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Volumn , Issue 44, 2004, Pages 231-243

The role of matrix metalloproteinases (MMPs) and their inhibitors in venous leg ulcer healing

Author keywords

Chronic venous insufficiency; Lipodermatosclerosis; Metalloproteinase; Proteinases; Varicose veins; Venous leg ulcers

Indexed keywords

MATRIX METALLOPROTEINASE; MATRIX METALLOPROTEINASE INHIBITOR; TISSUE INHIBITOR OF METALLOPROTEINASE;

EID: 1942423221     PISSN: 12860107     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (10)

References (98)
  • 1
    • 0033618337 scopus 로고    scopus 로고
    • Matrix metalloproteinases
    • Nagase H, Woessner JF Jr. Matrix metalloproteinases. J Biol Chem. 1999;274:21491-21494.
    • (1999) J Biol Chem , vol.274 , pp. 21491-21494
    • Nagase, H.1    Woessner Jr., J.F.2
  • 2
    • 0035188727 scopus 로고    scopus 로고
    • How matrix metalloproteinases regulate cell behavior
    • Sternlicht MD, Werb Z. How matrix metalloproteinases regulate cell behavior. Annu Rev Cell Dev Biol. 2001;17:463-516.
    • (2001) Annu Rev Cell Dev Biol , vol.17 , pp. 463-516
    • Sternlicht, M.D.1    Werb, Z.2
  • 3
    • 0001796893 scopus 로고    scopus 로고
    • The matrix metalloproteinase family
    • Parks WC, Mecham RP, eds. San Diego, Calif: Academic Press
    • Woessner JF. The matrix metalloproteinase family. In: Parks WC, Mecham RP, eds. Matrix Metalloproteinases. San Diego, Calif: Academic Press; 1998:1-13.
    • (1998) Matrix Metalloproteinases , pp. 1-13
    • Woessner, J.F.1
  • 4
    • 0030717692 scopus 로고    scopus 로고
    • Tissue inhibitors of metalloproteinases: Structure, regulation and biological functions
    • Gomez DE, Alonso DF, Yoshiji H, et al. Tissue inhibitors of metalloproteinases: structure, regulation and biological functions. Eur J Cell Biol. 1997;74:111-122.
    • (1997) Eur J Cell Biol , vol.74 , pp. 111-122
    • Gomez, D.E.1    Alonso, D.F.2    Yoshiji, H.3
  • 5
    • 0034615550 scopus 로고    scopus 로고
    • Tissue inhibitors of metalloproteinases: Evolution, structure and function
    • Brew K, Dinakarpandian D, Nagase H. Tissue inhibitors of metalloproteinases: evolution, structure and function. Biochim Biophys Acta. 2000;1477:267-283.
    • (2000) Biochim Biophys Acta , vol.1477 , pp. 267-283
    • Brew, K.1    Dinakarpandian, D.2    Nagase, H.3
  • 6
    • 0026437639 scopus 로고
    • Sequential changes in histologic pattern and extracellular matrix deposition during the healing of chronic venous ulcers
    • Herrick SE, Sloan P, McGurk M, et al. Sequential changes in histologic pattern and extracellular matrix deposition during the healing of chronic venous ulcers. Am J Pathol. 1992;141:1085-1095.
    • (1992) Am J Pathol , vol.141 , pp. 1085-1095
    • Herrick, S.E.1    Sloan, P.2    McGurk, M.3
  • 7
    • 0020318701 scopus 로고
    • The cause of venous ulceration
    • Browse NL, Burnand KG. The cause of venous ulceration. Lancet. 1982;2:243-245.
    • (1982) Lancet , vol.2 , pp. 243-245
    • Browse, N.L.1    Burnand, K.G.2
  • 8
    • 0023918945 scopus 로고
    • Causes of venous ulceration: A new hypothesis
    • Coleridge Smith PD, Thomas P, Acurr JH et al. Causes of venous ulceration: A new hypothesis. BMJ. 1988;296:1726-1727.
    • (1988) BMJ , vol.296 , pp. 1726-1727
    • Coleridge Smith, P.D.1    Thomas, P.2    Acurr, J.H.3
  • 9
    • 0026087711 scopus 로고
    • Increased collagen IV layer in the basal membrane area of the capillaries in severe chronic venous insufficiency
    • Neumann HA, Van den Broek MJ. Increased collagen IV layer in the basal membrane area of the capillaries in severe chronic venous insufficiency. Vasa. 1991;20:26-29.
    • (1991) Vasa , vol.20 , pp. 26-29
    • Neumann, H.A.1    Van Den Broek, M.J.2
  • 10
    • 0032820711 scopus 로고    scopus 로고
    • Proteolysis and cell migration: Creating a path?
    • Murphy G, Gavrilovic J. Proteolysis and cell migration: creating a path? Curr Opin Cell Biol. 1999;11:614-621.
    • (1999) Curr Opin Cell Biol , vol.11 , pp. 614-621
    • Murphy, G.1    Gavrilovic, J.2
  • 11
    • 0027939832 scopus 로고
    • The role of extracellular matrix in postinflammatory wound healing and fibrosis
    • Raghow R. The role of extracellular matrix in postinflammatory wound healing and fibrosis. FASEB J. 1994;8:823-831.
    • (1994) FASEB J , vol.8 , pp. 823-831
    • Raghow, R.1
  • 12
    • 0031671855 scopus 로고    scopus 로고
    • Matrix metalloproteinase degradation of extracellular matrix: Biological consequences
    • Shapiro SD. Matrix metalloproteinase degradation of extracellular matrix: biological consequences. Curr Opin Cell Biol. 1998;10: 602-608.
    • (1998) Curr Opin Cell Biol , vol.10 , pp. 602-608
    • Shapiro, S.D.1
  • 13
    • 0029150795 scopus 로고
    • Proteolytic remodeling of extracellular matrix
    • Birkedal-Hansen H. Proteolytic remodeling of extracellular matrix. Curr Opin Cell Biol. 1995;7:728-735.
    • (1995) Curr Opin Cell Biol , vol.7 , pp. 728-735
    • Birkedal-Hansen, H.1
  • 14
    • 0029991531 scopus 로고    scopus 로고
    • Complex roles of matrix metalloproteinases in tumor progression. Attempts to understand metastasis formation
    • Gunther U, Schlag PM, Birchmeier W, eds. Heidelberg, Germany: Springer-Verlag
    • Powell WC, Matrisan LM. Complex roles of matrix metalloproteinases in tumor progression. Attempts to understand metastasis formation. In: Gunther U, Schlag PM, Birchmeier W, eds. Metastasis Related Molecules. Heidelberg, Germany: Springer-Verlag; 1996:1-21.
    • (1996) Metastasis Related Molecules , pp. 1-21
    • Powell, W.C.1    Matrisan, L.M.2
  • 15
    • 0017716778 scopus 로고
    • Evidence for mammalian collagenase as zinc ion metalloenzymes
    • Seltzer JL, Jeffrey JJ, Eisen AZ. Evidence for mammalian collagenase as zinc ion metalloenzymes. Biochim Biophys Acta. 1977;485:179-187.
    • (1977) Biochim Biophys Acta , vol.485 , pp. 179-187
    • Seltzer, J.L.1    Jeffrey, J.J.2    Eisen, A.Z.3
  • 16
  • 17
    • 0028363393 scopus 로고
    • Distinct populations of basal keratinocytes express stromelysin-1 and stromelysin-2 in chronic wounds
    • Saarialho-Kere UK, Pentland AP, Birkedal-Hansen H, et al. Distinct populations of basal keratinocytes express stromelysin-1 and stromelysin-2 in chronic wounds. J Clin Invest. 1994;94:79-88.
    • (1994) J Clin Invest , vol.94 , pp. 79-88
    • Saarialho-Kere, U.K.1    Pentland, A.P.2    Birkedal-Hansen, H.3
  • 18
    • 0024987979 scopus 로고
    • Early expression of a collagenase-like hatching enzyme gene in the sea urchin embryo
    • Lepage T, Gache C. Early expression of a collagenase-like hatching enzyme gene in the sea urchin embryo. EMBO J. 1990;9:3003-3012.
    • (1990) EMBO J , vol.9 , pp. 3003-3012
    • Lepage, T.1    Gache, C.2
  • 19
    • 0034052480 scopus 로고    scopus 로고
    • A novel hydra matrix metalloproteinase (HMMP) functions in extracellular matrix degradation, morphogenesis and the maintenance of differentiated cells in the foot process
    • Leontovich AA, Zhang J, Shimokawa K, et al. A novel hydra matrix metalloproteinase (HMMP) functions in extracellular matrix degradation, morphogenesis and the maintenance of differentiated cells in the foot process. Development. 2000;127:907-920.
    • (2000) Development , vol.127 , pp. 907-920
    • Leontovich, A.A.1    Zhang, J.2    Shimokawa, K.3
  • 20
    • 0033521036 scopus 로고    scopus 로고
    • Matrix metalloproteinase homologues from Arabidopsis thaliana: Expression and activity
    • Maidment JM, Moore D, Murphy GP, et al. Matrix metalloproteinase homologues from Arabidopsis thaliana: expression and activity. J Biol Chem. 1999;274:34706-34710.
    • (1999) J Biol Chem , vol.274 , pp. 34706-34710
    • Maidment, J.M.1    Moore, D.2    Murphy, G.P.3
  • 21
    • 0029016567 scopus 로고
    • Binding of gelatinases A and B to type-I collagen and other matrix components
    • Allan JA, Docherty AJ, Barker PJ, et al. Binding of gelatinases A and B to type-I collagen and other matrix components. Biochem J. 1995;309:299-306.
    • (1995) Biochem J , vol.309 , pp. 299-306
    • Allan, J.A.1    Docherty, A.J.2    Barker, P.J.3
  • 22
    • 0028947020 scopus 로고
    • Matrix metalloproteinase-2 is an interstitial collagenase: Inhibitor-free enzyme catalyzes the cleavage of collagen fibrils and soluble native type I collagen generating the length fragments
    • Aimes RT, Quigley JP. Matrix metalloproteinase-2 is an interstitial collagenase: inhibitor-free enzyme catalyzes the cleavage of collagen fibrils and soluble native type I collagen generating the length fragments. J Biol Chem. 1995;270:5872-5876.
    • (1995) J Biol Chem , vol.270 , pp. 5872-5876
    • Aimes, R.T.1    Quigley, J.P.2
  • 23
    • 0035903020 scopus 로고    scopus 로고
    • Specific collagenolysis by gelatinase A, MMP-2, is determined by the hemopexin domain and not the fibronectin-like domain
    • Patterson ML, Atkinson SJ, Knäuper V, et al. Specific collagenolysis by gelatinase A, MMP-2, is determined by the hemopexin domain and not the fibronectin-like domain. FEBS Lett. 2001;503:158-162.
    • (2001) FEBS Lett , vol.503 , pp. 158-162
    • Patterson, M.L.1    Atkinson, S.J.2    Knäuper, V.3
  • 24
    • 0030884231 scopus 로고    scopus 로고
    • Unaltered secretion of β-amyloid precursor protein in gelatinase A (matrix metalloproteinase 2)-deficient mice
    • Itoh T, Ikeda T, Gomi H, et al. Unaltered secretion of β-amyloid precursor protein in gelatinase A (matrix metalloproteinase 2)-deficient mice. J Biol Chem. 1997;272: 22389-22392.
    • (1997) J Biol Chem , vol.272 , pp. 22389-22392
    • Itoh, T.1    Ikeda, T.2    Gomi, H.3
  • 25
    • 0034946637 scopus 로고    scopus 로고
    • Mutation of the matrix metalloproteinase 2 gene (MMP2) causes a multicentric osteolysis and arthritis syndrome
    • Martignetti JA, Aqeel AA, Sewairi WA, et al. Mutation of the matrix metalloproteinase 2 gene (MMP2) causes a multicentric osteolysis and arthritis syndrome. Nat Genet. 2001;28:261-265.
    • (2001) Nat Genet , vol.28 , pp. 261-265
    • Martignetti, J.A.1    Aqeel, A.A.2    Sewairi, W.A.3
  • 26
    • 0025026410 scopus 로고
    • Mechanisms of activation of tissue procollagenase by matrix metalloproteinase 3 (stromelysin)
    • Suzuki K, Enghild JJ, Morodomi T, et al. Mechanisms of activation of tissue procollagenase by matrix metalloproteinase 3 (stromelysin). Biochemistry. 1990;29:10261-10270.
    • (1990) Biochemistry , vol.29 , pp. 10261-10270
    • Suzuki, K.1    Enghild, J.J.2    Morodomi, T.3
  • 27
    • 0034283015 scopus 로고    scopus 로고
    • Matrilysin-2, a new matrix metalloproteinase expressed in human tumors and showing the minimal domain organization required for secretion, latency, and activity
    • Uria JA, López-Otín C. Matrilysin-2, a new matrix metalloproteinase expressed in human tumors and showing the minimal domain organization required for secretion, latency, and activity. Cancer Res. 2000;60:4745-4751.
    • (2000) Cancer Res , vol.60 , pp. 4745-4751
    • Uria, J.A.1    López-Otín, C.2
  • 28
    • 0034617262 scopus 로고    scopus 로고
    • Identification and characterization of human endometase (matrix metalloproteinase-26) from endometrial tumor
    • Park HI, Ni J, Gerkema FE, et al. Identification and characterization of human endometase (matrix metalloproteinase-26) from endometrial tumor. J Biol Chem. 2000;275:20540-20544.
    • (2000) J Biol Chem , vol.275 , pp. 20540-20544
    • Park, H.I.1    Ni, J.2    Gerkema, F.E.3
  • 29
    • 0031025218 scopus 로고    scopus 로고
    • Membrane type 1 matrix metalloproteinase digests interstitial collagens and other extracellular matrix macromolecules
    • Ohuchi E, Imai K, Fujii Y, et al. Membrane type 1 matrix metalloproteinase digests interstitial collagens and other extracellular matrix macromolecules. J Biol Chem. 1997;272:2446-2451.
    • (1997) J Biol Chem , vol.272 , pp. 2446-2451
    • Ohuchi, E.1    Imai, K.2    Fujii, Y.3
  • 30
    • 2142784516 scopus 로고    scopus 로고
    • MT1-MMP-defident mice develop dwarfism, osteopenia, arthritis, and connective tissue disease due to inadequate collagen turnover
    • Holmbeck K, Bianco P, Caterina J, et al. MT1-MMP-defident mice develop dwarfism, osteopenia, arthritis, and connective tissue disease due to inadequate collagen turnover. Cell. 1999;99:81-92.
    • (1999) Cell , vol.99 , pp. 81-92
    • Holmbeck, K.1    Bianco, P.2    Caterina, J.3
  • 31
    • 0034923623 scopus 로고    scopus 로고
    • Extracellular proteolysis and angiogenesis
    • Pepper MS. Extracellular proteolysis and angiogenesis. Thromb Haemost. 2001;86:346-355.
    • (2001) Thromb Haemost , vol.86 , pp. 346-355
    • Pepper, M.S.1
  • 32
    • 0035105154 scopus 로고    scopus 로고
    • Matrix metalloproteinase (MMP) system in brain: Identification and characterization of brain-specific MMP highly expressed in cerebellum
    • Sekine-Aizawa Y, Hama E, Watanabe K, et al. Matrix metalloproteinase (MMP) system in brain: identification and characterization of brain-specific MMP highly expressed in cerebellum. Eur J Neurosci. 2001;13:935-948.
    • (2001) Eur J Neurosci , vol.13 , pp. 935-948
    • Sekine-Aizawa, Y.1    Hama, E.2    Watanabe, K.3
  • 33
    • 0034652623 scopus 로고    scopus 로고
    • Human MT6-matrix metalloproteinase: Identification, progelatinase A activation, and expression in brain tumors
    • Velasco G, Cal S, Merlos-Suárez A, et al. Human MT6-matrix metalloproteinase: identification, progelatinase A activation, and expression in brain tumors. Cancer Res. 2000;60:877-882.
    • (2000) Cancer Res , vol.60 , pp. 877-882
    • Velasco, G.1    Cal, S.2    Merlos-Suárez, A.3
  • 34
    • 0033256294 scopus 로고    scopus 로고
    • Leukolysin/MMP25/MT6-MMP: A novel matrix metalloproteinase specifically expressed in the leukocyte lineage
    • Pei D. Leukolysin/MMP25/MT6-MMP: a novel matrix metalloproteinase specifically expressed in the leukocyte lineage. Cell Res. 1999;9:291-303.
    • (1999) Cell Res , vol.9 , pp. 291-303
    • Pei, D.1
  • 35
    • 0027515289 scopus 로고
    • Cloning and characterization of a unique elastolytic metalloproteinase produced by human alveolar macrophages
    • Shapiro SD, Kobayashi DK, Ley TJ. Cloning and characterization of a unique elastolytic metalloproteinase produced by human alveolar macrophages. J Biol Chem. 1993;268:23824-23829.
    • (1993) J Biol Chem , vol.268 , pp. 23824-23829
    • Shapiro, S.D.1    Kobayashi, D.K.2    Ley, T.J.3
  • 36
    • 0029911694 scopus 로고    scopus 로고
    • Metalloelastase is required for macrophage-mediated proteolysis and matrix invasion in mice
    • Shipley JM, Wesselschmidt RL, Kobayashi DK, et al. Metalloelastase is required for macrophage-mediated proteolysis and matrix invasion in mice. Proc Natl Acad Sci USA. 1996;93:3942-3946.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 3942-3946
    • Shipley, J.M.1    Wesselschmidt, R.L.2    Kobayashi, D.K.3
  • 37
    • 0031041647 scopus 로고    scopus 로고
    • Identification and characterization of a novel human matrix metalloproteinase with unique structural characteristics, chromosomal location, and tissue distribution
    • Péndas AM, Knäuper V, Puente XS, et al. Identification and characterization of a novel human matrix metalloproteinase with unique structural characteristics, chromosomal location, and tissue distribution. J Biol Chem. 1997;272:4281-4286.
    • (1997) J Biol Chem , vol.272 , pp. 4281-4286
    • Péndas, A.M.1    Knäuper, V.2    Puente, X.S.3
  • 38
    • 0030877993 scopus 로고    scopus 로고
    • The matrix metalloproteinase RASI-1 is expressed in synovial blood vessels of a rheumatoid arthritis patient
    • Kolb C, Mauch S, Peter HH, et al. The matrix metalloproteinase RASI-1 is expressed in synovial blood vessels of a rheumatoid arthritis patient. Immunol Lett. 1997;57:83-88.
    • (1997) Immunol Lett , vol.57 , pp. 83-88
    • Kolb, C.1    Mauch, S.2    Peter, H.H.3
  • 39
    • 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, Kurkinen M. 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. 1998;273:7893-17900.
    • (1998) J Biol Chem , vol.273 , pp. 7893-17900
    • Yang, M.1    Kurkinen, M.2
  • 40
    • 0033582513 scopus 로고    scopus 로고
    • Cloning and characterization of human MMP-23, a new matrix metalloproteinase predominantly expressed in reproductive tissues and lacking conserved domains in other family members
    • Velasco G, Pendas AM, Fueyo A, et al. Cloning and characterization of human MMP-23, a new matrix metalloproteinase predominantly expressed in reproductive tissues and lacking conserved domains in other family members. J Biol Chem. 1999;274:4570-4576.
    • (1999) J Biol Chem , vol.274 , pp. 4570-4576
    • Velasco, G.1    Pendas, A.M.2    Fueyo, A.3
  • 41
    • 0035819913 scopus 로고    scopus 로고
    • MMP-28, a new human matrix metalloproteinase with an unusual cysteine-switch sequence is widely expressed in tumors
    • Marchenko GN, Strongin AY. MMP-28, a new human matrix metalloproteinase with an unusual cysteine-switch sequence is widely expressed in tumors. Gene. 2001;265:87-93.
    • (2001) Gene , vol.265 , pp. 87-93
    • Marchenko, G.N.1    Strongin, A.Y.2
  • 42
    • 0035971090 scopus 로고    scopus 로고
    • Epilysin, a novel human matrix metalloproteinase (MMP-28) expressed in testis and keratinocytes and in response to injury
    • Lohi J, Wilson CL, Roby JD, et al. Epilysin, a novel human matrix metalloproteinase (MMP-28) expressed in testis and keratinocytes and in response to injury. J Biol Chem. 2001;276:10134-10144.
    • (2001) J Biol Chem , vol.276 , pp. 10134-10144
    • Lohi, J.1    Wilson, C.L.2    Roby, J.D.3
  • 43
    • 0036424303 scopus 로고    scopus 로고
    • Epilysin (MMP-28) expression is associated with cell proliferation during epithelial repair
    • Saarialho-Kere U, Kerkela E, Jahkola T, et al. Epilysin (MMP-28) expression is associated with cell proliferation during epithelial repair. J Invest Dermatol. 2002;119:14-21.
    • (2002) J Invest Dermatol , vol.119 , pp. 14-21
    • Saarialho-Kere, U.1    Kerkela, E.2    Jahkola, T.3
  • 44
    • 0032572033 scopus 로고    scopus 로고
    • In vitro expression of MMP-2 and MMP-9 in glioma cells following exposure to inflammatory mediators
    • Esteve PO, Tremblay P, Houde M, et al. In vitro expression of MMP-2 and MMP-9 in glioma cells following exposure to inflammatory mediators. Biochim Biophys Acta. 1998;1403:85-96.
    • (1998) Biochim Biophys Acta , vol.1403 , pp. 85-96
    • Esteve, P.O.1    Tremblay, P.2    Houde, M.3
  • 45
    • 0030957218 scopus 로고    scopus 로고
    • Activation mechanisms of matrix metalloproteinases
    • Nagase H. Activation mechanisms of matrix metalloproteinases. Biol Chem. 1997;378: 151-160
    • (1997) Biol Chem , vol.378 , pp. 151-160
    • Nagase, H.1
  • 46
    • 0030740249 scopus 로고    scopus 로고
    • Distinct populations of stromal cells express collagenase-3 (MMP-13) and collagenase-1 (MMP-1) in chronic ulcers but not in normally healing wounds
    • Vaalomo M, Mattila L, Johansson N, et al. Distinct populations of stromal cells express collagenase-3 (MMP-13) and collagenase-1 (MMP-1) in chronic ulcers but not in normally healing wounds. J Invest Dermatol. 1997;109:96-101.
    • (1997) J Invest Dermatol , vol.109 , pp. 96-101
    • Vaalomo, M.1    Mattila, L.2    Johansson, N.3
  • 48
    • 0023805619 scopus 로고
    • The precursor of a metalloendopeptidase from human rheumatoid synovial fibroblasts: Purification and mechanisms of activation by endopeptidases and 4-aminophenylmercuric acetate
    • Okada Y, Harris ED, Jr, Nagase H. The precursor of a metalloendopeptidase from human rheumatoid synovial fibroblasts: purification and mechanisms of activation by endopeptidases and 4-aminophenylmercuric acetate. Biochem J. 1988;254:731-741.
    • (1988) Biochem J , vol.254 , pp. 731-741
    • Okada, Y.1    Harris Jr., E.D.2    Nagase, H.3
  • 49
    • 0025335183 scopus 로고
    • Stepwise activation mechanisms of the precursor of matrix metalloproteinase 3 (stromelysin) by proteinases and (4-aminophenyl)mercuric acetate
    • Nagase H, Enghild JJ, Suzuki K, et al. Stepwise activation mechanisms of the precursor of matrix metalloproteinase 3 (stromelysin) by proteinases and (4-aminophenyl)mercuric acetate. Biochemistry. 1990;29:5783-5789.
    • (1990) Biochemistry , vol.29 , pp. 5783-5789
    • Nagase, H.1    Enghild, J.J.2    Suzuki, K.3
  • 50
    • 0030977009 scopus 로고    scopus 로고
    • Control of type IV collagenase activity by components of the urokinase-plasmin system: A regulatory mechanism with cell-bound reactants
    • Mazzieri R, Masiero L, Zanetta L, et al. Control of type IV collagenase activity by components of the urokinase-plasmin system: a regulatory mechanism with cell-bound reactants. EMBO J. 1997;16:2319-2332.
    • (1997) EMBO J , vol.16 , pp. 2319-2332
    • Mazzieri, R.1    Masiero, L.2    Zanetta, L.3
  • 51
    • 0034927107 scopus 로고    scopus 로고
    • Plasmin and matrix metalloproteinases in vascular remodeling
    • Lijnen HR. Plasmin and matrix metalloproteinases in vascular remodeling. Thromb Haemost. 2001;86:324-333.
    • (2001) Thromb Haemost , vol.86 , pp. 324-333
    • Lijnen, H.R.1
  • 52
    • 0028907318 scopus 로고
    • Mechanism of cell surface activation of 72 kDa type IV collagenase. Isolation of the activated form of the membrane metalloproteinase
    • Strongin AY, Collier I, Bannikov G, et al. Mechanism of cell surface activation of 72 kDa type IV collagenase. Isolation of the activated form of the membrane metalloproteinase. J Biol Chem. 1995;270:5331-5338.
    • (1995) J Biol Chem , vol.270 , pp. 5331-5338
    • Strongin, A.Y.1    Collier, I.2    Bannikov, G.3
  • 53
    • 0028924956 scopus 로고
    • The C-terminal region of membrane type matrix metalloproteinase is a functional transmembrane domain required for progelatinase A activation
    • Cao J, Sato H, Takino T, Seiki M. The C-terminal region of membrane type matrix metalloproteinase is a functional transmembrane domain required for progelatinase A activation. J Biol Chem. 1995;270:801-805.
    • (1995) J Biol Chem , vol.270 , pp. 801-805
    • Cao, J.1    Sato, H.2    Takino, T.3    Seiki, M.4
  • 54
    • 0033002795 scopus 로고    scopus 로고
    • Mechanisms for pro matrix metalloproteinase activation
    • Murphy G, Stanton H, Cowell S, et al. Mechanisms for pro matrix metalloproteinase activation. APMIS. 1999;107:38-44.
    • (1999) APMIS , vol.107 , pp. 38-44
    • Murphy, G.1    Stanton, H.2    Cowell, S.3
  • 55
    • 0031039965 scopus 로고    scopus 로고
    • Membrane-type-2 matrix metalloproteinase can initiate the processing of progelatinase A and is regulated by the tissue inhibitors of metalloproteinases
    • Butler GS, Will H, Atkinson SJ, et al. Membrane-type-2 matrix metalloproteinase can initiate the processing of progelatinase A and is regulated by the tissue inhibitors of metalloproteinases. Eur J Biochem. 1997;244:653-657.
    • (1997) Eur J Biochem , vol.244 , pp. 653-657
    • Butler, G.S.1    Will, H.2    Atkinson, S.J.3
  • 56
    • 0029118269 scopus 로고
    • Identification of the second membrane-type matrix metalloproteinase (MT-MMP-2) gene from a human placenta cDNA library: MT-MMPs form a unique membrane-type subclass in the MMP family
    • Takino T, Sato H, Shinagawa A, et al. Identification of the second membrane-type matrix metalloproteinase (MT-MMP-2) gene from a human placenta cDNA library: MT-MMPs form a unique membrane-type subclass in the MMP family. J Biol Chem. 1995;270:23013-23020.
    • (1995) J Biol Chem , vol.270 , pp. 23013-23020
    • Takino, T.1    Sato, H.2    Shinagawa, A.3
  • 57
    • 0033152980 scopus 로고    scopus 로고
    • Identification and characterization of human MT5-MMP, a new membrane-bound activator of progelatinase A overexpressed in brain tumors
    • Llano E, Pendas AM, Freije JP, et al. Identification and characterization of human MT5-MMP, a new membrane-bound activator of progelatinase A overexpressed in brain tumors. Cancer Res. 1999;59:2570-2576.
    • (1999) Cancer Res , vol.59 , pp. 2570-2576
    • Llano, E.1    Pendas, A.M.2    Freije, J.P.3
  • 58
    • 0033605561 scopus 로고    scopus 로고
    • Identification and characterization of the fifth membrane-type matrix metalloproteinase MT5-MMP
    • Pei D. Identification and characterization of the fifth membrane-type matrix metalloproteinase MT5-MMP. J Biol Chem. 1999;274:8925-8932.
    • (1999) J Biol Chem , vol.274 , pp. 8925-8932
    • Pei, D.1
  • 59
    • 0034640282 scopus 로고    scopus 로고
    • Membrane type 4 matrix metalloproteinase (MMP17) has tumor necrosis factor convertase activity but does not activate proMMP2
    • English WR, Puente XS, Freije JM, et al. Membrane type 4 matrix metalloproteinase (MMP17) has tumor necrosis factor convertase activity but does not activate proMMP2. J Biol Chem. 2000;275:14046-14055.
    • (2000) J Biol Chem , vol.275 , pp. 14046-14055
    • English, W.R.1    Puente, X.S.2    Freije, J.M.3
  • 60
    • 0031985228 scopus 로고    scopus 로고
    • The TIMP2 membrane type 1 metalloproteinase "receptor" regulates the concentration and efficient activation of progelatinase A: A kinetic study
    • Butler GS, Butler MJ, Atkinson SJ, et al. The TIMP2 membrane type 1 metalloproteinase "receptor" regulates the concentration and efficient activation of progelatinase A: a kinetic study. J Biol Chem. 1998;273:871-880.
    • (1998) J Biol Chem , vol.273 , pp. 871-880
    • Butler, G.S.1    Butler, M.J.2    Atkinson, S.J.3
  • 61
    • 0034714202 scopus 로고    scopus 로고
    • TIMP-2 is required for efficient activation of proMMP-2 in vivo
    • Wang Z, Juttermann R, Soloway PD. TIMP-2 is required for efficient activation of proMMP-2 in vivo. J Biol Chem. 2000; 275:26411-26415.
    • (2000) J Biol Chem , vol.275 , pp. 26411-26415
    • Wang, Z.1    Juttermann, R.2    Soloway, P.D.3
  • 62
    • 0025834914 scopus 로고
    • The purification of tissue inhibitor of metalloproteinase-2 form ist 72 kDa progelatinase complex. Demonstration of the biochemical similarities of tissue inhibitor of metalloproteinase-2 and tissue inhibitor of metalloproteinse-1
    • Ward RV, Hembry RM, Reynolds JJ, et al. The purification of tissue inhibitor of metalloproteinase-2 form ist 72 kDa progelatinase complex. Demonstration of the biochemical similarities of tissue inhibitor of metalloproteinase-2 and tissue inhibitor of metalloproteinse-1. Biochem J. 1991;278:179-187.
    • (1991) Biochem J , vol.278 , pp. 179-187
    • Ward, R.V.1    Hembry, R.M.2    Reynolds, J.J.3
  • 63
    • 0028024317 scopus 로고
    • Cloning and characterization of human tissue inhibitor of metalloproteinases-3
    • Wilde CG, Hawkins PR, Coleman RT, et al. Cloning and characterization of human tissue inhibitor of metalloproteinases-3. DNA Cell Biol. 1994;13:711-718.
    • (1994) DNA Cell Biol , vol.13 , pp. 711-718
    • Wilde, C.G.1    Hawkins, P.R.2    Coleman, R.T.3
  • 64
    • 0031029248 scopus 로고    scopus 로고
    • Murine tissue inhibitor of metalloproteinases-4 (TIMP-4) cDNA isolation and expression in adult mouse tissues
    • Leco KJ, Apte SS, Taniguchi GT, et al. Murine tissue inhibitor of metalloproteinases-4 (TIMP-4) cDNA isolation and expression in adult mouse tissues. FEBS Lett. 1997;401:213-217.
    • (1997) FEBS Lett , vol.401 , pp. 213-217
    • Leco, K.J.1    Apte, S.S.2    Taniguchi, G.T.3
  • 65
    • 0032800451 scopus 로고    scopus 로고
    • Differential expression of tissue inhibitors of metalloproteinases (TIMP-1, -2,-3 and -4) in normal and aberrant wound healing
    • Vaalamo M, Leivo T, Saarialho-Kere U. Differential expression of tissue inhibitors of metalloproteinases (TIMP-1, -2,-3 and -4) in normal and aberrant wound healing. Hum Pathol. 1999;30:795-802.
    • (1999) Hum Pathol , vol.30 , pp. 795-802
    • Vaalamo, M.1    Leivo, T.2    Saarialho-Kere, U.3
  • 66
    • 0025816440 scopus 로고
    • Preferential inhibition of 72- and 92-kDa gelatinases by tissue inhibitors of metalloproteinase-2
    • Howard EW, Bullen EC, Banda MJ. Preferential inhibition of 72- and 92-kDa gelatinases by tissue inhibitors of metalloproteinase-2. J Biol Chem. 1991;266:13070-13075.
    • (1991) J Biol Chem , vol.266 , pp. 13070-13075
    • Howard, E.W.1    Bullen, E.C.2    Banda, M.J.3
  • 67
    • 0027973352 scopus 로고
    • Solution structure of the active domain of tissue inhibitor of metalloproteinases-2: A new member of the OB fold protein family
    • Williamson RA, Martorell G, Carr MD, et al. Solution structure of the active domain of tissue inhibitor of metalloproteinases-2: a new member of the OB fold protein family. Biochemistry. 1994;33:11745-11759.
    • (1994) Biochemistry , vol.33 , pp. 11745-11759
    • Williamson, R.A.1    Martorell, G.2    Carr, M.D.3
  • 68
    • 0025944065 scopus 로고
    • The N-terminal domain of tissue inhibitor of metalloproteinases retains metalloproteinase inhibitory activity
    • Murphy G, Houbrechts A, Cockett MI, et al. The N-terminal domain of tissue inhibitor of metalloproteinases retains metalloproteinase inhibitory activity. Biochemistry. 1991;30:8097-8102
    • (1991) Biochemistry , vol.30 , pp. 8097-8102
    • Murphy, G.1    Houbrechts, A.2    Cockett, M.I.3
  • 69
    • 0030016342 scopus 로고    scopus 로고
    • The soluble catalytic domain of membrane type 1 matrix metalloproteinase cleaves the propeptide of progelatinase A and initiates autoproteolytic activation: Regulation by TIMP-2 and TIMP-3
    • Will H, Atkinson SJ, Butler GS, et al. The soluble catalytic domain of membrane type 1 matrix metalloproteinase cleaves the propeptide of progelatinase A and initiates autoproteolytic activation: regulation by TIMP-2 and TIMP-3. J Biol Chem. 1996;271:17119-17123.
    • (1996) J Biol Chem , vol.271 , pp. 17119-17123
    • Will, H.1    Atkinson, S.J.2    Butler, G.S.3
  • 70
    • 0032508675 scopus 로고    scopus 로고
    • TNF-alpha converting enzyme (TACE) is inhibited by TIMP-3
    • Amour A, Slocombe PM, Webster A, et al. TNF-alpha converting enzyme (TACE) is inhibited by TIMP-3. FEBS Lett. 1998;435: 39-44.
    • (1998) FEBS Lett , vol.435 , pp. 39-44
    • Amour, A.1    Slocombe, P.M.2    Webster, A.3
  • 71
    • 0034685834 scopus 로고    scopus 로고
    • The in vitro activity of ADAM-10 is inhibited by TIMP-1 and TIMP-3
    • Amour A, Knight CG, Webster A, et al. The in vitro activity of ADAM-10 is inhibited by TIMP-1 and TIMP-3. FEBS Lett. 2000;473:275-279.
    • (2000) FEBS Lett , vol.473 , pp. 275-279
    • Amour, A.1    Knight, C.G.2    Webster, A.3
  • 72
    • 0034736115 scopus 로고    scopus 로고
    • ADAM 12-S cleaves IGFBP-3 and IGFBP-5 and is inhibited by TIMP-3
    • Loechel F, Fox JW, Murphy G, et al. ADAM 12-S cleaves IGFBP-3 and IGFBP-5 and is inhibited by TIMP-3. Biochem Biophys Res Commun. 2000;278:511-515.
    • (2000) Biochem Biophys Res Commun , vol.278 , pp. 511-515
    • Loechel, F.1    Fox, J.W.2    Murphy, G.3
  • 73
    • 0035918309 scopus 로고    scopus 로고
    • TIMP-3 is a potent inhibitor of aggrecanase 1 (ADAM-TS4) and aggrecanase 2 (ADAM-TS5)
    • Kashiwagi M, Tortorella M, Nagase H, et al. TIMP-3 is a potent inhibitor of aggrecanase 1 (ADAM-TS4) and aggrecanase 2 (ADAM-TS5). J Biol Chem. 2001;276:12501-12504.
    • (2001) J Biol Chem , vol.276 , pp. 12501-12504
    • Kashiwagi, M.1    Tortorella, M.2    Nagase, H.3
  • 74
    • 0034613296 scopus 로고    scopus 로고
    • TIMP-3 binds to sulfated glycosaminoglycans of the extracellular matrix
    • Yu WH, Yu S, Meng Q, et al. TIMP-3 binds to sulfated glycosaminoglycans of the extracellular matrix. J Biol Chem. 2000;275:31226-31232.
    • (2000) J Biol Chem , vol.275 , pp. 31226-31232
    • Yu, W.H.1    Yu, S.2    Meng, Q.3
  • 75
    • 0037305238 scopus 로고    scopus 로고
    • Matrix remodeling in experimental and human heart failure: A possible regulatory role for TIMP-3
    • Fedak PW, Altamentova SM, Weisel RD, et al. Matrix remodeling in experimental and human heart failure: a possible regulatory role for TIMP-3. Am J Physiol. 2003;284: H626-H634.
    • (2003) Am J Physiol , vol.284
    • Fedak, P.W.1    Altamentova, S.M.2    Weisel, R.D.3
  • 76
    • 0032177931 scopus 로고    scopus 로고
    • Lipodermatosderosis and atrophie blanche
    • Vowden K. Lipodermatosderosis and atrophie blanche. J Wound Care. 1998;7: 441-443.
    • (1998) J Wound Care , vol.7 , pp. 441-443
    • Vowden, K.1
  • 78
    • 0029972104 scopus 로고    scopus 로고
    • Matrix metalloproteinases, gelatinase and collagenase in chronic leg ulcers
    • Weckroth M, Vaheri A, Lauharanta J, et al. Matrix metalloproteinases, gelatinase and collagenase in chronic leg ulcers. J Invest Dermatol 1996;106:1119-1124.
    • (1996) J Invest Dermatol , vol.106 , pp. 1119-1124
    • Weckroth, M.1    Vaheri, A.2    Lauharanta, J.3
  • 79
    • 0027202705 scopus 로고
    • Wound fluid from chronic leg ulcers contains elevated levels of metalloproteinases MMP-2 and MMP-9
    • Wysocki AB, Staiano-Coico L, Grinnell F. Wound fluid from chronic leg ulcers contains elevated levels of metalloproteinases MMP-2 and MMP-9. J Invest Dermatol. 1993;101:64-68.
    • (1993) J Invest Dermatol , vol.101 , pp. 64-68
    • Wysocki, A.B.1    Staiano-Coico, L.2    Grinnell, F.3
  • 80
    • 0031737360 scopus 로고    scopus 로고
    • Lipodermatosclerosis is characterized by elevated expression and activation of matrix metalloproteinases. Implications for venous ulcer formation
    • Herouy Y, May AE, Pornschlegel G, et al. Lipodermatosclerosis is characterized by elevated expression and activation of matrix metalloproteinases. Implications for venous ulcer formation. J Invest Dermatol. 1998;111:822-827.
    • (1998) J Invest Dermatol , vol.111 , pp. 822-827
    • Herouy, Y.1    May, A.E.2    Pornschlegel, G.3
  • 81
    • 0016917553 scopus 로고
    • Proceedings: Fibrinolysis and fat necrosis in the lower leg
    • Jarret PE, Burnand KG, Morland M, et al. Proceedings: Fibrinolysis and fat necrosis in the lower leg. Br J Surg. 1976;63:157-160.
    • (1976) Br J Surg , vol.63 , pp. 157-160
    • Jarret, P.E.1    Burnand, K.G.2    Morland, M.3
  • 82
    • 0033127460 scopus 로고    scopus 로고
    • Lipodermatosclerosis and the significance of proteolytic remodeling in the pathogenesis of venous ulceration
    • Herouy Y, Nockowski P, Schöpf E, et al. Lipodermatosclerosis and the significance of proteolytic remodeling in the pathogenesis of venous ulceration. Int J Mol Med. 1999;3: 511-515.
    • (1999) Int J Mol Med , vol.3 , pp. 511-515
    • Herouy, Y.1    Nockowski, P.2    Schöpf, E.3
  • 83
    • 0030949650 scopus 로고    scopus 로고
    • The activity of collagenase-1 is required for keratinocyte migration on a type I collagen matrix
    • Pilcher BK, Dumin JA, Sudbeck BD, et al. The activity of collagenase-1 is required for keratinocyte migration on a type I collagen matrix. Cell Biol. 1997;137:1445-1457.
    • (1997) Cell Biol , vol.137 , pp. 1445-1457
    • Pilcher, B.K.1    Dumin, J.A.2    Sudbeck, B.D.3
  • 84
    • 0028139044 scopus 로고
    • Collagen-stimulated induction of keratinocyte collagenase is mediated via tyrosine kinase and protein kinase C activities
    • Sudbeck BS, Parks WC, Welgus HG, et al. Collagen-stimulated induction of keratinocyte collagenase is mediated via tyrosine kinase and protein kinase C activities. J Biol Chem. 1994;269:30022-30029.
    • (1994) J Biol Chem , vol.269 , pp. 30022-30029
    • Sudbeck, B.S.1    Parks, W.C.2    Welgus, H.G.3
  • 85
    • 0030976125 scopus 로고    scopus 로고
    • Modulation of intracellular calcium levels inhibits secretion of collagenase-1 by migrating keratinocytes
    • Sudbeck BD, Pilcher BK, Pentland AP, et al. Modulation of intracellular calcium levels inhibits secretion of collagenase-1 by migrating keratinocytes. Mol Biol Cell. 1997;8:811-824.
    • (1997) Mol Biol Cell , vol.8 , pp. 811-824
    • Sudbeck, B.D.1    Pilcher, B.K.2    Pentland, A.P.3
  • 86
    • 0036885949 scopus 로고    scopus 로고
    • Elevated expression of extracellular matrix metalloproteinase inducer (CD147) and membrane-type matrix metalloproteinases in venous leg ulcers
    • Norgauer J, Hildenbrand T, Idzko M, et al. Elevated expression of extracellular matrix metalloproteinase inducer (CD147) and membrane-type matrix metalloproteinases in venous leg ulcers. Br J Dermatol. 2002;147:1180-1186.
    • (2002) Br J Dermatol , vol.147 , pp. 1180-1186
    • Norgauer, J.1    Hildenbrand, T.2    Idzko, M.3
  • 87
    • 0030880539 scopus 로고    scopus 로고
    • Upregulation of elastase in acute wounds of healthy aged humans and chronic venous leg ulcers are associated with matrix degradation
    • Herrick S, Ashcroft G, Ireland G, et al. Upregulation of elastase in acute wounds of healthy aged humans and chronic venous leg ulcers are associated with matrix degradation. Lab Invest. 1997;77:281-288.
    • (1997) Lab Invest , vol.77 , pp. 281-288
    • Herrick, S.1    Ashcroft, G.2    Ireland, G.3
  • 88
    • 0009809218 scopus 로고    scopus 로고
    • Biochemical analysis of acute and chronic wound environement
    • Tarnuzzer RW, Schultz GS. Biochemical analysis of acute and chronic wound environement. Wound Rep Reg. 1996;4:321-325.
    • (1996) Wound Rep Reg , vol.4 , pp. 321-325
    • Tarnuzzer, R.W.1    Schultz, G.S.2
  • 89
    • 15444343493 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitors: A structure activity study
    • Levy D, Lapierre F, Liang W, et al. Matrix metalloproteinase inhibitors: a structure activity study. J Med Chem. 1998;41:199-223.
    • (1998) J Med Chem , vol.41 , pp. 199-223
    • Levy, D.1    Lapierre, F.2    Liang, W.3
  • 90
    • 1842377505 scopus 로고    scopus 로고
    • Mechanism of inhibition of human matrix metalloproteinase stromelysin-1 by TIMP-1
    • Gomis-Ruth F, Maskos K, Betz M, et al. Mechanism of inhibition of human matrix metalloproteinase stromelysin-1 by TIMP-1. Nature. 1997;389:77-81.
    • (1997) Nature , vol.389 , pp. 77-81
    • Gomis-Ruth, F.1    Maskos, K.2    Betz, M.3
  • 91
    • 0030584673 scopus 로고    scopus 로고
    • X-ray structure of a hydroxamate inhibitor complex of stromelysin catalytic domain and its comparison with members of the zinc metalloproteinase superfamily
    • Dhanaraj V, Ye QZ, Johnson L, et al. X-ray structure of a hydroxamate inhibitor complex of stromelysin catalytic domain and its comparison with members of the zinc metalloproteinase superfamily. Structure. 1996;4:375-386.
    • (1996) Structure , vol.4 , pp. 375-386
    • Dhanaraj, V.1    Ye, Q.Z.2    Johnson, L.3
  • 92
    • 0030444920 scopus 로고    scopus 로고
    • Catalytic domains of matrix metalloproteinases: A molecular biology approach to drug discovery
    • Ye QZ, Hupe D, Johnson L. Catalytic domains of matrix metalloproteinases: a molecular biology approach to drug discovery. Curr Med Chem. 1996;3:407-418.
    • (1996) Curr Med Chem , vol.3 , pp. 407-418
    • Ye, Q.Z.1    Hupe, D.2    Johnson, L.3
  • 94
    • 0031460236 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitor drugs
    • Levy D, Ezrin A. Matrix metalloproteinase inhibitor drugs. Emerg Drugs. 1997;2:205-230.
    • (1997) Emerg Drugs , vol.2 , pp. 205-230
    • Levy, D.1    Ezrin, A.2
  • 95
    • 0036800192 scopus 로고    scopus 로고
    • Metalloproteinase inhibitors: Biological actions and therapeutic opportunities
    • Baker AH, Edwards DR, Murphy G. Metalloproteinase inhibitors: biological actions and therapeutic opportunities. J Cell Sci. 2002;115:3719-3727.
    • (2002) J Cell Sci , vol.115 , pp. 3719-3727
    • Baker, A.H.1    Edwards, D.R.2    Murphy, G.3
  • 96
    • 0034722898 scopus 로고    scopus 로고
    • Critical appraisal of the use of matrix metalloproteinase inhibitors in cancer treatment
    • Zucker S, Cao J, Chen WT. Critical appraisal of the use of matrix metalloproteinase inhibitors in cancer treatment. Oncogene. 2000;19:6642-6650.
    • (2000) Oncogene , vol.19 , pp. 6642-6650
    • Zucker, S.1    Cao, J.2    Chen, W.T.3
  • 97
    • 0033520042 scopus 로고    scopus 로고
    • Adenovirus-mediated overexpression of tissue inhibitor of metalloproteinase-1 reduces atherosclerotic lesions in apolipoprotein E-deficient mice
    • Rouis M, Adamy C, Duverger N, et al. Adenovirus-mediated overexpression of tissue inhibitor of metalloproteinase-1 reduces atherosclerotic lesions in apolipoprotein E-deficient mice. Circulation. 1999;100:533-540.
    • (1999) Circulation , vol.100 , pp. 533-540
    • Rouis, M.1    Adamy, C.2    Duverger, N.3
  • 98
    • 0032190478 scopus 로고    scopus 로고
    • Local overexpression of TIMP-1 prevents aortic aneurysm degeneration and rupture in a rat model
    • Allaire E, Forough R, Clowes M, et al. Local overexpression of TIMP-1 prevents aortic aneurysm degeneration and rupture in a rat model. J Clin Invest. 1998;102:1413-1420.
    • (1998) J Clin Invest , vol.102 , pp. 1413-1420
    • Allaire, E.1    Forough, R.2    Clowes, M.3


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