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Volumn 92, Issue 8, 2003, Pages 827-839

Matrix metalloproteinases and tissue inhibitors of metalloproteinases: Structure, function, and biochemistry

Author keywords

Extracellular matrix; Protease; Protease inhibitors

Indexed keywords

COLLAGENASE 3; GELATINASE A; GELATINASE B; INTERSTITIAL COLLAGENASE; MATRILYSIN; MATRILYSIN 2; MATRIX METALLOPROTEINASE; MATRIX METALLOPROTEINASE 14; NEUTROPHIL COLLAGENASE; STROMELYSIN; STROMELYSIN 2; STROMELYSIN 3; TISSUE INHIBITOR OF METALLOPROTEINASE; UNCLASSIFIED DRUG;

EID: 0037693895     PISSN: 00097330     EISSN: None     Source Type: Journal    
DOI: 10.1161/01.RES.0000070112.80711.3D     Document Type: Review
Times cited : (3986)

References (158)
  • 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 J.F., Jr.2
  • 2
    • 0035188727 scopus 로고    scopus 로고
    • How matrix metalloproteinases regulate cell behavior
    • Stemlicht 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
    • Stemlicht, 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, Thorgeirsson UP. 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    Thorgeirsson, U.P.4
  • 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
    • 0035800880 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibition after myocardial infarction: A new approach to prevent heart failure?
    • Creemers EE, Cleutjens JP, Smits JF, Daemen MJ. Matrix metalloproteinase inhibition after myocardial infarction: a new approach to prevent heart failure? Circ Res. 2001;89:201-210.
    • (2001) Circ Res , vol.89 , pp. 201-210
    • Creemers, E.E.1    Cleutjens, J.P.2    Smits, J.F.3    Daemen, M.J.4
  • 7
    • 0037155057 scopus 로고    scopus 로고
    • Matrix metalloproteinases in vascular remodeling and atherogenesis: The good, the bad, and the ugly
    • Galis ZS, Khatri JJ. Matrix metalloproteinases in vascular remodeling and atherogenesis: the good, the bad, and the ugly. Circ Res. 2002;90:251-262.
    • (2002) Circ Res , vol.90 , pp. 251-262
    • Galis, Z.S.1    Khatri, J.J.2
  • 8
    • 0037155784 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Regulation and dysregulation in the failing heart
    • Spinale FG. Matrix metalloproteinases: regulation and dysregulation in the failing heart. Circ Res. 2002;90:520-530.
    • (2002) Circ Res , vol.90 , pp. 520-530
    • Spinale, F.G.1
  • 9
    • 0034052480 scopus 로고    scopus 로고
    • A novel hydra matrix metalloproteinase (HMMP) functions in extra-cellular matrix degradation, morphogenesis and the maintenance of differentiated cells in the foot process
    • Leontovich AA, Zhang J, Shimokawa K, Nagase H, Sarras MP Jr. A novel hydra matrix metalloproteinase (HMMP) functions in extra-cellular 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    Nagase, H.4    Sarras M.P., Jr.5
  • 10
    • 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
  • 11
    • 0033521036 scopus 로고    scopus 로고
    • Matrix metalloproteinase homologues from Arabidopsis thaliana: Expression and activity
    • Maidment JM, Moore D, Murphy GP, Murphy G, Clark IM. 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    Murphy, G.4    Clark, I.M.5
  • 13
    • 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 specific 3/4- and 1/4-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 specific 3/4- and 1/4-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
  • 14
    • 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, Murphy G. 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    Murphy, G.4
  • 15
    • 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, Nakao S, Suzuki T, Itohara S. 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    Nakao, S.4    Suzuki, T.5    Itohara, S.6
  • 17
    • 0025026410 scopus 로고
    • Mechanisms of activation of tissue procollagenase by matrix metalloproteinase 3 (stromelysin)
    • Suzuki K, Enghild JJ, Morodomi T, Salvesen G, Nagase H. 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    Salvesen, G.4    Nagase, H.5
  • 18
    • 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
  • 19
    • 0034617262 scopus 로고    scopus 로고
    • Identification and characterization of human endometase (matrix metalloproteinase-26) from endometrial tumor
    • Park HI, Ni J, Gerkema FE, Liu D, Belozerov VE, Sang QX. 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    Liu, D.4    Belozerov, V.E.5    Sang, Q.X.6
  • 20
    • 0031025218 scopus 로고    scopus 로고
    • Membrane type I matrix metalloproteinase digests interstitial collagens and other extracellular matrix macromolecules
    • Ohuchi E, Imai K, Fujii Y, Sato H, Seiki M, Okada Y. Membrane type I 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    Sato, H.4    Seiki, M.5    Okada, Y.6
  • 22
    • 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
  • 25
    • 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
  • 26
    • 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
  • 28
    • 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, Llano E, Mattei MG, Apte S, Murphy G, Lopéz-Otín C. 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    Llano, E.4    Mattei, M.G.5    Apte, S.6    Murphy, G.7    Lopéz-Otín, C.8
  • 29
    • 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, Krawinkel U, Sedlacek R. 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    Krawinkel, U.4    Sedlacek, R.5
  • 30
    • 0035133863 scopus 로고    scopus 로고
    • Reduced hydrolysis of amelogenin may result in X-linked amelogenesis imperfecta
    • Li W, Gibson CW, Abrams WR, Andrews DW, DenBesten PK. Reduced hydrolysis of amelogenin may result in X-linked amelogenesis imperfecta. Matrix Biol. 2001;19:755-760.
    • (2001) Matrix Biol , vol.19 , pp. 755-760
    • Li, W.1    Gibson, C.W.2    Abrams, W.R.3    Andrews, D.W.4    DenBesten, P.K.5
  • 31
    • 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;273:17893-17900.
    • (1998) J Biol Chem , vol.273 , pp. 17893-17900
    • Yang, M.1    Kurkinen, M.2
  • 32
    • 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, Knäuper V, Murphy G, López-Otín C. 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    Knäuper, V.4    Murphy, G.5    López-Otín, C.6
  • 33
    • 0034721850 scopus 로고    scopus 로고
    • Cysteine array matrix metalloproteinase (CA-MMP)/MMP-23 is a type II transmembrane matrix metalloproteinase regulated by a single cleavage for both secretion and activation
    • Pei D, Kang T, Qi H. Cysteine array matrix metalloproteinase (CA-MMP)/MMP-23 is a type II transmembrane matrix metalloproteinase regulated by a single cleavage for both secretion and activation. J Biol Chem. 2000;275:33988-33997.
    • (2000) J Biol Chem , vol.275 , pp. 33988-33997
    • Pei, D.1    Kang, T.2    Qi, H.3
  • 34
    • 0035819913 scopus 로고    scopus 로고
    • MMP-28, a new human matrix metallo-proteinase with an unusual cysteine-switch sequence is widely expressed in tumors
    • Marchenko GN, Strongin AY. MMP-28, a new human matrix metallo-proteinase 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
  • 35
    • 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, Parks WC. 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    Parks, W.C.4
  • 38
    • 0027515396 scopus 로고
    • Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the "metzincins"
    • Bode W, Gomis-Rüth FX, Stöckler W. Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the "metzincins." FEBS Lett. 1993;331:134-140.
    • (1993) FEBS Lett , vol.331 , pp. 134-140
    • Bode, W.1    Gomis-Rüth, F.X.2    Stöckler, W.3
  • 41
    • 0035920182 scopus 로고    scopus 로고
    • Gelatin-binding region of human matrix metalloproteinase-2: Solution structure, dynamics, and function of the COL-23 two-domain construct
    • Briknarova K, Gehrmann M, Bányai L, Tordai H, Patthy L, Llinas M. Gelatin-binding region of human matrix metalloproteinase-2: solution structure, dynamics, and function of the COL-23 two-domain construct. J Biol Chem. 2001;276:27613-27621.
    • (2001) J Biol Chem , vol.276 , pp. 27613-27621
    • Briknarova, K.1    Gehrmann, M.2    Bányai, L.3    Tordai, H.4    Patthy, L.5    Llinas, M.6
  • 43
    • 0030669224 scopus 로고    scopus 로고
    • Kinetic analysis of the binding of human matrix metalloproteinase-2 and -9 to tissue inhibitor of metalloproteinase (TIMP)-I and TIMP-2
    • Olson MW, Gervasi DC, Mobashery S, Fridman R. Kinetic analysis of the binding of human matrix metalloproteinase-2 and -9 to tissue inhibitor of metalloproteinase (TIMP)-I and TIMP-2. J Biol Chem. 1997;272:29975-29983.
    • (1997) J Biol Chem , vol.272 , pp. 29975-29983
    • Olson, M.W.1    Gervasi, D.C.2    Mobashery, S.3    Fridman, R.4
  • 44
    • 0346319016 scopus 로고    scopus 로고
    • The matrix metalloproteinase 9 (mmp-9) hemopexin domain is a novel gelatin binding domain and acts as an antagonist
    • Roeb E, Schleinkofer K, Kernebeck T, Potsch S, Jansen B, Behrmann I, Matem S, Grotzinger J. The matrix metalloproteinase 9 (mmp-9) hemopexin domain is a novel gelatin binding domain and acts as an antagonist. J Biol Chem. 2002;277:50326-50332.
    • (2002) J Biol Chem , vol.277 , pp. 50326-50332
    • Roeb, E.1    Schleinkofer, K.2    Kernebeck, T.3    Potsch, S.4    Jansen, B.5    Behrmann, I.6    Matem, S.7    Grotzinger, J.8
  • 45
    • 0037188508 scopus 로고    scopus 로고
    • Structural insight into the complex formation of latent matrix metalloproteinase 2 with tissue inhibitor of metalloproteinase 2
    • Morgunova E, Tuuttila A, Bergmann U, Tryggvason K. Structural insight into the complex formation of latent matrix metalloproteinase 2 with tissue inhibitor of metalloproteinase 2. Proc Natl Acad Sci U S A. 2002;99:7414-7419.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 7414-7419
    • Morgunova, E.1    Tuuttila, A.2    Bergmann, U.3    Tryggvason, K.4
  • 47
    • 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
  • 48
    • 0025025442 scopus 로고
    • The cysteine switch: A principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family
    • Van Wart HE, Birkedal-Hansen H. The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family. Proc Natl Acad Sci U S A. 1990;87:5578-5582.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 5578-5582
    • Van Wart, H.E.1    Birkedal-Hansen, H.2
  • 49
    • 0027492897 scopus 로고
    • Disruption of the cysteine-75 and zinc ion coordination is not sufficient to activate the precursor of human matrix metalloproteinase 3 (stromelysin 1)
    • Chen LC, Noelken ME, Nagase H. Disruption of the cysteine-75 and zinc ion coordination is not sufficient to activate the precursor of human matrix metalloproteinase 3 (stromelysin 1). Biochemistry, 1993;32:10289-10295.
    • (1993) Biochemistry , vol.32 , pp. 10289-10295
    • Chen, L.C.1    Noelken, M.E.2    Nagase, H.3
  • 50
    • 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 E.D., Jr.2    Nagase, H.3
  • 51
    • 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, Salvesen G. 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    Salvesen, G.4
  • 53
    • 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
  • 54
    • 0031883960 scopus 로고    scopus 로고
    • Expression of human pro-matrix metalloproteinase 3 that lacks the N-terminal 34 residues in Escherichia coli: Autoactivation and interaction with tissue inhibitor of metalloproteinase 1 (TIMP-1)
    • Suzuki K, Kan CC, Hung W, Gehring MR, Brew K, Nagase H. Expression of human pro-matrix metalloproteinase 3 that lacks the N-terminal 34 residues in Escherichia coli: autoactivation and interaction with tissue inhibitor of metalloproteinase 1 (TIMP-1). Biol Chem. 1998;379:185-191.
    • (1998) Biol Chem , vol.379 , pp. 185-191
    • Suzuki, K.1    Kan, C.C.2    Hung, W.3    Gehring, M.R.4    Brew, K.5    Nagase, H.6
  • 55
    • 0029014101 scopus 로고
    • Furin-dependent intracellular activation of the human stromelysin 3 zymogen
    • Pei D, Weiss SJ. Furin-dependent intracellular activation of the human stromelysin 3 zymogen. Nature. 1995;375:244-247.
    • (1995) Nature , vol.375 , pp. 244-247
    • Pei, D.1    Weiss, S.J.2
  • 57
    • 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, Murphy G. 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    Murphy, G.4
  • 58
    • 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, Seiki M. 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    Seiki, M.4
  • 59
    • 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, Nakano A, Knäuper V, Murphy G, López-Otín C. 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    Nakano, A.4    Knäuper, V.5    Murphy, G.6    López-Otín, C.7
  • 60
    • 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
  • 61
    • 0034640282 scopus 로고    scopus 로고
    • Membrane type 4 matrix metalloproteinase (MMP17) has tumor necrosis factor-α convertase activity but does not activate pro-MMP2
    • English WR, Puente XS, Freije JM, Knäuper V, Amour A, Merryweather A, López-Otín C, Murphy G. Membrane type 4 matrix metalloproteinase (MMP17) has tumor necrosis factor-α convertase activity but does not activate pro-MMP2. 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    Knäuper, V.4    Amour, A.5    Merryweather, A.6    López-Otín, C.7    Murphy, G.8
  • 62
    • 0028907318 scopus 로고
    • Mechanism of cell surface activation of 72-kDa type IV collagenase: Isolation of the activated form of the membrane metalloprotease
    • Strongin AY, Collier I, Bannikov G, Marmer BL, Grant GA, Goldberg GI. Mechanism of cell surface activation of 72-kDa type IV collagenase: isolation of the activated form of the membrane metalloprotease. 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    Marmer, B.L.4    Grant, G.A.5    Goldberg, G.I.6
  • 64
    • 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
  • 65
    • 0035801473 scopus 로고    scopus 로고
    • Homophilic complex formation of MT1-MMP facilitates proMMP-2 activation on the cell surface and promotes tumor cell invasion
    • Itoh Y, Takamura A, Ito N, Maru Y, Sato H, Suenaga N, Aoki T, Seiki M. Homophilic complex formation of MT1-MMP facilitates proMMP-2 activation on the cell surface and promotes tumor cell invasion. EMBO J. 2001;20:4782-4793.
    • (2001) EMBO J , vol.20 , pp. 4782-4793
    • Itoh, Y.1    Takamura, A.2    Ito, N.3    Maru, Y.4    Sato, H.5    Suenaga, N.6    Aoki, T.7    Seiki, M.8
  • 66
    • 0034141350 scopus 로고    scopus 로고
    • Analysis of tissue inhibitor of metalloproteinases-2 effect on pro-matrix metalloproteinase-2 activation by membrane-type I matrix metalloproteinase using baculovirus/insect-cell expression system
    • Jo Y, Yeon J, Kim HJ, Lee ST. Analysis of tissue inhibitor of metalloproteinases-2 effect on pro-matrix metalloproteinase-2 activation by membrane-type I matrix metalloproteinase using baculovirus/insect-cell expression system. Biochem J. 2000;345:511-519.
    • (2000) Biochem J , vol.345 , pp. 511-519
    • Jo, Y.1    Yeon, J.2    Kim, H.J.3    Lee, S.T.4
  • 67
    • 0035861560 scopus 로고    scopus 로고
    • Cellular activation of MMP-2 (gelatinase A) by MT2-MMP occurs via a TIMP-2-independent pathway
    • Morrison CJ, Butler GS, Bigg HF, Roberts CR, Soloway PD, Overall CM. Cellular activation of MMP-2 (gelatinase A) by MT2-MMP occurs via a TIMP-2-independent pathway. J Biol Chem. 2001;276:47402-47410.
    • (2001) J Biol Chem , vol.276 , pp. 47402-47410
    • Morrison, C.J.1    Butler, G.S.2    Bigg, H.F.3    Roberts, C.R.4    Soloway, P.D.5    Overall, C.M.6
  • 69
    • 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-Otín C, Smith B, Atkinson SJ, Stanton H, Hembry RM, Murphy G. 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. 1996;271:17124-17131.
    • (1996) J Biol Chem , vol.271 , pp. 17124-17131
    • Knäuper, V.1    Will, H.2    López-Otín, C.3    Smith, B.4    Atkinson, S.J.5    Stanton, H.6    Hembry, R.M.7    Murphy, G.8
  • 70
    • 0037021469 scopus 로고    scopus 로고
    • Cellular activation of proMMP-13 by MT1-MMP depends on the C-terminal domain of MMP-13
    • Knäuper V, Bailey L, Worley JR, Soloway P, Patterson ML, Murphy G. Cellular activation of proMMP-13 by MT1-MMP depends on the C-terminal domain of MMP-13. FEBS Lett. 2002;532:127-130.
    • (2002) FEBS Lett , vol.532 , pp. 127-130
    • Knäuper, V.1    Bailey, L.2    Worley, J.R.3    Soloway, P.4    Patterson, M.L.5    Murphy, G.6
  • 71
    • 0029758751 scopus 로고    scopus 로고
    • Human matrix metalloproteinase specificity studies using collagen sequence-based synthetic peptides
    • Nagase H, Fields GB. Human matrix metalloproteinase specificity studies using collagen sequence-based synthetic peptides. Biopolymers. 1996;40:399-416.
    • (1996) Biopolymers , vol.40 , pp. 399-416
    • Nagase, H.1    Fields, G.B.2
  • 73
    • 0037942320 scopus 로고    scopus 로고
    • Substrate specificity of MMPs
    • Clendenninn NJ, Appelt K, eds. Totowa, NJ: Humana Press Inc
    • Nagase H. Substrate specificity of MMPs. In: Clendenninn NJ, Appelt K, eds. Matrix Metalloproteinase Inhibitors in Cancer Therapy. Totowa, NJ: Humana Press Inc; 2001:39-66.
    • (2001) Matrix Metalloproteinase Inhibitors in Cancer Therapy , pp. 39-66
    • Nagase, H.1
  • 75
    • 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 JM, Doyle GA, Fliszar CJ, Ye QZ, Johnson LL, Shapiro SD, Welgus HG, Senior RM. The structural basis for the elastolytic activity of the 92-kDa and 72-kDa gelatinases: role of the fibronectin type H-like repeats. J Biol Chem. 1996;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
  • 76
    • 0034703074 scopus 로고    scopus 로고
    • Identification of the (183)RWTNNFREY(191) region as a critical segment of matrix metalloproteinase 1 for the expression of collagenolytic activity
    • Chung L, Shimokawa K, Dinakarpandian D, Grams F, Fields GB, Nagase H. Identification of the (183)RWTNNFREY(191) region as a critical segment of matrix metalloproteinase 1 for the expression of collagenolytic activity. J Biol Chem. 2000;275:29610-29617.
    • (2000) J Biol Chem , vol.275 , pp. 29610-29617
    • Chung, L.1    Shimokawa, K.2    Dinakarpandian, D.3    Grams, F.4    Fields, G.B.5    Nagase, H.6
  • 77
    • 0036741135 scopus 로고    scopus 로고
    • Molecular determinants of metalloproteinase substrate specificity: Matrix metalloproteinase substrate binding domains, modules, and exosites
    • Overall CM. Molecular determinants of metalloproteinase substrate specificity: matrix metalloproteinase substrate binding domains, modules, and exosites. Mol Biotechnol. 2002;22:51-86.
    • (2002) Mol Biotechnol , vol.22 , pp. 51-86
    • Overall, C.M.1
  • 79
    • 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, Krane SM, Welgus HG, Parks WC. The activity of collagenase-1 is required for keratinocyte migration on a type I collagen matrix. J Cell Biol. 1997:137:1445-1457.
    • (1997) J Cell Biol , vol.137 , pp. 1445-1457
    • Pilcher, B.K.1    Dumin, J.A.2    Sudbeck, B.D.3    Krane, S.M.4    Welgus, H.G.5    Parks, W.C.6
  • 82
    • 0034614939 scopus 로고    scopus 로고
    • Role of cell surface metalloprotease MT1-MMP in epithelial cell migration over laminin-5
    • Koshikawa N, Giannelli G, Cirulli V, Miyazaki K, Quaranta V. Role of cell surface metalloprotease MT1-MMP in epithelial cell migration over laminin-5. J Cell Biol. 2000;148:615-624.
    • (2000) J Cell Biol , vol.148 , pp. 615-624
    • Koshikawa, N.1    Giannelli, G.2    Cirulli, V.3    Miyazaki, K.4    Quaranta, V.5
  • 83
    • 0035947766 scopus 로고    scopus 로고
    • Membrane-type I matrix metalloproteinase cleaves CD44 and promotes cell migration
    • Kajita M, Itoh Y, Chiba T, Mori H, Okada A, Kinoh H, Seiki M. Membrane-type I matrix metalloproteinase cleaves CD44 and promotes cell migration. J Cell Biol.;2001;153:893-904.
    • (2001) J Cell Biol , vol.153 , pp. 893-904
    • Kajita, M.1    Itoh, Y.2    Chiba, T.3    Mori, H.4    Okada, A.5    Kinoh, H.6    Seiki, M.7
  • 84
    • 0036896962 scopus 로고    scopus 로고
    • Metalloproteinase-dependent predegeneration in vitro enhances axonal regeneration within acellular peripheral nerve grafts
    • Krekoski CA, Neubauer D, Graham JB, Muir D. Metalloproteinase-dependent predegeneration in vitro enhances axonal regeneration within acellular peripheral nerve grafts. J Neurosci. 2002;22:10408-10415.
    • (2002) J Neurosci , vol.22 , pp. 10408-10415
    • Krekoski, C.A.1    Neubauer, D.2    Graham, J.B.3    Muir, D.4
  • 85
    • 0035479845 scopus 로고    scopus 로고
    • Matrix metalloproteinases: They're not just for matrix anymore!
    • McCawley LJ, Matrisian LM. Matrix metalloproteinases: they're not just for matrix anymore! Curr Opin Cell Biol. 2001;13:534-540.
    • (2001) Curr Opin Cell Biol , vol.13 , pp. 534-540
    • McCawley, L.J.1    Matrisian, L.M.2
  • 86
    • 0025944065 scopus 로고
    • The N-terminal domain of tissue inhibitor of metalloproteinases retains metalloproteinase inhibitory activity
    • Murphy G, Houbrechts A, Cockett MI, Williamson RA, O'Shea M, Docherty AJ. 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    Williamson, R.A.4    O'Shea, M.5    Docherty, A.J.6
  • 88
    • 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, Murphy G, Docherty AJ, Freedman RB, Feeney J. 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    Murphy, G.4    Docherty, A.J.5    Freedman, R.B.6    Feeney, J.7
  • 90
    • 0032167522 scopus 로고    scopus 로고
    • Crystal structure of the complex formed by the membrane type I-matrix metalloproteinase with the tissue inhibitor of metalloproteinases-2, the soluble progelatinase A receptor
    • Fernandez-Catalan C, Bode W, Huber R, Turk D, Calvete JJ, Lichte A, Tschesche H, Maskos K. Crystal structure of the complex formed by the membrane type I-matrix metalloproteinase with the tissue inhibitor of metalloproteinases-2, the soluble progelatinase A receptor. EMBO J. 1998;17:5238-5248.
    • (1998) EMBO J , vol.17 , pp. 5238-5248
    • Fernandez-Catalan, C.1    Bode, W.2    Huber, R.3    Turk, D.4    Calvete, J.J.5    Lichte, A.6    Tschesche, H.7    Maskos, K.8
  • 91
    • 0030016342 scopus 로고    scopus 로고
    • The soluble catalytic domain of membrane type I 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, Smith B, Murphy G. The soluble catalytic domain of membrane type I 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    Smith, B.4    Murphy, G.5
  • 95
    • 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, Brew K. 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    Brew, K.4
  • 96
    • 0034613296 scopus 로고    scopus 로고
    • TIMP-3 binds to sulfated glycosaminoglycans of the extracellular matrix
    • Yu WH, Yu S, Meng Q, Brew K, Woessner JF Jr. 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    Brew, K.4    Woessner J.F., Jr.5
  • 98
    • 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
  • 99
    • 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
  • 101
    • 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, Starcher B, Clowes AW. 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    Starcher, B.4    Clowes, A.W.5
  • 102
    • 0019739066 scopus 로고
    • α2-macroglobulin
    • Barrett AJ. α2-Macroglobulin. Methods Enzymol. 1981;80:737-754.
    • (1981) Methods Enzymol , vol.80 , pp. 737-754
    • Barrett, A.J.1
  • 103
    • 0022861319 scopus 로고
    • Preferential binding of collagenase to α2-macroglobulin in the presence of the tissue inhibitor of metalloproteinases
    • Cawston TE, Mercer E. Preferential binding of collagenase to α2-macroglobulin in the presence of the tissue inhibitor of metalloproteinases. FEBS Lett. 1986;209:9-12.
    • (1986) FEBS Lett , vol.209 , pp. 9-12
    • Cawston, T.E.1    Mercer, E.2
  • 104
    • 0035023342 scopus 로고    scopus 로고
    • Tissue factor pathway inhibitor-2 is a novel inhibitor of matrix metalloproteinases with implications for atherosclerosis
    • Herman MP, Sukhova GK, Kisiel W, Foster D, Kehry MR, Libby P, Schonbeck U. Tissue factor pathway inhibitor-2 is a novel inhibitor of matrix metalloproteinases with implications for atherosclerosis. J Clin Invest. 2001;107:1117-1126.
    • (2001) J Clin Invest , vol.107 , pp. 1117-1126
    • Herman, M.P.1    Sukhova, G.K.2    Kisiel, W.3    Foster, D.4    Kehry, M.R.5    Libby, P.6    Schonbeck, U.7
  • 105
    • 0033955104 scopus 로고    scopus 로고
    • Post-translational proteolytic processing of procollagen C-terminal proteinase enhancer releases a metalloproteinase inhibitor
    • Mott JD, Thomas CL, Rosenbach MT, Takahara K, Greenspan DS, Banda MJ. Post-translational proteolytic processing of procollagen C-terminal proteinase enhancer releases a metalloproteinase inhibitor. J Biol Chem. 2000;275:1384-1390.
    • (2000) J Biol Chem , vol.275 , pp. 1384-1390
    • Mott, J.D.1    Thomas, C.L.2    Rosenbach, M.T.3    Takahara, K.4    Greenspan, D.S.5    Banda, M.J.6
  • 106
    • 0027254060 scopus 로고
    • A metalloproteinase inhibitor domain in Alzheimer amyloid protein precursor
    • Miyazaki K, Hasegawa M, Funahashi K, Umeda M. A metalloproteinase inhibitor domain in Alzheimer amyloid protein precursor. Nature. 1993;362:839-841.
    • (1993) Nature , vol.362 , pp. 839-841
    • Miyazaki, K.1    Hasegawa, M.2    Funahashi, K.3    Umeda, M.4
  • 109
    • 0037423212 scopus 로고    scopus 로고
    • Chlorotoxin inhibits glioma cell invasion via matrix metalloproteinase-2
    • Deshane J, Garner CC, Sontheimer H. Chlorotoxin inhibits glioma cell invasion via matrix metalloproteinase-2. J Biol Chem. 2003;278:4135-4144.
    • (2003) J Biol Chem , vol.278 , pp. 4135-4144
    • Deshane, J.1    Garner, C.C.2    Sontheimer, H.3
  • 111
    • 0026601513 scopus 로고
    • Tissue inhibitor of metalloproteinase-2 (TIMP-2) has erythroid-potentiating activity
    • Stetler-Stevenson WG, Bersch N, Golde DW. Tissue inhibitor of metalloproteinase-2 (TIMP-2) has erythroid-potentiating activity. FEBS Lett. 1992;296:231-234.
    • (1992) FEBS Lett , vol.296 , pp. 231-234
    • Stetler-Stevenson, W.G.1    Bersch, N.2    Golde, D.W.3
  • 112
    • 0026568011 scopus 로고
    • Growthpromoting activity of tissue inhibitor of metalloproteinases-1 (TIMP-1) for a wide range of cells: A possible new growth factor in serum
    • Hayakawa T, Yamashita K, Tanzawa K, Uchijima E, Iwata K. Growthpromoting activity of tissue inhibitor of metalloproteinases-1 (TIMP-1) for a wide range of cells: a possible new growth factor in serum. FEBS Lett. 1992;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
  • 113
    • 0028132867 scopus 로고
    • Cell growthpromoting activity of tissue inhibitor of metalloproteinases-2 (TIMP-2)
    • Hayakawa T, Yamashita K, Ohuchi E, Shinagawa A. Cell growthpromoting activity of tissue inhibitor of metalloproteinases-2 (TIMP-2). J Cell Sci. 1994;107:2373-2379.
    • (1994) J Cell Sci , vol.107 , pp. 2373-2379
    • Hayakawa, T.1    Yamashita, K.2    Ohuchi, E.3    Shinagawa, A.4
  • 114
    • 0031750878 scopus 로고    scopus 로고
    • Cell cycle-associated accumulation of tissue inhibitor of metalloproteinases-1 (TIMP-1) in the nuclei of human gingival fibroblasts
    • Zhao WQ, Li H, Yamashita K, Guo XK, Hoshino T, Yoshida S, Shinya T, Hayakawa T. Cell cycle-associated accumulation of tissue inhibitor of metalloproteinases-1 (TIMP-1) in the nuclei of human gingival fibroblasts. J Cell Sci. 1998;111:1147-1153.
    • (1998) J Cell Sci , vol.111 , pp. 1147-1153
    • Zhao, W.Q.1    Li, H.2    Yamashita, K.3    Guo, X.K.4    Hoshino, T.5    Yoshida, S.6    Shinya, T.7    Hayakawa, T.8
  • 115
    • 0033551186 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinases-1 (TIMP-1) binds to the cell surface and translocates to the nucleus of human MCF-7 breast carcinoma cells
    • Ritter LM, Garfield SH, Thorgeirsson UP. Tissue inhibitor of metalloproteinases-1 (TIMP-1) binds to the cell surface and translocates to the nucleus of human MCF-7 breast carcinoma cells. Biochem Biophys Res Commun. 1999;257:494-499.
    • (1999) Biochem Biophys Res Commun , vol.257 , pp. 494-499
    • Ritter, L.M.1    Garfield, S.H.2    Thorgeirsson, U.P.3
  • 116
    • 0033135715 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinase-2 stimulates mesenchymal growth and regulates epithelial branching during morphogenesis of the rat metanephros
    • Barasch J, Yang J, Qiao J, Tempst P, Erdjument-Bromage H, Leung W, Oliver JA. Tissue inhibitor of metalloproteinase-2 stimulates mesenchymal growth and regulates epithelial branching during morphogenesis of the rat metanephros. J Clin Invest. 1999;103:1299-1307.
    • (1999) J Clin Invest , vol.103 , pp. 1299-1307
    • Barasch, J.1    Yang, J.2    Qiao, J.3    Tempst, P.4    Erdjument-Bromage, H.5    Leung, W.6    Oliver, J.A.7
  • 117
    • 0027383944 scopus 로고
    • Tissue inhibitor of metalloproteinases-2 inhibits bFGF-induced human microvascular endothelial cell proliferation
    • Murphy AN, Unsworth EJ, Stetler-Stevenson WG. Tissue inhibitor of metalloproteinases-2 inhibits bFGF-induced human microvascular endothelial cell proliferation. J Cell Physiol. 1993;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
  • 118
    • 0037134536 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinase-3 induces a Fas-associated death domain-dependent type II apoptotic pathway
    • Bond M, Murphy G, Bennett MR, Newby AC, Baker AH. Tissue inhibitor of metalloproteinase-3 induces a Fas-associated death domain-dependent type II apoptotic pathway. J Biol Chem. 2002;277:13787-13795.
    • (2002) J Biol Chem , vol.277 , pp. 13787-13795
    • Bond, M.1    Murphy, G.2    Bennett, M.R.3    Newby, A.C.4    Baker, A.H.5
  • 119
    • 0038297557 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinase-3 induces apoptosis in melanoma cells by stabilization of death receptors
    • Ahonen M, Poukkula M, Baker AH, Kashiwagi M, Nagase H, Erikson JE, Kähäri VM. Tissue inhibitor of metalloproteinase-3 induces apoptosis in melanoma cells by stabilization of death receptors. Oncogene. 2003;22:2121-2134.
    • (2003) Oncogene , vol.22 , pp. 2121-2134
    • Ahonen, M.1    Poukkula, M.2    Baker, A.H.3    Kashiwagi, M.4    Nagase, H.5    Erikson, J.E.6    Kähäri, V.M.7
  • 121
    • 0032529290 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinase (TIMP)-1 induces differentiation and an antiapoptotic phenotype in germinal center B cells
    • Guedez L, Courtemanch L, Stetler-Stevenson M. Tissue inhibitor of metalloproteinase (TIMP)-1 induces differentiation and an antiapoptotic phenotype in germinal center B cells. Blood. 1998;92:1342-1349.
    • (1998) Blood , vol.92 , pp. 1342-1349
    • Guedez, L.1    Courtemanch, L.2    Stetler-Stevenson, M.3
  • 122
    • 0028097367 scopus 로고
    • Mutations in the tissue inhibitor of metalloproteinases-3 (TIMP3) in patients with Sorsby's fundus dystrophy
    • Weber BH, Vogt G, Pruett RC, Stohr H, Felbor U. Mutations in the tissue inhibitor of metalloproteinases-3 (TIMP3) in patients with Sorsby's fundus dystrophy. Nat Genet. 1994;8:352-356.
    • (1994) Nat Genet , vol.8 , pp. 352-356
    • Weber, B.H.1    Vogt, G.2    Pruett, R.C.3    Stohr, H.4    Felbor, U.5
  • 123
    • 0031799120 scopus 로고    scopus 로고
    • Sorsby's fundus dystrophy: A genetically homogeneous disease
    • Felbor U. Weber BH. Sorsby's fundus dystrophy: a genetically homogeneous disease. Ophthalmologe. 1998;95:287-290.
    • (1998) Ophthalmologe , vol.95 , pp. 287-290
    • Felbor, U.1    Weber, B.H.2
  • 124
    • 0034282898 scopus 로고    scopus 로고
    • A novel tissue inhibitor of metalloproteinases-3 mutation reveals a common molecular phenotype in Sorsby's fundus dystrophy
    • Langton KP, McKie N, Curtis A, Goodship JA, Bond PM, Barker MD, Clarke M. A novel tissue inhibitor of metalloproteinases-3 mutation reveals a common molecular phenotype in Sorsby's fundus dystrophy. J Biol Chem. 2000;275:27027-27031.
    • (2000) J Biol Chem , vol.275 , pp. 27027-27031
    • Langton, K.P.1    McKie, N.2    Curtis, A.3    Goodship, J.A.4    Bond, P.M.5    Barker, M.D.6    Clarke, M.7
  • 125
    • 0031668129 scopus 로고    scopus 로고
    • A novel splice site mutation in the tissue inhibitor of the metalloproteinases-3 gene in Sorsby's fundus dystrophy with unusual clinical features
    • Tabata Y, Isashiki Y, Kamimura K, Nakao K, Ohba N. A novel splice site mutation in the tissue inhibitor of the metalloproteinases-3 gene in Sorsby's fundus dystrophy with unusual clinical features. Hum Genet. 1998;103:179-182.
    • (1998) Hum Genet , vol.103 , pp. 179-182
    • Tabata, Y.1    Isashiki, Y.2    Kamimura, K.3    Nakao, K.4    Ohba, N.5
  • 126
    • 0037134433 scopus 로고    scopus 로고
    • Expression of Sorsby's fundus dystrophy mutations in human retinal pigment epithelial cells reduces matrix metalloproteinase inhibition and may promote angiogenesis
    • Qi JH, Ebrahem Q, Yeow K, Edwards DR, Fox PL, Anand-Apte B. Expression of Sorsby's fundus dystrophy mutations in human retinal pigment epithelial cells reduces matrix metalloproteinase inhibition and may promote angiogenesis. J Biol Chem. 2002;277:13394-13400.
    • (2002) J Biol Chem , vol.277 , pp. 13394-13400
    • Qi, J.H.1    Ebrahem, Q.2    Yeow, K.3    Edwards, D.R.4    Fox, P.L.5    Anand-Apte, B.6
  • 127
    • 0036154168 scopus 로고    scopus 로고
    • Sorsby's fundus dystrophy tissue inhibitor of metalloproteinases-3 (TIMP-3) mutants have unimpaired matrix metalloproteinase inhibitory activities, but affect cell adhesion to the extracellular matrix
    • Yeow KM, Kishnani NS, Hutton M, Hawkes SP, Murphy G, Edwards DR. Sorsby's fundus dystrophy tissue inhibitor of metalloproteinases-3 (TIMP-3) mutants have unimpaired matrix metalloproteinase inhibitory activities, but affect cell adhesion to the extracellular matrix. Matrix Biol. 2002;21:75-88.
    • (2002) Matrix Biol , vol.21 , pp. 75-88
    • Yeow, K.M.1    Kishnani, N.S.2    Hutton, M.3    Hawkes, S.P.4    Murphy, G.5    Edwards, D.R.6
  • 129
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex N, Peitsch MC. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis. 1997;18:2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 130
    • 0029090299 scopus 로고
    • Release of biological activities from quiescent fibronectin by a conformational change and limited proteolysis by matrix metalloproteinases
    • Fukai F, Ohtaki M, Fujii N, Yajima H, Ishii T, Nishizawa Y, Miyazaki K, Katayama T. Release of biological activities from quiescent fibronectin by a conformational change and limited proteolysis by matrix metalloproteinases. Biochemistry. 1995;34:11453-11459.
    • (1995) Biochemistry , vol.34 , pp. 11453-11459
    • Fukai, F.1    Ohtaki, M.2    Fujii, N.3    Yajima, H.4    Ishii, T.5    Nishizawa, Y.6    Miyazaki, K.7    Katayama, T.8
  • 131
    • 0028927484 scopus 로고
    • Suppression of ICE and apoptosis in mammary epithelial cells by extracellular matrix
    • Boudreau N, Sympson CJ, Werb Z, Bissell MJ. Suppression of ICE and apoptosis in mammary epithelial cells by extracellular matrix. Science. 1995;267:891-893.
    • (1995) Science , vol.267 , pp. 891-893
    • Boudreau, N.1    Sympson, C.J.2    Werb, Z.3    Bissell, M.J.4
  • 132
    • 0028302990 scopus 로고
    • Targeted expression of stromelysin-1 in mammary gland provides evidence for a role of proteinases in branching morphogenesis and the requirement for an intact basement membrane for tissue-specific gene expression
    • Sympson CJ, Talhouk RS, Alexander CM, Chin JR, Clift SM, Bissell MJ, Werb Z. Targeted expression of stromelysin-1 in mammary gland provides evidence for a role of proteinases in branching morphogenesis and the requirement for an intact basement membrane for tissue-specific gene expression. J Cell Biol. 1994;125:681-693.
    • (1994) J Cell Biol , vol.125 , pp. 681-693
    • Sympson, C.J.1    Talhouk, R.S.2    Alexander, C.M.3    Chin, J.R.4    Clift, S.M.5    Bissell, M.J.6    Werb, Z.7
  • 133
    • 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 JP, Wright JH, Matrisian LM. 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. 1995;6:1287-1303.
    • (1995) Mol Biol Cell , vol.6 , pp. 1287-1303
    • Witty, J.P.1    Wright, J.H.2    Matrisian, L.M.3
  • 134
    • 0031426654 scopus 로고    scopus 로고
    • Matrix metalloproteinase stromelysin-1 triggers a cascade of molecular alterations that leads to stable epithelial-to-mesenchymal conversion and a premalignant phenotype in mammary epithelial cells
    • Lochter A, Galosy S, Muschler J, Freedman N, Werb Z, Bissell MJ. Matrix metalloproteinase stromelysin-1 triggers a cascade of molecular alterations that leads to stable epithelial-to-mesenchymal conversion and a premalignant phenotype in mammary epithelial cells. J Cell Biol. 1997;139:1861-1872.
    • (1997) J Cell Biol , vol.139 , pp. 1861-1872
    • Lochter, A.1    Galosy, S.2    Muschler, J.3    Freedman, N.4    Werb, Z.5    Bissell, M.J.6
  • 135
    • 0031877357 scopus 로고    scopus 로고
    • Expression of autoactivated stromelysin-1 in mammary glands of transgenic mice leads to a reactive stroma during early development
    • Thomasset N, Lochter A, Sympson CJ, Lund LR, Williams DR, Behrendtsen O, Werb Z, Bissell MJ. Expression of autoactivated stromelysin-1 in mammary glands of transgenic mice leads to a reactive stroma during early development. Am J Pathol. 1998;153:457-467.
    • (1998) Am J Pathol , vol.153 , pp. 457-467
    • Thomasset, N.1    Lochter, A.2    Sympson, C.J.3    Lund, L.R.4    Williams, D.R.5    Behrendtsen, O.6    Werb, Z.7    Bissell, M.J.8
  • 136
    • 0030953577 scopus 로고    scopus 로고
    • Gelatinase A is a glomerular mesangial cell growth and differentiation factor
    • Turck J, Pollock AS, Lovett DH. Gelatinase A is a glomerular mesangial cell growth and differentiation factor. Kidney Int. 1997;51:1397-1400.
    • (1997) Kidney Int , vol.51 , pp. 1397-1400
    • Turck, J.1    Pollock, A.S.2    Lovett, D.H.3
  • 137
    • 0030946445 scopus 로고    scopus 로고
    • Release of gelatinase A during platelet activation mediates aggregation
    • Sawicki G, Salas E, Murat J, Miszta-Lane H, Radomski MW. Release of gelatinase A during platelet activation mediates aggregation. Nature. 1997;386:616-619.
    • (1997) Nature , vol.386 , pp. 616-619
    • Sawicki, G.1    Salas, E.2    Murat, J.3    Miszta-Lane, H.4    Radomski, M.W.5
  • 138
    • 0032492713 scopus 로고    scopus 로고
    • Generation of an angiostatin-like fragment from plasminogen by stromelysin-1 (MMP-3)
    • Lijnen HR, Ugwu F, Bini A, Collen D. Generation of an angiostatin-like fragment from plasminogen by stromelysin-1 (MMP-3). Biochemistry. 1998;37:4699-4702.
    • (1998) Biochemistry , vol.37 , pp. 4699-4702
    • Lijnen, H.R.1    Ugwu, F.2    Bini, A.3    Collen, D.4
  • 139
    • 15444352707 scopus 로고    scopus 로고
    • Angiostatin-converting enzyme activities of human matrilysin (MMP-7) and gelatinase B/type IV collagenase (MMP-9)
    • Patterson BC, Sang QA. Angiostatin-converting enzyme activities of human matrilysin (MMP-7) and gelatinase B/type IV collagenase (MMP-9). J Biol Chem. 1997;272:28823-28825.
    • (1997) J Biol Chem , vol.272 , pp. 28823-28825
    • Patterson, B.C.1    Sang, Q.A.2
  • 140
    • 0030749569 scopus 로고    scopus 로고
    • A dominant negative mutant of jun blocking 12-O-tetradecanoylphorbol-13-acetate-induced invasion in mouse keratinocytes
    • Dong Z, Crawford HC, Lavrovsky V, Taub D, Watts R, Matrisian LM, Colburn NH. A dominant negative mutant of jun blocking 12-O-tetradecanoylphorbol-13-acetate-induced invasion in mouse keratinocytes. Mol Carcinog. 1997;19:204-212.
    • (1997) Mol Carcinog , vol.19 , pp. 204-212
    • Dong, Z.1    Crawford, H.C.2    Lavrovsky, V.3    Taub, D.4    Watts, R.5    Matrisian, L.M.6    Colburn, N.H.7
  • 142
    • 1842338681 scopus 로고    scopus 로고
    • Limited cleavage of extracellular matrix protein BM-40 by matrix metalloproteinases increases its affinity for collagens
    • Sasaki T, Gohring W, Mann K, Maurer P, Hohenester E, Knäuper V, Murphy G, Timpl R. Limited cleavage of extracellular matrix protein BM-40 by matrix metalloproteinases increases its affinity for collagens. J Biol Chem. 1997;272:9237-9243.
    • (1997) J Biol Chem , vol.272 , pp. 9237-9243
    • Sasaki, T.1    Gohring, W.2    Mann, K.3    Maurer, P.4    Hohenester, E.5    Knäuper, V.6    Murphy, G.7    Timpl, R.8
  • 143
    • 0032524041 scopus 로고    scopus 로고
    • Transformation of epithelial Madin-Darby canine kidney cells with p60(v-src) induces expression of membrane-type I matrix metalloproteinase and invasiveness
    • Kadono Y, Okada Y, Namiki M, Seiki M, Sato H. Transformation of epithelial Madin-Darby canine kidney cells with p60(v-src) induces expression of membrane-type I matrix metalloproteinase and invasiveness. Cancer Res. 1998;58:2240-2244.
    • (1998) Cancer Res , vol.58 , pp. 2240-2244
    • Kadono, Y.1    Okada, Y.2    Namiki, M.3    Seiki, M.4    Sato, H.5
  • 144
    • 0029876376 scopus 로고    scopus 로고
    • The degradation of human endothelial cell-derived perlecan and release of bound basic fibroblast growth factor by stromelysin, collagenase, plasmin, and heparanases
    • Whitelock JM, Murdoch AD, Iozzo RV, Underwood PA. The degradation of human endothelial cell-derived perlecan and release of bound basic fibroblast growth factor by stromelysin, collagenase, plasmin, and heparanases. J Biol Chem. 1996;271:10079-10086.
    • (1996) J Biol Chem , vol.271 , pp. 10079-10086
    • Whitelock, J.M.1    Murdoch, A.D.2    Iozzo, R.V.3    Underwood, P.A.4
  • 145
    • 0028020082 scopus 로고
    • Matrix metalloproteinases degrade insulin-like growth factor-binding protein-3 in dermal fibroblast cultures
    • Fowlkes JL, Enghild JJ, Suzuki K, Nagase H. Matrix metalloproteinases degrade insulin-like growth factor-binding protein-3 in dermal fibroblast cultures. J Biol Chem. 1994;269:25742-25746.
    • (1994) J Biol Chem , vol.269 , pp. 25742-25746
    • Fowlkes, J.L.1    Enghild, J.J.2    Suzuki, K.3    Nagase, H.4
  • 146
    • 0029121178 scopus 로고
    • Characterization of insulin-like growth factor-binding protein 5-degrading proteases produced throughout murine osteoblast differentiation
    • Thrailkill KM, Quarles LD, Nagase H, Suzuki K, Serra DM, Fowlkes JL. Characterization of insulin-like growth factor-binding protein 5-degrading proteases produced throughout murine osteoblast differentiation. Endocrinology. 1995;136:3527-3533.
    • (1995) Endocrinology , vol.136 , pp. 3527-3533
    • Thrailkill, K.M.1    Quarles, L.D.2    Nagase, H.3    Suzuki, K.4    Serra, D.M.5    Fowlkes, J.L.6
  • 148
    • 0037183997 scopus 로고    scopus 로고
    • Matrix metalloproteinases cleave connective tissue growth factor and reactivate angiogenic activity of vascular endothelial growth factor 165
    • Hashimoto G, Inoki I, Fujii Y, Aoki T, Ikeda E, Okada Y. Matrix metalloproteinases cleave connective tissue growth factor and reactivate angiogenic activity of vascular endothelial growth factor 165. J Biol Chem. 2002;277:36288-36295.
    • (2002) J Biol Chem , vol.277 , pp. 36288-36295
    • Hashimoto, G.1    Inoki, I.2    Fujii, Y.3    Aoki, T.4    Ikeda, E.5    Okada, Y.6
  • 149
    • 0032194115 scopus 로고    scopus 로고
    • Generation of biologically active IL-1 β by matrix metalloproteinases: A novel caspase-1-independent pathway of IL-1 β processing
    • Schonbeck U, Mach F, Libby P. Generation of biologically active IL-1 β by matrix metalloproteinases: a novel caspase-1-independent pathway of IL-1 β processing. J Immunol. 1998;161:3340-3346.
    • (1998) J Immunol , vol.161 , pp. 3340-3346
    • Schonbeck, U.1    Mach, F.2    Libby, P.3
  • 150
    • 0037043820 scopus 로고    scopus 로고
    • Matrix metalloproteinase 9 (MMP-9/gelatinase B) proteolytically cleaves ICAM-1 and participates in tumor cell resistance to natural killer cell-mediated cytotoxicity
    • Fiore E, Fusco C, Romero P, Stamenkovic I. Matrix metalloproteinase 9 (MMP-9/gelatinase B) proteolytically cleaves ICAM-1 and participates in tumor cell resistance to natural killer cell-mediated cytotoxicity. Oncogene. 2002;21:5213-5223.
    • (2002) Oncogene , vol.21 , pp. 5213-5223
    • Fiore, E.1    Fusco, C.2    Romero, P.3    Stamenkovic, I.4
  • 154
    • 0030958072 scopus 로고    scopus 로고
    • Degradation of decorin by matrix metalloproteinases: Identification of the cleavage sites, kinetic analyses and transforming growth factor-beta1 release
    • Imai K, Hiramatsu A, Fukushima D, Pierschbacher MD, Okada Y. Degradation of decorin by matrix metalloproteinases: identification of the cleavage sites, kinetic analyses and transforming growth factor-beta1 release. Biochem J. 1997;322:809-814.
    • (1997) Biochem J , vol.322 , pp. 809-814
    • Imai, K.1    Hiramatsu, A.2    Fukushima, D.3    Pierschbacher, M.D.4    Okada, Y.5
  • 156
    • 0035947675 scopus 로고    scopus 로고
    • Matrix-dependent proteolysis of surface transglutaminase by membrane-type metalloproteinase regulates cancer cell adhesion and locomotion
    • Belkin AM, Akimov SS, Zaritskaya LS, Ratnikov BI, Deryugina EI, Strongin AY. Matrix-dependent proteolysis of surface transglutaminase by membrane-type metalloproteinase regulates cancer cell adhesion and locomotion. J Biol Chem. 2001;276:18415-18422.
    • (2001) J Biol Chem , vol.276 , pp. 18415-18422
    • Belkin, A.M.1    Akimov, S.S.2    Zaritskaya, L.S.3    Ratnikov, B.I.4    Deryugina, E.I.5    Strongin, A.Y.6
  • 157
    • 0033576645 scopus 로고    scopus 로고
    • The metalloproteinase matrilysin proteolytically generates active soluble Fas ligand and potentiates epithelial cell apoptosis
    • Powell WC, Fingleton B, Wilson CL, Boothby M, Matrisian LM. The metalloproteinase matrilysin proteolytically generates active soluble Fas ligand and potentiates epithelial cell apoptosis. Curr Biol. 1999;9:1441-1447.
    • (1999) Curr Biol , vol.9 , pp. 1441-1447
    • Powell, W.C.1    Fingleton, B.2    Wilson, C.L.3    Boothby, M.4    Matrisian, L.M.5
  • 158
    • 0035137707 scopus 로고    scopus 로고
    • A novel role of metalloproteinase in cancer-mediated immunosuppression
    • Sheu BC, Hsu SM, Ho HN, Lien HC, Huang SC, Lin RH. A novel role of metalloproteinase in cancer-mediated immunosuppression. Cancer Res. 2001;61:237-242.
    • (2001) Cancer Res , vol.61 , pp. 237-242
    • Sheu, B.C.1    Hsu, S.M.2    Ho, H.N.3    Lien, H.C.4    Huang, S.C.5    Lin, R.H.6


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