and Iwata, K. 1992. Growth-promoting activity of tissue inhibitor of metalloproteinase-1 (TIMP-1) for a wide range of cells. A possible new growth factor in serum. FEBS Lett. 298: 29-32.
    • (1992) FEBS Lett. , vol.298 , pp. 29-32
    • Hayakawa, T.1    Yamashita, K.2    Tanzawa, K.3    Uchijima, E.4    Iwata, K.5
  • 47
    • 0028132867 scopus 로고
    • Cell growth-promoting activity of tissue inhibitor of metalloproteinase-2 (TIMP-2)
    • Hayakawa, T., Yamashita, K., Ohuchi, E., and Shinagawa, A. 1994. Cell growth-promoting activity of tissue inhibitor of metalloproteinase-2 (TIMP-2). J. Cell Sci. 107: 2373-2379.
    • (1994) J. Cell Sci. , vol.107 , pp. 2373-2379
    • Hayakawa, T.1    Yamashita, K.2    Ohuchi, E.3    Shinagawa, A.4
  • 48
    • 0027262416 scopus 로고
    • Inhibition of stimulated bone resorption in vitro by TIMP-1 and TIMP-2
    • Hill, P.A., Reynolds, J.J., and Meikle, M.C. 1993. Inhibition of stimulated bone resorption in vitro by TIMP-1 and TIMP-2. Biochim. Biophys. Acta, 1177: 71-74.
    • (1993) Biochim. Biophys. Acta , vol.1177 , pp. 71-74
    • Hill, P.A.1    Reynolds, J.J.2    Meikle, M.C.3
  • 49
    • 0027960243 scopus 로고
    • The effects of selective inhibitors of matrix metalloproteinases (MMPs) on bone resorption and the identification of MMPs and TIMP-1 in isolated osteoclasts
    • Hill, P.A., Murphy, G., Docherty, A.J., Hembry, R.M., Millican, T.A., Reynolds, J.J., and Meikle, M.C. 1994. The effects of selective inhibitors of matrix metalloproteinases (MMPs) on bone resorption and the identification of MMPs and TIMP-1 in isolated osteoclasts. J. Cell Sci. 107: 3055-3064.
    • (1994) J. Cell Sci. , vol.107 , pp. 3055-3064
    • Hill, P.A.1    Murphy, G.2    Docherty, A.J.3    Hembry, R.M.4    Millican, T.A.5    Reynolds, J.J.6    Meikle, M.C.7
  • 50
    • 0027533506 scopus 로고
    • Structure-function relationship of human neutrophil collagenase: Identification of regions responsible for substrate specificity and general proteinase activity
    • Hirose, T., Patterson, C., Pourmotabbed, T., Mainardi, C.L., and Hasty, K.A. 1993. Structure-function relationship of human neutrophil collagenase: identification of regions responsible for substrate specificity and general proteinase activity. Proc. Natl. Acad. Sci. U.S.A. 90: 2569-2573.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 2569-2573
    • Hirose, T.1    Patterson, C.2    Pourmotabbed, T.3    Mainardi, C.L.4    Hasty, K.A.5
  • 51
    • 0025739240 scopus 로고
    • Regulation of the autoactivation of human 72-kDa progelatinase by tissue inhibitor of metalloproteinase-2
    • Howard, E.W., Bullen, E.C., and Banda, M.J. 1991. Regulation of the autoactivation of human 72-kDa progelatinase by tissue inhibitor of metalloproteinase-2. J. Biol. Chem. 266: 13064-13069.
    • (1991) J. Biol. Chem. , vol.266 , pp. 13064-13069
    • Howard, E.W.1    Bullen, E.C.2    Banda, M.J.3
  • 52
    • 0030010940 scopus 로고    scopus 로고
    • Membrane-type matrix metalloproteinase 1 is a gelatinolytic enzyme and is secreted in a complex with tissue inhibitor of metalloproteinase 2
    • Imai, K., Ohuchi, E., Aoki, T., Nomura, H., Fujii, Y., Sato, H., Seiki, M., and Okada, Y. 1996. Membrane-type matrix metalloproteinase 1 is a gelatinolytic enzyme and is secreted in a complex with tissue inhibitor of metalloproteinase 2. Cancer Res. 56: 2707-2710.
    • (1996) Cancer Res. , vol.56 , pp. 2707-2710
    • Imai, K.1    Ohuchi, E.2    Aoki, T.3    Nomura, H.4    Fujii, Y.5    Sato, H.6    Seiki, M.7    Okada, Y.8
  • 53
    • 0032031861 scopus 로고    scopus 로고
    • Reduced angiogenesis and tumor progression in gelatinase A-deficient mice
    • Itoh, T., Tanioka, M., Yoshida, H., Yoshioka, T., Nishimoto, H., and Itohara, S. 1998. Reduced angiogenesis and tumor progression in gelatinase A-deficient mice. Cancer Res. 58: 1048-1051.
    • (1998) Cancer Res. , vol.58 , pp. 1048-1051
    • Itoh, T.1    Tanioka, M.2    Yoshida, H.3    Yoshioka, T.4    Nishimoto, H.5    Itohara, S.6
  • 54
    • 0018937957 scopus 로고
    • Destruction of extracellular matrices containing glycoproteins, elastin and collagen by metastatic human tumor cells
    • Jones, P.A., and DeClerck, Y.A. 1980. Destruction of extracellular matrices containing glycoproteins, elastin and collagen by metastatic human tumor cells. Cancer Res. 40: 3222-3227.
    • (1980) Cancer Res. , vol.40 , pp. 3222-3227
    • Jones, P.A.1    DeClerck, Y.A.2
  • 56
    • 0026717181 scopus 로고
    • Suppression of invasion by inducible expression of tissue inhibitor of metalloproteinase-1 (TIMP-1) in B16-F10 melanoma cells
    • Khokha, R., Zimmer, M.J., Graham, C.H., Lala, P.K., and Waterhouse, P. 1992. Suppression of invasion by inducible expression of tissue inhibitor of metalloproteinase-1 (TIMP-1) in B16-F10 melanoma cells. J. Natl. Cancer Inst. 84: 1017-1022.
    • (1992) J. Natl. Cancer Inst. , vol.84 , pp. 1017-1022
    • Khokha, R.1    Zimmer, M.J.2    Graham, C.H.3    Lala, P.K.4    Waterhouse, P.5
  • 57
    • 0030037395 scopus 로고    scopus 로고
    • Cellular mechanisms for human procollagenase-3 (MMP-13) activation. Evidence that MT1-MMP (MMP-14) and gelatinase A (MMP-2) are able to generate active enzyme
    • Knäuper, V., Will, H., López-Otin, C., Smith, B., Atkinson, S.J., Stanton, H., Hembry, R.M., and Murphy, G. 1996. Cellular mechanisms for human procollagenase-3 (MMP-13) activation. Evidence that MT1-MMP (MMP-14) and gelatinase A (MMP-2) are able to generate active enzyme. J. Biol. Chem. 271: 17124-17131.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17124-17131
    • Knäuper, V.1    Will, H.2    López-Otin, C.3    Smith, B.4    Atkinson, S.J.5    Stanton, H.6    Hembry, R.M.7    Murphy, G.8
  • 58
    • 0032493066 scopus 로고    scopus 로고
    • Host TIMP-1 overexpression confers resistance to experimental brain metastasis of a fibrosarcoma cell line
    • Kruger, A., Sanchez-Sweatman, O.H., Martin, D.C., Fata, J.E., Ho, A.T., Orr, F.W., Ruther, U., and Khokha, R. 1998. Host TIMP-1 overexpression confers resistance to experimental brain metastasis of a fibrosarcoma cell line. Oncogene, 16: 2419-2423.
    • (1998) Oncogene , vol.16 , pp. 2419-2423
    • Kruger, A.1    Sanchez-Sweatman, O.H.2    Martin, D.C.3    Fata, J.E.4    Ho, A.T.5    Orr, F.W.6    Ruther, U.7    Khokha, R.8
  • 59
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London), 227: 680-685.
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 60
    • 0028334115 scopus 로고
    • Zymographic techniques for detection and characterization of microbial proteases
    • Lantz, M.S., and Ciborowski, P. 1994. Zymographic techniques for detection and characterization of microbial proteases. Methods Enzymol. 235: 563-594.
    • (1994) Methods Enzymol. , vol.235 , pp. 563-594
    • Lantz, M.S.1    Ciborowski, P.2
  • 61
    • 0028244447 scopus 로고
    • Tissue inhibitor of metalloproteinase-3 (TIMP-3) is an extracellular matrix-associated protein with a distinctive pattern of expression in mouse cells and tissues
    • Leco, K.J., Khokha, R., Pavloff, N., Hawkes, S.P., and Edwards, D.R. 1994. Tissue inhibitor of metalloproteinase-3 (TIMP-3) is an extracellular matrix-associated protein with a distinctive pattern of expression in mouse cells and tissues. J. Biol. Chem. 269: 9352-9360.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9352-9360
    • Leco, K.J.1    Khokha, R.2    Pavloff, N.3    Hawkes, S.P.4    Edwards, D.R.5
  • 62
    • 0029417131 scopus 로고
    • Gelatinase a possesses a beta-secretase-like activity in cleaving the amyloid protein precursor of Alzheimer's disease
    • LePage, R.N., Fosang, A.J., Fuller, S.J., Murphy, G., Evin, G., Beyreuther, K., Masters, C.L., and Small, D.H. 1995. Gelatinase A possesses a beta-secretase-like activity in cleaving the amyloid protein precursor of Alzheimer's disease. FEBS Lett. 377: 267-270.
    • (1995) FEBS Lett. , vol.377 , pp. 267-270
    • LePage, R.N.1    Fosang, A.J.2    Fuller, S.J.3    Murphy, G.4    Evin, G.5    Beyreuther, K.6    Masters, C.L.7    Small, D.H.8
  • 65
    • 0030030021 scopus 로고    scopus 로고
    • Two distinct phases of apoptosis in mammary gland involution: Proteinase-independent and -dependent pathways
    • Lund, L.R., Romer, J., Thomasset, N., Solberg, H., Pyke, C., Bissell, M.J., Dano, K., and Werb, Z. 1996. Two distinct phases of apoptosis in mammary gland involution: proteinase-independent and -dependent pathways. Development, 122: 181-193.
    • (1996) Development , vol.122 , pp. 181-193
    • Lund, L.R.1    Romer, J.2    Thomasset, N.3    Solberg, H.4    Pyke, C.5    Bissell, M.J.6    Dano, K.7    Werb, Z.8
  • 66
    • 0029594498 scopus 로고
    • Contributions of tumor and stromal matrix metalloproteinases to tumor progression, invasion and metastasis
    • MacDougall, J.R., and Matrisian, L.M. 1995. Contributions of tumor and stromal matrix metalloproteinases to tumor progression, invasion and metastasis. Cancer Metastasis Rev. 14: 351-362.
    • (1995) Cancer Metastasis Rev. , vol.14 , pp. 351-362
    • MacDougall, J.R.1    Matrisian, L.M.2
  • 67
    • 0025149103 scopus 로고
    • Discoordinate expression of stromelysin, collagenase, and tissue inhibitor of metalloproteinase-1 in rheumatoid human synovial fibroblasts. Synergistic effects of interleukin-1 and tumor necrosis factor-α on stromelysin expression
    • MacNaul, K.L., Chartrain, N., Lark, M., Tocci, M.J., and Hutchinson, N.I. 1990. Discoordinate expression of stromelysin, collagenase, and tissue inhibitor of metalloproteinase-1 in rheumatoid human synovial fibroblasts. Synergistic effects of interleukin-1 and tumor necrosis factor-α on stromelysin expression. J. Biol. Chem. 265: 17238-17245.
    • (1990) J. Biol. Chem. , vol.265 , pp. 17238-17245
    • MacNaul, K.L.1    Chartrain, N.2    Lark, M.3    Tocci, M.J.4    Hutchinson, N.I.5
  • 68
    • 0029867128 scopus 로고    scopus 로고
    • Matrix metalloproteinases in the normal human central nervous system, microglial nodules, and multiple sclerosis lesions
    • Maeda, A., and Sobel, R.A. 1996. Matrix metalloproteinases in the normal human central nervous system, microglial nodules, and multiple sclerosis lesions. J. Neuropathol. Exp. Neurol. 55: 300-309.
    • (1996) J. Neuropathol. Exp. Neurol. , vol.55 , pp. 300-309
    • Maeda, A.1    Sobel, R.A.2
  • 70
    • 0031656460 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Structures, evolution and diversification
    • Massova, I., Kotra, L.P., Fridman, R., and Mobashery, S. 1998. Matrix metalloproteinases: structures, evolution and diversification. FASEB J. 12: 1075-1095.
    • (1998) FASEB J. , vol.12 , pp. 1075-1095
    • Massova, I.1    Kotra, L.P.2    Fridman, R.3    Mobashery, S.4
  • 71
    • 0026896029 scopus 로고
    • The matrix-degrading metalloproteinases
    • Matrisian, L.M. 1992. The matrix-degrading metalloproteinases. Bioessays, 14: 455-463.
    • (1992) Bioessays , vol.14 , pp. 455-463
    • Matrisian, L.M.1
  • 72
    • 0025995226 scopus 로고
    • Expression of metalloproteinases and metalloproteinase inhibitor in human arthritic synovium
    • McCachren, S.S. 1991. Expression of metalloproteinases and metalloproteinase inhibitor in human arthritic synovium. Arthritis Rheum. 34: 1085-1093.
    • (1991) Arthritis Rheum. , vol.34 , pp. 1085-1093
    • McCachren, S.S.1
  • 73
    • 0027535914 scopus 로고
    • Biology and biochemistry of proteinases in tumor invasion
    • Mignatti, P., and Rifkin, D.B. 1993. Biology and biochemistry of proteinases in tumor invasion. Physiol. Rev. 73: 161-195.
    • (1993) Physiol. Rev. , vol.73 , pp. 161-195
    • Mignatti, P.1    Rifkin, D.B.2
  • 74
    • 0029943568 scopus 로고    scopus 로고
    • Plasminogen activators and matrix metalloproteinases in angiogenesis
    • Mignatti, P., and Rifkin, D.B. 1996. Plasminogen activators and matrix metalloproteinases in angiogenesis. Enzyme Protein, 49: 117-137.
    • (1996) Enzyme Protein , vol.49 , pp. 117-137
    • Mignatti, P.1    Rifkin, D.B.2
  • 75
    • 0024504371 scopus 로고
    • In vitro angiogenesis on the human amniotic membrane: Requirements for basic fibroblast growth factor-induced proteinases
    • Mignatti, P., Tsuboi, R., Robbins, E., and Rifkin, D.B. 1989. In vitro angiogenesis on the human amniotic membrane: requirements for basic fibroblast growth factor-induced proteinases. J. Cell Biol. 108: 671-682.
    • (1989) J. Cell Biol. , vol.108 , pp. 671-682
    • Mignatti, P.1    Tsuboi, R.2    Robbins, E.3    Rifkin, D.B.4
  • 76
    • 0028857264 scopus 로고
    • Assignment of the human membrane-type matrix metalloproteinase (MMP14) gene to 14q11-q12 by in situ hybridization
    • Mignon, C., Okada, A., Mattei, M.G., and Basset, P. 1995. Assignment of the human membrane-type matrix metalloproteinase (MMP14) gene to 14q11-q12 by in situ hybridization. Genomics, 28: 360-361.
    • (1995) Genomics , vol.28 , pp. 360-361
    • Mignon, C.1    Okada, A.2    Mattei, M.G.3    Basset, P.4
  • 77
    • 0027254060 scopus 로고
    • A metalloproteinase inhibitor domain in Alzheimer amyloid protein precursor
    • Miyazaki, K., Hasegawa, M., Funahashi, K., and Umeda, M. 1993. A metalloproteinase inhibitor domain in Alzheimer amyloid protein precursor. Nature (London), 362: 839-841.
    • (1993) Nature (London) , vol.362 , pp. 839-841
    • Miyazaki, K.1    Hasegawa, M.2    Funahashi, K.3    Umeda, M.4
  • 79
    • 0027499073 scopus 로고
    • Melanoma-mediated dissolution of extracellular matrix: Contribution of urokinase-dependant and metalloproteinase-dependant proteolytic pathways
    • Montgomery, A.M., DeClerck, Y.A., Langley, K.E., Reisfeld, R.A., and Mueller, B.M. 1993. Melanoma-mediated dissolution of extracellular matrix: contribution of urokinase-dependant and metalloproteinase-dependant proteolytic pathways. Cancer Res. 53: 693-700.
    • (1993) Cancer Res. , vol.53 , pp. 693-700
    • Montgomery, A.M.1    DeClerck, Y.A.2    Langley, K.E.3    Reisfeld, R.A.4    Mueller, B.M.5
  • 80
    • 0028919172 scopus 로고
    • Overexpression of plasminogen activator inhibitor 2 in human melanoma cells inhibits spontaneous metastasis in scid/scid mice
    • Mueller, B.M., Yu, Y.B., and Laug, W.E. 1995. Overexpression of plasminogen activator inhibitor 2 in human melanoma cells inhibits spontaneous metastasis in scid/scid mice. Proc. Natl. Acad. Sci. U.S.A. 92: 205-209.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 205-209
    • Mueller, B.M.1    Yu, Y.B.2    Laug, W.E.3
  • 81
    • 0027383944 scopus 로고
    • Tissue inhibitor of metalloproteinase-2 inhibits bFGF-induced human microvascular endothelial cell proliferation
    • Murphy, A.N., Unsworth, E.J., and Stetler-Stevenson, W.G. 1993. Tissue inhibitor of metalloproteinase-2 inhibits bFGF-induced human microvascular endothelial cell proliferation. J. Cell. Physiol. 157: 351-358.
    • (1993) J. Cell. Physiol. , vol.157 , pp. 351-358
    • Murphy, A.N.1    Unsworth, E.J.2    Stetler-Stevenson, W.G.3
  • 82
    • 0025879527 scopus 로고
    • Essential AP-1 and PEA3 binding elements in the human urokinase enhancer display cell type-specific activity
    • Nerlov, C., Rorth, P., Blasi, F., and Johnsen, M. 1991. Essential AP-1 and PEA3 binding elements in the human urokinase enhancer display cell type-specific activity. Oncogene, 6: 1583-1592.
    • (1991) Oncogene , vol.6 , pp. 1583-1592
    • Nerlov, C.1    Rorth, P.2    Blasi, F.3    Johnsen, M.4
  • 83
    • 0032570712 scopus 로고    scopus 로고
    • Active and tissue inhibitor of matrix metalloproteinase-free gelatinase B accumulates within human microvascular endothelial vesicles
    • Nguyen, M., Arkell, J., and Jackson, C.J. 1998. Active and tissue inhibitor of matrix metalloproteinase-free gelatinase B accumulates within human microvascular endothelial vesicles. J. Biol. Chem. 273: 5400-5404.
    • (1998) J. Biol. Chem. , vol.273 , pp. 5400-5404
    • Nguyen, M.1    Arkell, J.2    Jackson, C.J.3
  • 84
    • 0025744104 scopus 로고
    • The specificity of sea urchin hatching enzyme (envelysin) places it in the mammalian matrix metalloproteinase family
    • Nomura, K., Tanaka, H., Kikkawa, Y., Yamaguchi, M., and Suzuki, N. 1991. The specificity of sea urchin hatching enzyme (envelysin) places it in the mammalian matrix metalloproteinase family. Biochemistry, 30: 6115-6123.
    • (1991) Biochemistry , vol.30 , pp. 6115-6123
    • Nomura, K.1    Tanaka, H.2    Kikkawa, Y.3    Yamaguchi, M.4    Suzuki, N.5
  • 85
    • 0031007612 scopus 로고    scopus 로고
    • Sea urchin hatching enzyme (envelysin): cDNA cloning and deprivation of protein substrate specificity by autolytic degradation
    • Nomura, K., Shimizu, T., Kinoh, H., Sendai, Y., Inomata, M., and Suzuki, N. 1997. Sea urchin hatching enzyme (envelysin): cDNA cloning and deprivation of protein substrate specificity by autolytic degradation. Biochemistry, 36: 7225-7238.
    • (1997) Biochemistry , vol.36 , pp. 7225-7238
    • Nomura, K.1    Shimizu, T.2    Kinoh, H.3    Sendai, Y.4    Inomata, M.5    Suzuki, N.6
  • 86
    • 0029837140 scopus 로고    scopus 로고
    • The activity of the Ets transcription factor PEA3 is regulated by two distinct MAPK cascades
    • O'Hagan, R.C., Tozer, R.G., Symons, M., McCormick, F., and Kassel, J.A. 1996. The activity of the Ets transcription factor PEA3 is regulated by two distinct MAPK cascades. Oncogene, 13: 1323-1333.
    • (1996) Oncogene , vol.13 , pp. 1323-1333
    • O'Hagan, R.C.1    Tozer, R.G.2    Symons, M.3    McCormick, F.4    Kassel, J.A.5
  • 87
    • 0031025218 scopus 로고    scopus 로고
    • Membrane type 1 matrix metalloproteinase digests interstitial collagens and other extracellular matrix macromolecules
    • Ohuchi, E., Imai, K., Fujii, Y., Sato, H., Seiki, M., and Okada, Y. 1997. Membrane type 1 matrix metalloproteinase digests interstitial collagens and other extracellular matrix macromolecules. J. Biol. Chem. 272: 2446-2451.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2446-2451
    • Ohuchi, E.1    Imai, K.2    Fujii, Y.3    Sato, H.4    Seiki, M.5    Okada, Y.6
  • 88
    • 0027197860 scopus 로고
    • Demonstration of 72-kDa and 92-kDa forms of type IV collagenase in human skin: Variable expression in various blistering diseases, induction during re-epithelialization, and decrease by topical glucocorticoids
    • Oikarinen, A., Kylmaniemi, M., Autio-Harmainen, H., Autio, P., and Salo, T. 1993. Demonstration of 72-kDa and 92-kDa forms of type IV collagenase in human skin: variable expression in various blistering diseases, induction during re-epithelialization, and decrease by topical glucocorticoids. J. Invest. Dermatol. 101: 205-210.
    • (1993) J. Invest. Dermatol. , vol.101 , pp. 205-210
    • Oikarinen, A.1    Kylmaniemi, M.2    Autio-Harmainen, H.3    Autio, P.4    Salo, T.5
  • 89
    • 0031048966 scopus 로고    scopus 로고
    • Proteolytic activation of the precursor of membrane type 1 matrix metalloproteinase by human plasmin. A possible cell surface activator
    • Okumura, Y., Sato, H., Seiki, M., and Kido, H. 1997. Proteolytic activation of the precursor of membrane type 1 matrix metalloproteinase by human plasmin. A possible cell surface activator. FEBS Lett. 402: 181-184.
    • (1997) FEBS Lett. , vol.402 , pp. 181-184
    • Okumura, Y.1    Sato, H.2    Seiki, M.3    Kido, H.4
  • 90
    • 0032126344 scopus 로고    scopus 로고
    • Cloning of the human tissue inhibitor of metalloproteinase-4 gene (TIMP4) and localization of the TIMP4 and Timp4 genes to human chromosome 3p25 and mouse chromosome 6, respectively
    • Olson, T.M., Hirohata, S., Ye, J., Leco, K., Seldin, M.F., and Apte, S.S. 1998. Cloning of the human tissue inhibitor of metalloproteinase-4 gene (TIMP4) and localization of the TIMP4 and Timp4 genes to human chromosome 3p25 and mouse chromosome 6, respectively. Genomics, 51: 148-151.
    • (1998) Genomics , vol.51 , pp. 148-151
    • Olson, T.M.1    Hirohata, S.2    Ye, J.3    Leco, K.4    Seldin, M.F.5    Apte, S.S.6
  • 91
    • 0028328881 scopus 로고
    • Cytokine-regulated proteases in autoimmune diseases
    • Opdenakker, G., and Van Damme, J. 1994. Cytokine-regulated proteases in autoimmune diseases. Immunol. Today, 15: 103-107.
    • (1994) Immunol. Today , vol.15 , pp. 103-107
    • Opdenakker, G.1    Van Damme, J.2
  • 92
    • 0029014101 scopus 로고
    • Furin-dependent intracellular activation of the human stromelysin-3 zymogen
    • Pei, D., and Weiss, S.J. 1995. Furin-dependent intracellular activation of the human stromelysin-3 zymogen. Nature (London), 375: 244-247.
    • (1995) Nature (London) , vol.375 , pp. 244-247
    • Pei, D.1    Weiss, S.J.2
  • 93
    • 0029001324 scopus 로고
    • The human collagenase-3 (CLG3) gene is located on chromosome 11q22.3 clustered to other members of the matrix metalloproteinase gene family
    • Pendas, A.M., Matilla, T., Estivill, X., and Lopez-Otin, C. 1995. The human collagenase-3 (CLG3) gene is located on chromosome 11q22.3 clustered to other members of the matrix metalloproteinase gene family. Genomics, 26: 615-618.
    • (1995) Genomics , vol.26 , pp. 615-618
    • Pendas, A.M.1    Matilla, T.2    Estivill, X.3    Lopez-Otin, C.4
  • 94
    • 0030588072 scopus 로고    scopus 로고
    • Fine physical mapping of the human matrix metalloproteinase genes clustered on chromosome 11q22.3
    • Pendas, A.M., Santamaria, I., Alvarez, M.V., Pritchard, M., and Lopez-Otin, C. 1996. Fine physical mapping of the human matrix metalloproteinase genes clustered on chromosome 11q22.3. Genomics, 37: 266-268.
    • (1996) Genomics , vol.37 , pp. 266-268
    • Pendas, A.M.1    Santamaria, I.2    Alvarez, M.V.3    Pritchard, M.4    Lopez-Otin, C.5
  • 95
    • 0031041647 scopus 로고    scopus 로고
    • Identification and characterization of a novel human matrix metalloproteinase with unique structural characteristics, chromosomal location, and tissue distribution
    • Pendas, A.M., Knäuper, V., Puente, X.S., Llano, E., Mattei, M.G., Apte, S., Murphy, G., and Lopez-Otin, C. 1997. Identification and characterization of a novel human matrix metalloproteinase with unique structural characteristics, chromosomal location, and tissue distribution. J. Biol. Chem. 272: 4281-4286.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4281-4286
    • Pendas, A.M.1    Knäuper, V.2    Puente, X.S.3    Llano, E.4    Mattei, M.G.5    Apte, S.6    Murphy, G.7    Lopez-Otin, C.8
  • 96
    • 0029991531 scopus 로고    scopus 로고
    • Complex roles of matrix metalloproteinases in tumor progression
    • Powell, W.C., and Matrisian, L.M. 1996. Complex roles of matrix metalloproteinases in tumor progression. Curr. Top. Microbiol. Immunol. 213: 1-21.
    • (1996) Curr. Top. Microbiol. Immunol. , vol.213 , pp. 1-21
    • Powell, W.C.1    Matrisian, L.M.2
  • 97
    • 0027530706 scopus 로고
    • Expression of the metalloproteinase matrilysin in DU-145 cells increases their invasive potential in severe combined immunodeficient mice
    • Powell, W.C., Knox, J.D., Navre, M., Grogan, T.M., Kittelson, J., Nagle, R.B., and Bowden, G.T. 1993. Expression of the metalloproteinase matrilysin in DU-145 cells increases their invasive potential in severe combined immunodeficient mice. Cancer Res. 53: 417-422.
    • (1993) Cancer Res. , vol.53 , pp. 417-422
    • Powell, W.C.1    Knox, J.D.2    Navre, M.3    Grogan, T.M.4    Kittelson, J.5    Nagle, R.B.6    Bowden, G.T.7
  • 98
    • 0032535233 scopus 로고    scopus 로고
    • Localization of the human membrane type 4-matrix metalloproteinase gene (MMP17) to chromosome 12q24
    • Puente, X.S., Pendas, A.M., Llano, E., and Lopez-Otin, C. 1998. Localization of the human membrane type 4-matrix metalloproteinase gene (MMP17) to chromosome 12q24. Genomics, 54: 578-579.
    • (1998) Genomics , vol.54 , pp. 578-579
    • Puente, X.S.1    Pendas, A.M.2    Llano, E.3    Lopez-Otin, C.4
  • 100
    • 0027266761 scopus 로고
    • Collagenase, its inhibitors, and decorin in the lower uterine segment in pregnant women
    • Rechberger, T., and Woessner, J.F., Jr. 1993. Collagenase, its inhibitors, and decorin in the lower uterine segment in pregnant women. Am. J. Obstet. Gynecol. 168: 1598-1603.
    • (1993) Am. J. Obstet. Gynecol. , vol.168 , pp. 1598-1603
    • Rechberger, T.1    Woessner J.F., Jr.2
  • 101
    • 0027450757 scopus 로고
    • Expression and localization of matrilysin, a matrix metalloproteinase, in human endometrium during the reproductive cycle
    • Rodgers, W.H., Osteen, K.G., Matrisian, L.M., Navre, M., Giudice, L.C., and Gorstein, F. 1993. Expression and localization of matrilysin, a matrix metalloproteinase, in human endometrium during the reproductive cycle. Am. J. Obstet. Gynecol. 168: 253-260.
    • (1993) Am. J. Obstet. Gynecol. , vol.168 , pp. 253-260
    • Rodgers, W.H.1    Osteen, K.G.2    Matrisian, L.M.3    Navre, M.4    Giudice, L.C.5    Gorstein, F.6
  • 102
    • 0028825270 scopus 로고
    • Matrix metalloproteinases in brain injury
    • Rosenberg, G.A. 1995. Matrix metalloproteinases in brain injury. J. Neurotrauma, 12: 833-842.
    • (1995) J. Neurotrauma , vol.12 , pp. 833-842
    • Rosenberg, G.A.1
  • 103
    • 0030899195 scopus 로고    scopus 로고
    • Metalloproteinase inhibition blocks edema in intracerebral hemorrhage in the rat
    • Rosenberg, G.A., and Navratil, M. 1997. Metalloproteinase inhibition blocks edema in intracerebral hemorrhage in the rat. Neurology, 48: 921-926.
    • (1997) Neurology , vol.48 , pp. 921-926
    • Rosenberg, G.A.1    Navratil, M.2
  • 104
    • 0030785485 scopus 로고    scopus 로고
    • Coordinate expression of matrix metalloproteinase family members in the uterus of normal, matrilysin-deficient, and stromelysin-1-deficient mice
    • Rudolph-Owen, L.A., Hulboy, D.L., Wilson, C.L., Mudgett, J., and Matrisian, L.M. 1997. Coordinate expression of matrix metalloproteinase family members in the uterus of normal, matrilysin-deficient, and stromelysin-1-deficient mice. Endocrinology, 138: 4902-4911.
    • (1997) Endocrinology , vol.138 , pp. 4902-4911
    • Rudolph-Owen, L.A.1    Hulboy, D.L.2    Wilson, C.L.3    Mudgett, J.4    Matrisian, L.M.5
  • 105
    • 0030756920 scopus 로고    scopus 로고
    • Membrane-type matrix metalloproteinases (MT-MMPs) in cell invasion
    • Sato, H., Okada, Y., and Seiki, M. 1997a. Membrane-type matrix metalloproteinases (MT-MMPs) in cell invasion. Thromb. Haemostasis, 78: 497-500.
    • (1997) Thromb. Haemostasis , vol.78 , pp. 497-500
    • Sato, H.1    Okada, Y.2    Seiki, M.3
  • 106
    • 0031081554 scopus 로고    scopus 로고
    • Assignment of the human genes for membrane-type-1, -2, and -3 matrix metalloproteinases (MMP14, MMP15 and MMP16) to 14q12.2, 16q12.2-q21, and 8q21, respectively by in situ hybridization
    • Sato, H., Tanaka, M., Takino, T., Inoue, M., and Seiki, M. 1997b. Assignment of the human genes for membrane-type-1, -2, and -3 matrix metalloproteinases (MMP14, MMP15 and MMP16) to 14q12.2, 16q12.2-q21, and 8q21, respectively by in situ hybridization. Genomics, 39: 412-413.
    • (1997) Genomics , vol.39 , pp. 412-413
    • Sato, H.1    Tanaka, M.2    Takino, T.3    Inoue, M.4    Seiki, M.5
  • 108
    • 0023696675 scopus 로고
    • Inhibition by human 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., Bajkowski, A.S., and Carmichael, D.F. 1988. Inhibition by human recombinant tissue inhibitor of metalloproteinases of human amnion invasion and lung colonization by murine B16-F10 melanoma cells. Cancer Res. 48: 5539-5545.
    • (1988) Cancer Res. , vol.48 , pp. 5539-5545
    • Schultz, R.M.1    Silberman, S.2    Persky, B.3    Bajkowski, A.S.4    Carmichael, D.F.5
  • 109
    • 0029883408 scopus 로고    scopus 로고
    • Membrane type-matrix metalloproteinase and tumor invasion
    • Seiki, M. 1996. Membrane type-matrix metalloproteinase and tumor invasion. Curr. Top. Microbiol. Immunol. 213: 23-32.
    • (1996) Curr. Top. Microbiol. Immunol. , vol.213 , pp. 23-32
    • Seiki, M.1
  • 110
    • 0030890685 scopus 로고    scopus 로고
    • Mighty mice: Transgenic technology "knocks out" questions of matrix metalloproteinase function
    • Shapiro, S.D. 1997. Mighty mice: transgenic technology "knocks out" questions of matrix metalloproteinase function. Matrix Biol. 15: 527-533.
    • (1997) Matrix Biol. , vol.15 , pp. 527-533
    • Shapiro, S.D.1
  • 111
    • 0031671855 scopus 로고    scopus 로고
    • Matrix metalloproteinase degradation of extracellular matrix: Biological consequences
    • Shapiro, S.D. 1998. Matrix metalloproteinase degradation of extracellular matrix: biological consequences. Curr. Opin. Cell Biol. 10: 602-608.
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 602-608
    • Shapiro, S.D.1
  • 112
    • 0030068937 scopus 로고    scopus 로고
    • The structural basis for the elastolytic activity of the 92-kDa and 72-kDa gelatinases. Role of the fibronectin type II-like repeats
    • Shipley, J.M., Doyle, G.A., Fliszar, C.J., Ye, Q.Z., Johnson, L.L., Shapiro S.D., Welgus, H.G., and Senior, R.M. 1996. The structural basis for the elastolytic activity of the 92-kDa and 72-kDa gelatinases. Role of the fibronectin type II-like repeats. J. Biol. Chem. 271: 4335-4341.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4335-4341
    • Shipley, J.M.1    Doyle, G.A.2    Fliszar, C.J.3    Ye, Q.Z.4    Johnson, L.L.5    Shapiro, S.D.6    Welgus, H.G.7    Senior, R.M.8
  • 113
    • 0030471877 scopus 로고    scopus 로고
    • Targeted mutagenesis of Timp-1 reveals that lung tumor invasion is influenced by Timp-1 genotype of the tumor but not by that of the host
    • Soloway, P.D., Alexander, C.M., Werb, Z., and Jaenisch, R. 1996. Targeted mutagenesis of Timp-1 reveals that lung tumor invasion is influenced by Timp-1 genotype of the tumor but not by that of the host. Oncogene, 13: 2307-2314.
    • (1996) Oncogene , vol.13 , pp. 2307-2314
    • Soloway, P.D.1    Alexander, C.M.2    Werb, Z.3    Jaenisch, R.4
  • 114
    • 0025096722 scopus 로고
    • Multiple modes of activation of latent human fibroblast collagenase: Evidence for the role of a Cys73 activesite zinc complex in latency and a "cysteine-switch" mechanism for activation
    • Springman, E.B., Angleton, E.L., Birkedal-Hansen, H., and Van Wart, H.E. 1990. Multiple modes of activation of latent human fibroblast collagenase: evidence for the role of a Cys73 activesite zinc complex in latency and a "cysteine-switch" mechanism for activation. Proc. Natl. Acad. Sci. U.S.A. 87: 364-368.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 364-368
    • Springman, E.B.1    Angleton, E.L.2    Birkedal-Hansen, H.3    Van Wart, H.E.4
  • 115
    • 0027333411 scopus 로고
    • Tumor cell interactions with the extracellular matrix during invasion and metastasis
    • Stetler-Stevenson, W.G., Aznavoorian, S., and Liotta, L.A. 1993a. Tumor cell interactions with the extracellular matrix during invasion and metastasis. Annu. Rev. Cell Biol. 9: 541-573.
    • (1993) Annu. Rev. Cell Biol. , vol.9 , pp. 541-573
    • Stetler-Stevenson, W.G.1    Aznavoorian, S.2    Liotta, L.A.3
  • 116
    • 0027140406 scopus 로고
    • Extracellular matrix 6: Role of matrix metalloproteinases in tumor invasion and metastasis
    • Stetler-Stevenson, W.G., Liotta, L.A., and Kleiner, D.E., Jr. 1993b. Extracellular matrix 6: role of matrix metalloproteinases in tumor invasion and metastasis. FASEB J. 7: 1434-1441.
    • (1993) FASEB J. , vol.7 , pp. 1434-1441
    • Stetler-Stevenson, W.G.1    Liotta, L.A.2    Kleiner D.E., Jr.3
  • 117
    • 0029825963 scopus 로고    scopus 로고
    • Identification and characterization of a novel collagenase in Xenopus laevis: Possible roles during frog development
    • Stolow, M.A., Bauzon, D.D., Li, J., Sedgwick, T., Liang, V.C.T., Sang, Q.A., and Shi, Y.B. 1996. Identification and characterization of a novel collagenase in Xenopus laevis: possible roles during frog development. Mol. Biol. Cell, 7: 1471-1483.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1471-1483
    • Stolow, M.A.1    Bauzon, D.D.2    Li, J.3    Sedgwick, T.4    Liang, V.C.T.5    Sang, Q.A.6    Shi, Y.B.7
  • 118
    • 0020974880 scopus 로고
    • Human skin fibroblast collagenase inhibitor. Purification and biochemical characterization
    • Stricklin, G.P., and Welgus, H.G. 1983. Human skin fibroblast collagenase inhibitor. Purification and biochemical characterization. J. Biol. Chem. 258: 12252-12258.
    • (1983) J. Biol. Chem. , vol.258 , pp. 12252-12258
    • Stricklin, G.P.1    Welgus, H.G.2
  • 119
    • 0027172634 scopus 로고
    • Plasma membrane-dependant activation of the 72-kDa type IV collagenase is prevented by complex formation with TIMP-2
    • Strongin, A.Y., Marmer, B.L., Grant, G.A., and Goldberg, G.I. 1993. Plasma membrane-dependant activation of the 72-kDa type IV collagenase is prevented by complex formation with TIMP-2. J. Biol. Chem. 268: 14033-14039.
    • (1993) J. Biol. Chem. , vol.268 , pp. 14033-14039
    • Strongin, A.Y.1    Marmer, B.L.2    Grant, G.A.3    Goldberg, G.I.4
  • 120
    • 0032523792 scopus 로고    scopus 로고
    • Matrix metalloproteinases-2 and -9 are expressed in human neuroblastoma: Contribution of stromal cells to their production and correlation with metastasis
    • Sugiura, Y., Shimada, H., Seeger, R.C., Laug, W.E., and DeClerck, Y.A. 1998. Matrix metalloproteinases-2 and -9 are expressed in human neuroblastoma: contribution of stromal cells to their production and correlation with metastasis. Cancer Res. 58: 2209-2216.
    • (1998) Cancer Res. , vol.58 , pp. 2209-2216
    • Sugiura, Y.1    Shimada, H.2    Seeger, R.C.3    Laug, W.E.4    DeClerck, Y.A.5
  • 121
    • 0029312344 scopus 로고
    • Mammary gland tumor formation in transgenic mice overexpressing stromelysin-1
    • Sympson, C.J., Bissel, M.J., and Werb, Z. 1995. Mammary gland tumor formation in transgenic mice overexpressing stromelysin-1. Semin. Cancer Biol. 6: 159-163.
    • (1995) Semin. Cancer Biol. , vol.6 , pp. 159-163
    • Sympson, C.J.1    Bissel, M.J.2    Werb, Z.3
  • 122
    • 0026768210 scopus 로고
    • Coordinated expression of extracellular matrix-degrading proteinases and their inhibitors regulates mammary epithelial function during involution
    • Talhouk, R.S., Bissell, M.J., and Werb, Z. 1992. Coordinated expression of extracellular matrix-degrading proteinases and their inhibitors regulates mammary epithelial function during involution. J. Cell Biol. 118: 1271-1282.
    • (1992) J. Cell Biol. , vol.118 , pp. 1271-1282
    • Talhouk, R.S.1    Bissell, M.J.2    Werb, Z.3
  • 124
    • 0030775242 scopus 로고    scopus 로고
    • Postsurgical wound progression monitored by temporal changes in the expression of matrix metalloproteinase-9
    • Tarlton, J.F., Vickery, C.J., Leaper, D.J., and Bailey, A.J. 1997. Postsurgical wound progression monitored by temporal changes in the expression of matrix metalloproteinase-9. Br. J. Dermatol. 137: 506-516.
    • (1997) Br. J. Dermatol. , vol.137 , pp. 506-516
    • Tarlton, J.F.1    Vickery, C.J.2    Leaper, D.J.3    Bailey, A.J.4
  • 126
    • 0029906468 scopus 로고    scopus 로고
    • Glioma invasion in vitro: Regulation by matrix metalloprotease-2 and protein kinase C
    • Uhm, J.H., Dooley, N.P., Villemure, J.G., and Yong, V.W. 1996. Glioma invasion in vitro: regulation by matrix metalloprotease-2 and protein kinase C. Clin. Exp. Metastasis, 14: 421-433.
    • (1996) Clin. Exp. Metastasis , vol.14 , pp. 421-433
    • Uhm, J.H.1    Dooley, N.P.2    Villemure, J.G.3    Yong, V.W.4
  • 127
    • 0030968580 scopus 로고    scopus 로고
    • Rho GTPases and signaling networks
    • Van Aelst, L., and D'Souza-Schorey, C. 1997. Rho GTPases and signaling networks. Genes Dev. 11: 2295-2322.
    • (1997) Genes Dev. , vol.11 , pp. 2295-2322
    • Van Aelst, L.1    D'Souza-Schorey, C.2
  • 128
    • 0346963598 scopus 로고    scopus 로고
    • MMP-9/gelatinase B is a key regulator of growth plate angiogenesis and apoptosis of hypertrophic chondrocytes
    • Vu, T.H., Shipley, J.M., Bergers, G., Berger, J.E., Helms, J.A., Hanahan, D., Shapiro, S.D., Senior, R.M., and Werb, Z. 1998. MMP-9/gelatinase B is a key regulator of growth plate angiogenesis and apoptosis of hypertrophic chondrocytes. Cell, 93: 411-422.
    • (1998) Cell , vol.93 , pp. 411-422
    • Vu, T.H.1    Shipley, J.M.2    Bergers, G.3    Berger, J.E.4    Helms, J.A.5    Hanahan, D.6    Shapiro, S.D.7    Senior, R.M.8    Werb, Z.9
  • 129
    • 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., Sheng, S., Fuchs, A., Rosen, E.M., and Shi, Y.E. 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    Sheng, S.4    Fuchs, A.5    Rosen, E.M.6    Shi, Y.E.7
  • 132
    • 0030061278 scopus 로고    scopus 로고
    • Matrilysin, an epithelial matrix metalloproteinase with potentially novel functions
    • Wilson, C.L., and Matrisian, L.M. 1996. Matrilysin, an epithelial matrix metalloproteinase with potentially novel functions. Int. J. Biochem. Cell Biol. 28: 123-136.
    • (1996) Int. J. Biochem. Cell Biol. , vol.28 , pp. 123-136
    • Wilson, C.L.1    Matrisian, L.M.2
  • 135
    • 0028916958 scopus 로고
    • Decreased tumor formation in 7,12-dimethylbenz-anthracene-treated stromelysin-1 transgenic mice is associated with alterations in mammary epithelial cell apoptosis
    • Witty, J.P., Lempka, T., Coffey, R.J., Jr., and Matrisian, L.M. 1995a. Decreased tumor formation in 7,12-dimethylbenz-anthracene-treated stromelysin-1 transgenic mice is associated with alterations in mammary epithelial cell apoptosis. Cancer Res. 55: 1401-1406.
    • (1995) Cancer Res. , vol.55 , pp. 1401-1406
    • Witty, J.P.1    Lempka, T.2    Coffey R.J., Jr.3    Matrisian, L.M.4
  • 136
    • 0028877124 scopus 로고
    • Matrix metalloproteinases are expressed during ductal and alveolar mammary morphogenesis, and misregulation of stromelysin-1 in transgenic mice induces unscheduled alveolar development
    • Witty, J.P., Wright, J.H., and Matrisian, L.M. 1995b. Matrix metalloproteinases are expressed during ductal and alveolar mammary morphogenesis, and misregulation of stromelysin-1 in transgenic mice induces unscheduled alveolar development. Mol. Biol. Cell, 6: 1287-1303.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1287-1303
    • Witty, J.P.1    Wright, J.H.2    Matrisian, L.M.3
  • 137
    • 0023716802 scopus 로고
    • Purification and properties of a small latent matrix metalloproteinase of the rat uterus
    • Woessner, J.F., Jr., and Taplin, C.J. 1988. Purification and properties of a small latent matrix metalloproteinase of the rat uterus. J. Biol. Chem. 263: 16918-16925.
    • (1988) J. Biol. Chem. , vol.263 , pp. 16918-16925
    • Woessner J.F., Jr.1    Taplin, C.J.2
  • 138
    • 0027202705 scopus 로고
    • Wound fluid from chronic leg ulcers contains elevated levels of metalloproteinases MMP-2 and MMP-9
    • Wysocki, A.B., Staiano-Coico, L., and Grinnel, F. 1993. Wound fluid from chronic leg ulcers contains elevated levels of metalloproteinases MMP-2 and MMP-9. J. Invest. Dermatol. 101: 64-68.
    • (1993) J. Invest. Dermatol. , vol.101 , pp. 64-68
    • Wysocki, A.B.1    Staiano-Coico, L.2    Grinnel, F.3
  • 139
    • 9044246674 scopus 로고    scopus 로고
    • Differential expression of membrane-type matrix metalloproteinase and its correlation with gelatinase A activation in human malignant brain tumors in vivo and in vitro
    • Yamamoto, M., Mohanam, S., Sawaya, R., Fuller, G.N., Seiki, M., Sato, H., Gokaslan, Z.L., Liotta, L.A., Nicolson, G.L., and Rao, J.S. 1996. Differential expression of membrane-type matrix metalloproteinase and its correlation with gelatinase A activation in human malignant brain tumors in vivo and in vitro. Cancer Res. 56: 384-392.
    • (1996) Cancer Res. , vol.56 , pp. 384-392
    • Yamamoto, M.1    Mohanam, S.2    Sawaya, R.3    Fuller, G.N.4    Seiki, M.5    Sato, H.6    Gokaslan, Z.L.7    Liotta, L.A.8    Nicolson, G.L.9    Rao, J.S.10
  • 140
    • 0032504177 scopus 로고    scopus 로고
    • Cloning and characterization of a novel matrix metalloproteinase (MMP), CMMP, from chicken embryo fibroblasts. CMMP, Xenopus XMMP, and human MMP19 have a conserved unique cysteine in the catalytic domain
    • Yang, M., and Kurkinen, M. 1998. Cloning and characterization of a novel matrix metalloproteinase (MMP), CMMP, from chicken embryo fibroblasts. CMMP, Xenopus XMMP, and human MMP19 have a conserved unique cysteine in the catalytic domain. J. Biol. Chem. 273: 17893-17900.
    • (1998) J. Biol. Chem. , vol.273 , pp. 17893-17900
    • Yang, M.1    Kurkinen, M.2
  • 141
    • 0030991956 scopus 로고    scopus 로고
    • A novel matrix metalloproteinase gene (XMMP) encoding vitronectin-like motifs is transiently expressed in Xenopus laevis early embryo development
    • Yang, M., Murray, M.T., and Kurkinen, M. 1997. A novel matrix metalloproteinase gene (XMMP) encoding vitronectin-like motifs is transiently expressed in Xenopus laevis early embryo development. J. Biol. Chem. 272: 13527-13533.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13527-13533
    • Yang, M.1    Murray, M.T.2    Kurkinen, M.3
  • 143
    • 0027948534 scopus 로고
    • Metalloproteinase activation cascade after burn injury: A longitudinal analysis of the human wound environment
    • Young, P.K., and Grinnel, F. 1994. Metalloproteinase activation cascade after burn injury: a longitudinal analysis of the human wound environment. J. Invest. Dermatol. 103: 660-664.
    • (1994) J. Invest. Dermatol. , vol.103 , pp. 660-664
    • Young, P.K.1    Grinnel, F.2
  • 144
    • 0031984868 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinase-2 (TIMP-2) binds to the catalytic domain of the cell surface receptor, membrane type 1-matrix metalloproteinase 1 (MT1-MMP)
    • Zucker, S., Drews, M., Conner, C., Foda, H.D., DeClerck, Y.A., Langley, K.E., Bahou, W.F., Docherty, A.J.P., and Cao, J. 1998. Tissue inhibitor of metalloproteinase-2 (TIMP-2) binds to the catalytic domain of the cell surface receptor, membrane type 1-matrix metalloproteinase 1 (MT1-MMP). J. Biol. Chem. 273: 1216-1222.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1216-1222
    • Zucker, S.1    Drews, M.2    Conner, C.3    Foda, H.D.4    DeClerck, Y.A.5    Langley, K.E.6    Bahou, W.F.7    Docherty, A.J.P.8    Cao, J.9


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