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Volumn 169, Issue 4, 2006, Pages 1390-1401

Matrix metalloproteinase 3 is present in the cell nucleus and is involved in apoptosis

Author keywords

[No Author keywords available]

Indexed keywords

GREEN FLUORESCENT PROTEIN; ILOMASTAT; STROMELYSIN;

EID: 33847062172     PISSN: 00029440     EISSN: None     Source Type: Journal    
DOI: 10.2353/ajpath.2006.060005     Document Type: Article
Times cited : (149)

References (41)
  • 1
    • 0031656460 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Structures, evolution, and diversification
    • Massova I, Kotra LP, Fridman R, Mobashery S: Matrix metalloproteinases: structures, evolution, and diversification. FASEB J 1998, 12:1075-1095
    • (1998) FASEB J , vol.12 , pp. 1075-1095
    • Massova, I.1    Kotra, L.P.2    Fridman, R.3    Mobashery, S.4
  • 2
    • 0033618337 scopus 로고    scopus 로고
    • Matrix metalloproteinases
    • Nagase H, Woessner Jr JF: 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
  • 3
    • 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
  • 4
    • 0035500490 scopus 로고    scopus 로고
    • The many faces of metalloproteases: Cell growth, invasion, angiogenesis and metastasis
    • Chang C, Werb Z: The many faces of metalloproteases: cell growth, invasion, angiogenesis and metastasis. Trends Cell Biol 2001, 11:S37-S43
    • (2001) Trends Cell Biol , vol.11
    • Chang, C.1    Werb, Z.2
  • 5
    • 0023024460 scopus 로고
    • A metalloproteinase from human rheumatoid synovial fibroblasts that digests connective tissue matrix components. Purification and characterization
    • Okada Y, Nagase H, Harris ED: A metalloproteinase from human rheumatoid synovial fibroblasts that digests connective tissue matrix components. Purification and characterization. J Biol Chem 1986, 261:14245-14255
    • (1986) J Biol Chem , vol.261 , pp. 14245-14255
    • Okada, Y.1    Nagase, H.2    Harris, E.D.3
  • 6
    • 1642390201 scopus 로고    scopus 로고
    • Matrix metalloproteinases: A review of their structure and role in acute coronary syndrome
    • Jones CB, Sane DC, Herrington DM: Matrix metalloproteinases: a review of their structure and role in acute coronary syndrome. Cardiovasc Res 2003, 59:812-823
    • (2003) Cardiovasc Res , vol.59 , pp. 812-823
    • Jones, C.B.1    Sane, D.C.2    Herrington, D.M.3
  • 8
    • 0035892755 scopus 로고    scopus 로고
    • Regulation of hepatic fibrosis and extracellular matrix genes by the th response: New insight into the role of tissue inhibitors of matrix metalloproteinases
    • Vaillant B, Chiaramonte MG, Cheever AW, Soloway PD, Wynn TA: Regulation of hepatic fibrosis and extracellular matrix genes by the th response: new insight into the role of tissue inhibitors of matrix metalloproteinases. J Immunol 2001, 167:7017-7026
    • (2001) J Immunol , vol.167 , pp. 7017-7026
    • Vaillant, B.1    Chiaramonte, M.G.2    Cheever, A.W.3    Soloway, P.D.4    Wynn, T.A.5
  • 9
    • 0029644945 scopus 로고
    • A helping hand for collagenases: The haemopexin-like domain
    • Bode W: A helping hand for collagenases: the haemopexin-like domain. Structure 1995, 3:527-530
    • (1995) Structure , vol.3 , pp. 527-530
    • Bode, W.1
  • 11
    • 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 USA 1990, 87:5578-5582
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 5578-5582
    • Van Wart, H.E.1    Birkedal-Hansen, H.2
  • 12
    • 0037067669 scopus 로고    scopus 로고
    • Alternative splicing and promoter usage generates an intracellular stromelysin 3 isoform directly translated as an active matrix metalloproteinase
    • Luo D, Mari B, Stoll I, Anglard P: Alternative splicing and promoter usage generates an intracellular stromelysin 3 isoform directly translated as an active matrix metalloproteinase. J Biol Chem 2002, 277:25527-25536
    • (2002) J Biol Chem , vol.277 , pp. 25527-25536
    • Luo, D.1    Mari, B.2    Stoll, I.3    Anglard, P.4
  • 14
    • 3042745695 scopus 로고    scopus 로고
    • Matrix metalloproteinase-2 (MMP-2) is present in the nucleus of cardiac myocytes and is capable of cleaving poly (ADP-ribose) polymerase (PARP) in vitro
    • Kwan JA, Schulze CJ, Wang W, Leon H, Sariahmetoglu M, Sung M, Sawicka J, Sims DE, Sawicki G, Schulz R: Matrix metalloproteinase-2 (MMP-2) is present in the nucleus of cardiac myocytes and is capable of cleaving poly (ADP-ribose) polymerase (PARP) in vitro. FASEB J 2004, 18:690-692
    • (2004) FASEB J , vol.18 , pp. 690-692
    • Kwan, J.A.1    Schulze, C.J.2    Wang, W.3    Leon, H.4    Sariahmetoglu, M.5    Sung, M.6    Sawicka, J.7    Sims, D.E.8    Sawicki, G.9    Schulz, R.10
  • 16
    • 0033994361 scopus 로고    scopus 로고
    • Extrinsic regulators of epithelial tumor progression: Metalloproteinases
    • Bergers G, Coussens LM: Extrinsic regulators of epithelial tumor progression: metalloproteinases. Curr Opin Genet Dev 2000, 10:120-127
    • (2000) Curr Opin Genet Dev , vol.10 , pp. 120-127
    • Bergers, G.1    Coussens, L.M.2
  • 17
    • 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, 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.2    Nagase, H.3
  • 18
    • 0037050023 scopus 로고    scopus 로고
    • Involvement of matrix metalloproteinase type-3 in hepatocyte growth factor-induced invasion of human hepatocellular carcinoma cells
    • Monvoisin A, Bisson C, Si-Tayeb K, Balabaud C, Desmouliere A, Rosenbaum J: Involvement of matrix metalloproteinase type-3 in hepatocyte growth factor-induced invasion of human hepatocellular carcinoma cells. Int J Cancer 2002, 97:157-162
    • (2002) Int J Cancer , vol.97 , pp. 157-162
    • Monvoisin, A.1    Bisson, C.2    Si-Tayeb, K.3    Balabaud, C.4    Desmouliere, A.5    Rosenbaum, J.6
  • 19
    • 0034652217 scopus 로고    scopus 로고
    • Dopamine tone regulates D1 receptor trafficking and delivery in striatal neurons in dopamine transporter-deficient mice
    • Dumartin B, Jaber M, Gonon F, Caron MG, Giros B, Bloch B: Dopamine tone regulates D1 receptor trafficking and delivery in striatal neurons in dopamine transporter-deficient mice. Proc Natl Acad Sci USA 2000, 97:1879-1884
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 1879-1884
    • Dumartin, B.1    Jaber, M.2    Gonon, F.3    Caron, M.G.4    Giros, B.5    Bloch, B.6
  • 20
    • 0027166733 scopus 로고
    • Mitogenic effect of transforming growth factor-beta 1 on human Ito cells in culture: Evidence for mediation by endogenous platelet-derived growth factor
    • Win KM, Charlotte F, Mallat A, Cherqui D, Martin N, Mavier P, Preaux AM, Dhumeaux D, Rosenbaum J: Mitogenic effect of transforming growth factor-beta 1 on human Ito cells in culture: evidence for mediation by endogenous platelet-derived growth factor. Hepatology 1993, 18:137-145
    • (1993) Hepatology , vol.18 , pp. 137-145
    • Win, K.M.1    Charlotte, F.2    Mallat, A.3    Cherqui, D.4    Martin, N.5    Mavier, P.6    Preaux, A.M.7    Dhumeaux, D.8    Rosenbaum, J.9
  • 22
    • 0024380087 scopus 로고
    • Rapid detection of octamer binding proteins with 'mini-extracts', prepared from a small number of cells
    • Schreiber E, Matthias P, Muller MM, Schaffner W: Rapid detection of octamer binding proteins with 'mini-extracts', prepared from a small number of cells. Nucleic Acids Res 1989, 17:6419
    • (1989) Nucleic Acids Res , vol.17 , pp. 6419
    • Schreiber, E.1    Matthias, P.2    Muller, M.M.3    Schaffner, W.4
  • 23
    • 0242666128 scopus 로고    scopus 로고
    • Identification of nuclear export signals in antizyme-1
    • Murai N, Murakami Y, Matsufuji S: Identification of nuclear export signals in antizyme-1. J Biol Chem 2003, 278:44791-44798
    • (2003) J Biol Chem , vol.278 , pp. 44791-44798
    • Murai, N.1    Murakami, Y.2    Matsufuji, S.3
  • 24
    • 0021716406 scopus 로고
    • A short amino acid sequence able to specify nuclear location
    • Kalderon D, Roberts BL, Richardson WD, Smith AE: A short amino acid sequence able to specify nuclear location. Cell 1984, 39:499-509
    • (1984) Cell , vol.39 , pp. 499-509
    • Kalderon, D.1    Roberts, B.L.2    Richardson, W.D.3    Smith, A.E.4
  • 25
    • 0034608799 scopus 로고    scopus 로고
    • A distinct nuclear localization signal in the N terminus of Smad 3 determines its ligand-induced nuclear translocation
    • Xiao Z, Liu X, Henis YI, Lodish HF: A distinct nuclear localization signal in the N terminus of Smad 3 determines its ligand-induced nuclear translocation. Proc Natl Acad Sci USA 2000, 97:7853-7858
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 7853-7858
    • Xiao, Z.1    Liu, X.2    Henis, Y.I.3    Lodish, H.F.4
  • 26
    • 0034818299 scopus 로고    scopus 로고
    • Critical role of glutamic acid 202 in the enzymatic activity of stromelysin-1 (MMP-3)
    • Arza B, De Maeyer M, Felez J, Collen D, Lijnen HR: Critical role of glutamic acid 202 in the enzymatic activity of stromelysin-1 (MMP-3). Eur J Biochem 2001, 268:826-831
    • (2001) Eur J Biochem , vol.268 , pp. 826-831
    • Arza, B.1    De Maeyer, M.2    Felez, J.3    Collen, D.4    Lijnen, H.R.5
  • 28
    • 0025831535 scopus 로고
    • Purification of recombinant human prostromelysin. Studies on heat activation to give high-Mr and low-Mr active forms, and a comparison of recombinant with natural stromelysin activities
    • Koklitis PA, Murphy G, Sutton C, Angal S: Purification of recombinant human prostromelysin. Studies on heat activation to give high-Mr and low-Mr active forms, and a comparison of recombinant with natural stromelysin activities. Biochem J 1991, 276:217-221
    • (1991) Biochem J , vol.276 , pp. 217-221
    • Koklitis, P.A.1    Murphy, G.2    Sutton, C.3    Angal, S.4
  • 29
    • 0031467314 scopus 로고    scopus 로고
    • Matrix metalloproteinase-3 releases active heparin-binding EGF-like growth factor by cleavage at a specific juxtamembrane site
    • Suzuki M, Raab G, Moses MA, Fernandez CA, Klagsbrun M: Matrix metalloproteinase-3 releases active heparin-binding EGF-like growth factor by cleavage at a specific juxtamembrane site. J Biol Chem 1997, 272:31730-31737
    • (1997) J Biol Chem , vol.272 , pp. 31730-31737
    • Suzuki, M.1    Raab, G.2    Moses, M.A.3    Fernandez, C.A.4    Klagsbrun, M.5
  • 30
    • 0031868017 scopus 로고    scopus 로고
    • Expression of matrix metalloproteinases by human plasma cells and B lymphocytes
    • Di Girolamo N, Tedla N, Lloyd A, Wakefield D: Expression of matrix metalloproteinases by human plasma cells and B lymphocytes. Eur J Immunol 1998, 28:1773-1784
    • (1998) Eur J Immunol , vol.28 , pp. 1773-1784
    • Di Girolamo, N.1    Tedla, N.2    Lloyd, A.3    Wakefield, D.4
  • 31
    • 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
  • 32
    • 0022353379 scopus 로고
    • Stromelysin, a connective tissue-degrading metalloendopeptidase secreted by stimulated rabbit synovial fibroblasts in parallel with collagenase. Biosynthesis, isolation, characterization, and substrates
    • Chin JR, Murphy G, Werb Z: Stromelysin, a connective tissue-degrading metalloendopeptidase secreted by stimulated rabbit synovial fibroblasts in parallel with collagenase. Biosynthesis, isolation, characterization, and substrates. J Biol Chem 1985, 260:12367-12376
    • (1985) J Biol Chem , vol.260 , pp. 12367-12376
    • Chin, J.R.1    Murphy, G.2    Werb, Z.3
  • 33
    • 0031707505 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: The soluble phase
    • Mattaj IW, Englmeier L: Nucleocytoplasmic transport: the soluble phase. Annu Rev Biochem 1998, 67:265-306
    • (1998) Annu Rev Biochem , vol.67 , pp. 265-306
    • Mattaj, I.W.1    Englmeier, L.2
  • 34
    • 0027105007 scopus 로고
    • A knowledge base for predicting protein localization sites in eukaryotic cells
    • Nakai K, Kanehisa M: A knowledge base for predicting protein localization sites in eukaryotic cells. Genomics 1992, 14:897-911
    • (1992) Genomics , vol.14 , pp. 897-911
    • Nakai, K.1    Kanehisa, M.2
  • 35
  • 36
    • 0029006135 scopus 로고
    • Human stromelysins 1 and 2
    • Nagase H: Human stromelysins 1 and 2. Methods Enzymol 1995, 248:449-470
    • (1995) Methods Enzymol , vol.248 , pp. 449-470
    • Nagase, H.1
  • 37
    • 0023055373 scopus 로고
    • Fluorescence microphotolysis to measure nucleocytoplasmic transport and intracellular mobility
    • Peters R: Fluorescence microphotolysis to measure nucleocytoplasmic transport and intracellular mobility. Biochim Biophys Acta 1986, 864:305-359
    • (1986) Biochim Biophys Acta , vol.864 , pp. 305-359
    • Peters, R.1
  • 38
    • 15744404638 scopus 로고    scopus 로고
    • Furin directly cleaves proMMP-2 in the trans-Golgi network resulting in a nonfunctioning proteinase
    • Cao J, Rehemtulla A, Pavlaki M, Kozarekar P, Chiarelli C: Furin directly cleaves proMMP-2 in the trans-Golgi network resulting in a nonfunctioning proteinase. J Biol Chem 2005, 280:10974-10980
    • (2005) J Biol Chem , vol.280 , pp. 10974-10980
    • Cao, J.1    Rehemtulla, A.2    Pavlaki, M.3    Kozarekar, P.4    Chiarelli, C.5
  • 39
    • 17844383733 scopus 로고    scopus 로고
    • Matrix metalloproteinase-1 associates with intracellular organelles and confers resistance to lamin A/C degradation during apoptosis
    • Limb GA, Matter K, Murphy G, Cambrey AD, Bishop PN, Morris GE, Khaw PT: Matrix metalloproteinase-1 associates with intracellular organelles and confers resistance to lamin A/C degradation during apoptosis. Am J Pathol 2005, 166:1555-1563
    • (2005) Am J Pathol , vol.166 , pp. 1555-1563
    • Limb, G.A.1    Matter, K.2    Murphy, G.3    Cambrey, A.D.4    Bishop, P.N.5    Morris, G.E.6    Khaw, P.T.7


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