메뉴 건너뛰기




Volumn 350, Issue 4, 2005, Pages 682-698

Pancreatic trypsin activates human promatrix metalloproteinase-2

Author keywords

GelatinaseA; MT MMP; Promatrix metalloproteinase 2; TIMP; Trypsin

Indexed keywords

CALCIUM ION; ENZYME INHIBITOR; ENZYME PRECURSOR; GELATINASE A; LYSINE; MATRIX METALLOPROTEINASE 14; PANCREAS ENZYME; PHENYLALANINE; POLIDOCANOL; TRYPSIN; TRYPTOPHAN; TYROSINE;

EID: 20544478569     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.05.018     Document Type: Article
Times cited : (23)

References (83)
  • 1
    • 0027601224 scopus 로고
    • Role of matrix metalloproteinases in human periodontal diseases
    • H. Birkedal-Hansen Role of matrix metalloproteinases in human periodontal diseases J. Periodontol. 64 1993 474 484
    • (1993) J. Periodontol. , vol.64 , pp. 474-484
    • Birkedal-Hansen, H.1
  • 3
    • 0030957218 scopus 로고    scopus 로고
    • Activation mechanisms of matrix metalloproteinases
    • H. Nagase Activation mechanisms of matrix metalloproteinases Biol. Chem. 378 1997 151 160
    • (1997) Biol. Chem. , vol.378 , pp. 151-160
    • Nagase, H.1
  • 4
    • 0032722873 scopus 로고    scopus 로고
    • Catalytic activities and substrate specificity of the human membrane type 4 matrix metalloproteinase catalytic domain
    • Y. Wang, A.R. Johnson, Q.Z. Ye, and R.D. Dyer Catalytic activities and substrate specificity of the human membrane type 4 matrix metalloproteinase catalytic domain J. Biol. Chem. 274 1999 33043 33049
    • (1999) J. Biol. Chem. , vol.274 , pp. 33043-33049
    • Wang, Y.1    Johnson, A.R.2    Ye, Q.Z.3    Dyer, R.D.4
  • 5
    • 0034652623 scopus 로고    scopus 로고
    • Human MT6-matrix metalloproteinase: Identification, progelatinase a activation, and expression in brain tumors
    • G. Velasco, S. Cal, A. Merlos-Suarez, A.A. Ferrando, S. Alvarez, and A. Nakano Human MT6-matrix metalloproteinase: identification, progelatinase A activation, and expression in brain tumors Cancer Res. 60 2000 877 882
    • (2000) Cancer Res. , vol.60 , pp. 877-882
    • Velasco, G.1    Cal, S.2    Merlos-Suarez, A.3    Ferrando, A.A.4    Alvarez, S.5    Nakano, A.6
  • 7
    • 1542495411 scopus 로고    scopus 로고
    • Structural basis of matrix metalloproteinase function
    • W. Bode Structural basis of matrix metalloproteinase function Biochem. Soc. Symp. 2003 1 14
    • (2003) Biochem. Soc. Symp. , pp. 1-14
    • Bode, W.1
  • 8
    • 0037810391 scopus 로고    scopus 로고
    • Structural basis of the matrix metalloproteinases and their physiological inhibitors, the tissue inhibitors of metalloproteinases
    • W. Bode, and K. Maskos Structural basis of the matrix metalloproteinases and their physiological inhibitors, the tissue inhibitors of metalloproteinases Biol. Chem. 384 2003 863 872
    • (2003) Biol. Chem. , vol.384 , pp. 863-872
    • Bode, W.1    Maskos, K.2
  • 9
    • 0037693895 scopus 로고    scopus 로고
    • Matrix metalloproteinases and tissue inhibitors of metalloproteinases: Structure, function, and biochemistry
    • R. Visse, and H. Nagase Matrix metalloproteinases and tissue inhibitors of metalloproteinases: structure, function, and biochemistry Circ. Res. 92 2003 827 839
    • (2003) Circ. Res. , vol.92 , pp. 827-839
    • Visse, R.1    Nagase, H.2
  • 11
    • 0037188508 scopus 로고    scopus 로고
    • Structural insight into the complex formation of latent matrix metalloproteinase 2 with tissue inhibitor of metalloproteinase 2
    • E. Morgunova, A. Tuuttila, U. Bergmann, and K. Tryggvason Structural insight into the complex formation of latent matrix metalloproteinase 2 with tissue inhibitor of metalloproteinase 2 Proc. Natl Acad. Sci. USA 99 2002 7414 7419
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 7414-7419
    • Morgunova, E.1    Tuuttila, A.2    Bergmann, U.3    Tryggvason, K.4
  • 12
    • 0342502272 scopus 로고    scopus 로고
    • The C-terminal (haemopexin-like) domain structure of human gelatinase a (MMP2): Structural implications for its function
    • U. Gohlke, F.X. Gomis-Ruth, T. Crabbe, G. Murphy, A.J. Docherty, and W. Bode The C-terminal (haemopexin-like) domain structure of human gelatinase A (MMP2): structural implications for its function FEBS Letters 378 1996 126 130
    • (1996) FEBS Letters , vol.378 , pp. 126-130
    • Gohlke, U.1    Gomis-Ruth, F.X.2    Crabbe, T.3    Murphy, G.4    Docherty, A.J.5    Bode, W.6
  • 13
    • 0040051981 scopus 로고    scopus 로고
    • The helping hand of collagenase-3 (MMP-13): 2.7 Å crystal structure of its C-terminal haemopexin-like domain
    • F.X. Gomis-Ruth, U. Gohlke, M. Betz, V. Knauper, G. Murphy, C. Lopez-Otin, and W. Bode The helping hand of collagenase-3 (MMP-13): 2.7 Å crystal structure of its C-terminal haemopexin-like domain J. Mol. Biol. 264 1996 556 566
    • (1996) J. Mol. Biol. , vol.264 , pp. 556-566
    • Gomis-Ruth, F.X.1    Gohlke, U.2    Betz, M.3    Knauper, V.4    Murphy, G.5    Lopez-Otin, C.6    Bode, W.7
  • 14
    • 0034615550 scopus 로고    scopus 로고
    • Tissue inhibitors of metalloproteinases: Evolution, structure and function
    • K. Brew, D. Dinakarpandian, and H. Nagase Tissue inhibitors of metalloproteinases: evolution, structure and function Biochim. Biophys. Acta. 1477 2000 267 283
    • (2000) Biochim. Biophys. Acta. , vol.1477 , pp. 267-283
    • Brew, K.1    Dinakarpandian, D.2    Nagase, H.3
  • 15
    • 0036995757 scopus 로고    scopus 로고
    • Matrix metalloproteinases in tumor-host cell communication
    • C.C. Lynch, and L.M. Matrisian Matrix metalloproteinases in tumor-host cell communication Differentiation 70 2002 561 573
    • (2002) Differentiation , vol.70 , pp. 561-573
    • Lynch, C.C.1    Matrisian, L.M.2
  • 16
    • 0035479845 scopus 로고    scopus 로고
    • Matrix metalloproteinases: They're not just for matrix anymore!
    • L.J. McCawley, and L.M. Matrisian Matrix metalloproteinases: they're not just for matrix anymore! Curr. Opin. Cell Biol. 13 2001 534 540
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 534-540
    • McCawley, L.J.1    Matrisian, L.M.2
  • 17
    • 0025847582 scopus 로고
    • Matrix metalloproteinases and their inhibitors in connective tissue remodeling
    • J.F. Woessner Jr Matrix metalloproteinases and their inhibitors in connective tissue remodeling FASEB J. 5 1991 2145 2154
    • (1991) FASEB J. , vol.5 , pp. 2145-2154
    • Woessner, J.F.1    Jr2
  • 19
    • 0028792509 scopus 로고
    • Matrix metalloproteinases and cardiovascular disease
    • C.M. Dollery, J.R. McEwan, and A.M. Henney Matrix metalloproteinases and cardiovascular disease Circ. Res. 77 1995 863 868
    • (1995) Circ. Res. , vol.77 , pp. 863-868
    • Dollery, C.M.1    McEwan, J.R.2    Henney, A.M.3
  • 20
    • 0032403129 scopus 로고    scopus 로고
    • The matrix metalloproteinase matrilysin influences early-stage mammary tumorigenesis
    • L.A. Rudolph-Owen, R. Chan, W.J. Muller, and L.M. Matrisian The matrix metalloproteinase matrilysin influences early-stage mammary tumorigenesis Cancer Res. 58 1998 5500 5506
    • (1998) Cancer Res. , vol.58 , pp. 5500-5506
    • Rudolph-Owen, L.A.1    Chan, R.2    Muller, W.J.3    Matrisian, L.M.4
  • 21
    • 9444232274 scopus 로고    scopus 로고
    • Matrix metalloproteinases (MMPs) in oral diseases
    • T. Sorsa, L. Tjaderhane, and T. Salo Matrix metalloproteinases (MMPs) in oral diseases Oral Dis. 10 2004 311 318
    • (2004) Oral Dis. , vol.10 , pp. 311-318
    • Sorsa, T.1    Tjaderhane, L.2    Salo, T.3
  • 22
    • 2942542978 scopus 로고    scopus 로고
    • Cardiac rupture complicating myocardial infarction
    • X.H. Wehrens, and P.A. Doevendans Cardiac rupture complicating myocardial infarction Int. J. Cardiol. 95 2004 285 292
    • (2004) Int. J. Cardiol. , vol.95 , pp. 285-292
    • Wehrens, X.H.1    Doevendans, P.A.2
  • 23
    • 0042090224 scopus 로고    scopus 로고
    • Adhesion molecules and matrix metalloproteinases in Multiple Sclerosis: Effects induced by Interferon-beta
    • C. Avolio, F. Giuliani, G.M. Liuzzi, M. Ruggieri, D. Paolicelli, and P. Riccio Adhesion molecules and matrix metalloproteinases in Multiple Sclerosis: effects induced by Interferon-beta Brain Res. Bull. 61 2003 357 364
    • (2003) Brain Res. Bull. , vol.61 , pp. 357-364
    • Avolio, C.1    Giuliani, F.2    Liuzzi, G.M.3    Ruggieri, M.4    Paolicelli, D.5    Riccio, P.6
  • 24
    • 0029594498 scopus 로고
    • Contributions of tumor and stromal matrix metalloproteinases to tumor progression, invasion and metastasis
    • J.R. MacDougall, and L.M. Matrisian Contributions of tumor and stromal matrix metalloproteinases to tumor progression, invasion and metastasis Cancer Metastasis Rev. 14 1995 351 362
    • (1995) Cancer Metastasis Rev. , vol.14 , pp. 351-362
    • MacDougall, J.R.1    Matrisian, L.M.2
  • 25
    • 0040439972 scopus 로고    scopus 로고
    • The matrix metalloproteinase-9 regulates the insulin-like growth factor-triggered autocrine response in DU-145 carcinoma cells
    • S. Manes, M. Llorente, R.A. Lacalle, C. Gomez-Mouton, L. Kremer, E. Mira, and A.C. Martinez The matrix metalloproteinase-9 regulates the insulin-like growth factor-triggered autocrine response in DU-145 carcinoma cells J. Biol. Chem. 274 1999 6935 6945
    • (1999) J. Biol. Chem. , vol.274 , pp. 6935-6945
    • Manes, S.1    Llorente, M.2    Lacalle, R.A.3    Gomez-Mouton, C.4    Kremer, L.5    Mira, E.6    Martinez, A.C.7
  • 26
    • 0037052641 scopus 로고    scopus 로고
    • Matrix metalloproteinases in cancer: Prognostic markers and therapeutic targets
    • P. Vihinen, and V.M. Kahari Matrix metalloproteinases in cancer: prognostic markers and therapeutic targets Int. J. Cancer 99 2002 157 166
    • (2002) Int. J. Cancer , vol.99 , pp. 157-166
    • Vihinen, P.1    Kahari, V.M.2
  • 27
    • 0025611427 scopus 로고
    • Type IV collagenases in tumor invasion and metastasis
    • W.G. Stetler-Stevenson Type IV collagenases in tumor invasion and metastasis Cancer Metastasis Rev. 9 1990 289 303
    • (1990) Cancer Metastasis Rev. , vol.9 , pp. 289-303
    • Stetler-Stevenson, W.G.1
  • 28
    • 0028095634 scopus 로고
    • Metastasis of human colon tumor cells in vivo: Correlation with the overexpression of plasminogen activators and 72 kDa gelatinase
    • V. Shah, S. Kumar, and K.A. Zirvi Metastasis of human colon tumor cells in vivo: correlation with the overexpression of plasminogen activators and 72 kDa gelatinase In Vivo 8 1994 321 326
    • (1994) In Vivo , vol.8 , pp. 321-326
    • Shah, V.1    Kumar, S.2    Zirvi, K.A.3
  • 29
    • 0028886482 scopus 로고
    • Expression of matrix proteinases during human intrahepatic bile duct development. a possible role in biliary cell migration
    • T. Terada, Y. Okada, and Y. Nakanuma Expression of matrix proteinases during human intrahepatic bile duct development. A possible role in biliary cell migration Am. J. Pathol. 147 1995 1207 1213
    • (1995) Am. J. Pathol. , vol.147 , pp. 1207-1213
    • Terada, T.1    Okada, Y.2    Nakanuma, Y.3
  • 30
    • 0025616093 scopus 로고
    • Matrix metalloproteinase 2 from human rheumatoid synovial fibroblasts. Purification and activation of the precursor and enzymic properties
    • Y. Okada, T. Morodomi, J.J. Enghild, K. Suzuki, A. Yasui, and I. Nakanishi Matrix metalloproteinase 2 from human rheumatoid synovial fibroblasts. Purification and activation of the precursor and enzymic properties Eur. J. Biochem. 194 1990 721 730
    • (1990) Eur. J. Biochem. , vol.194 , pp. 721-730
    • Okada, Y.1    Morodomi, T.2    Enghild, J.J.3    Suzuki, K.4    Yasui, A.5    Nakanishi, I.6
  • 31
    • 0028556638 scopus 로고
    • Reciprocated matrix metalloproteinase activation: A process performed by interstitial collagenase and progelatinase a
    • T. Crabbe, J.P. O'Connell, B.J. Smith, and A.J. Docherty Reciprocated matrix metalloproteinase activation: a process performed by interstitial collagenase and progelatinase A Biochemistry 33 1994 14419 14425
    • (1994) Biochemistry , vol.33 , pp. 14419-14425
    • Crabbe, T.1    O'Connell, J.P.2    Smith, B.J.3    Docherty, A.J.4
  • 32
    • 0028291374 scopus 로고
    • Human progelatinase a can be activated by matrilysin
    • T. Crabbe, B. Smith, J. O'Connell, and A. Docherty Human progelatinase A can be activated by matrilysin FEBS Letters 345 1994 14 16
    • (1994) FEBS Letters , vol.345 , pp. 14-16
    • Crabbe, T.1    Smith, B.2    O'Connell, J.3    Docherty, A.4
  • 33
    • 0028907318 scopus 로고
    • Mechanism of cell surface activation of 72-kDa type IV collagenase. Isolation of the activated form of the membrane metalloprotease
    • A.Y. Strongin, I. Collier, G. Bannikov, B.L. Marmer, G.A. Grant, and G.I. Goldberg Mechanism of cell surface activation of 72-kDa type IV collagenase. Isolation of the activated form of the membrane metalloprotease J. Biol. Chem. 270 1995 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
  • 34
    • 0033597728 scopus 로고    scopus 로고
    • Tissue inhibitor of matrix metalloproteinase-2 regulates matrix metalloproteinase-2 activation by modulation of membrane-type 1 matrix metalloproteinase activity in high and low invasive melanoma cell lines
    • P. Kurschat, P. Zigrino, R. Nischt, K. Breitkopf, P. Steurer, and C.E. Klein Tissue inhibitor of matrix metalloproteinase-2 regulates matrix metalloproteinase-2 activation by modulation of membrane-type 1 matrix metalloproteinase activity in high and low invasive melanoma cell lines J. Biol. Chem. 274 1999 21056 21062
    • (1999) J. Biol. Chem. , vol.274 , pp. 21056-21062
    • Kurschat, P.1    Zigrino, P.2    Nischt, R.3    Breitkopf, K.4    Steurer, P.5    Klein, C.E.6
  • 35
    • 0033003771 scopus 로고    scopus 로고
    • Membrane-type matrix metalloproteinases
    • M. Seiki Membrane-type matrix metalloproteinases APMIS 107 1999 137 143
    • (1999) APMIS , vol.107 , pp. 137-143
    • Seiki, M.1
  • 36
    • 0041568655 scopus 로고    scopus 로고
    • Proteinase-3 directly activates MMP-2 and degrades gelatin and Matrigel; Differential inhibition by (-)epigallocatechin-3-gallate
    • E. Pezzato, M. Dona, L. Sartor, I. Dell'Aica, R. Benelli, A. Albini, and S. Garbisa Proteinase-3 directly activates MMP-2 and degrades gelatin and Matrigel; differential inhibition by (-)epigallocatechin-3-gallate J. Leukoc. Biol. 74 2003 88 94
    • (2003) J. Leukoc. Biol. , vol.74 , pp. 88-94
    • Pezzato, E.1    Dona, M.2    Sartor, L.3    Dell'Aica, I.4    Benelli, R.5    Albini, A.6    Garbisa, S.7
  • 37
    • 0034737767 scopus 로고    scopus 로고
    • Activated protein C directly activates human endothelial gelatinase a
    • M. Nguyen, J. Arkell, and C.J. Jackson Activated protein C directly activates human endothelial gelatinase A J. Biol. Chem. 275 2000 9095 9098
    • (2000) J. Biol. Chem. , vol.275 , pp. 9095-9098
    • Nguyen, M.1    Arkell, J.2    Jackson, C.J.3
  • 38
    • 0034607041 scopus 로고    scopus 로고
    • Activation of human progelatinase A/promatrix metalloproteinase 2 by Escherichia coli-derived serine proteinase
    • M. Takeda, K. Imada, T. Sato, and A. Ito Activation of human progelatinase A/promatrix metalloproteinase 2 by Escherichia coli-derived serine proteinase Biochem. Biophys. Res. Commun. 268 2000 128 132
    • (2000) Biochem. Biophys. Res. Commun. , vol.268 , pp. 128-132
    • Takeda, M.1    Imada, K.2    Sato, T.3    Ito, A.4
  • 40
    • 0024323967 scopus 로고
    • Activation of matrix metalloproteinase 3 (stromelysin) and matrix metalloproteinase 2 ("gelatinase") by human neutrophil elastase and cathepsin G
    • Y. Okada, and I. Nakanishi Activation of matrix metalloproteinase 3 (stromelysin) and matrix metalloproteinase 2 ("gelatinase") by human neutrophil elastase and cathepsin G FEBS Letters 249 1989 353 356
    • (1989) FEBS Letters , vol.249 , pp. 353-356
    • Okada, Y.1    Nakanishi, I.2
  • 41
    • 0026145519 scopus 로고
    • Purification and characterization of human 72-kDa gelatinase (type IV collagenase). Use of immunolocalisation to demonstrate the non-coordinate regulation of the 72-kDa and 95-kDa gelatinases by human fibroblasts
    • D.S. Hipps, R.M. Hembry, A.J. Docherty, J.J. Reynolds, and G. Murphy Purification and characterization of human 72-kDa gelatinase (type IV collagenase). Use of immunolocalisation to demonstrate the non-coordinate regulation of the 72-kDa and 95-kDa gelatinases by human fibroblasts Biol. Chem. Hoppe Seyler 372 1991 287 296
    • (1991) Biol. Chem. Hoppe Seyler , vol.372 , pp. 287-296
    • Hipps, D.S.1    Hembry, R.M.2    Docherty, A.J.3    Reynolds, J.J.4    Murphy, G.5
  • 43
    • 0021016140 scopus 로고
    • Generalized dominant epidermolysis bullosa simplex: Decreased activity of a gelatinolytic protease in cultured fibroblasts as a phenotypic marker
    • G. Sanchez, J.L. Seltzer, A.Z. Eisen, P. Stapler, and E.A. Bauer Generalized dominant epidermolysis bullosa simplex: decreased activity of a gelatinolytic protease in cultured fibroblasts as a phenotypic marker J. Invest. Dermatol. 81 1983 576 579
    • (1983) J. Invest. Dermatol. , vol.81 , pp. 576-579
    • Sanchez, G.1    Seltzer, J.L.2    Eisen, A.Z.3    Stapler, P.4    Bauer, E.A.5
  • 44
    • 0025764664 scopus 로고
    • Production of gelatin-degrading matrix metalloproteinases ("type IV collagenases") and inhibitors by articular chondrocytes during their dedifferentiation by serial subcultures and under stimulation by interleukin-1 and tumor necrosis factor alpha
    • V. Lefebvre, C. Peeters-Joris, and G. Vaes Production of gelatin-degrading matrix metalloproteinases ("type IV collagenases") and inhibitors by articular chondrocytes during their dedifferentiation by serial subcultures and under stimulation by interleukin-1 and tumor necrosis factor alpha Biochim. Biophys. Acta 1094 1991 8 18
    • (1991) Biochim. Biophys. Acta , vol.1094 , pp. 8-18
    • Lefebvre, V.1    Peeters-Joris, C.2    Vaes, G.3
  • 45
    • 0022449762 scopus 로고
    • Gelatinase expression in generalized epidermolysis bullosa simplex fibroblasts
    • J.O. Winberg, and T. Gedde-Dahl Gelatinase expression in generalized epidermolysis bullosa simplex fibroblasts J. Invest. Dermatol. 87 1986 326 329
    • (1986) J. Invest. Dermatol. , vol.87 , pp. 326-329
    • Winberg, J.O.1    Gedde-Dahl, T.2
  • 46
    • 0026743132 scopus 로고
    • Epidermolysis bullosa simplex: Expression of gelatinase activity in cultured human skin fibroblasts
    • J.O. Winberg, and T. Gedde-Dahl Jr Epidermolysis bullosa simplex: expression of gelatinase activity in cultured human skin fibroblasts Biochem. Genet. 30 1992 401 420
    • (1992) Biochem. Genet. , vol.30 , pp. 401-420
    • Winberg, J.O.1    Gedde-Dahl Jr., T.2
  • 47
    • 0242611620 scopus 로고    scopus 로고
    • Characterizing degradation products of peptides containing N-terminal Cys residues by (off-line high-performance liquid chromatography)/matrix-assisted laser desorption/ionization quadrupole time-of-flight measurements
    • O.V. Krokhin, W. Ens, and K.G. Standing Characterizing degradation products of peptides containing N-terminal Cys residues by (off-line high-performance liquid chromatography)/matrix-assisted laser desorption/ionization quadrupole time-of-flight measurements Rapid Commun. Mass Spectrom. 17 2003 2528 2534
    • (2003) Rapid Commun. Mass Spectrom. , vol.17 , pp. 2528-2534
    • Krokhin, O.V.1    Ens, W.2    Standing, K.G.3
  • 48
    • 0024493129 scopus 로고
    • The activation of human type IV collagenase proenzyme. Sequence identification of the major conversion product following organomercurial activation
    • W.G. Stetler-Stevenson, H.C. Krutzsch, M.P. Wacher, I.M. Margulies, and L.A. Liotta The activation of human type IV collagenase proenzyme. Sequence identification of the major conversion product following organomercurial activation J. Biol. Chem. 264 1989 1353 1356
    • (1989) J. Biol. Chem. , vol.264 , pp. 1353-1356
    • Stetler-Stevenson, W.G.1    Krutzsch, H.C.2    Wacher, M.P.3    Margulies, I.M.4    Liotta, L.A.5
  • 49
    • 0034752257 scopus 로고    scopus 로고
    • Zymographic analysis of circulating and tissue forms of colon carcinoma gelatinase a (MMP-2) and B (MMP-9) separated by mono- and two-dimensional electrophoresis
    • I. Pucci-Minafra, S. Minafra, G. La Rocca, M. Barranca, S. Fontana, G. Alaimo, and Y. Okada Zymographic analysis of circulating and tissue forms of colon carcinoma gelatinase A (MMP-2) and B (MMP-9) separated by mono- and two-dimensional electrophoresis Matrix Biol. 20 2001 419 427
    • (2001) Matrix Biol. , vol.20 , pp. 419-427
    • Pucci-Minafra, I.1    Minafra, S.2    La Rocca, G.3    Barranca, M.4    Fontana, S.5    Alaimo, G.6    Okada, Y.7
  • 50
    • 0015327378 scopus 로고
    • A linear equation that describes the steady-state kinetics of enzymes and subcellular particles interacting with tightly bound inhibitors
    • P.J. Henderson A linear equation that describes the steady-state kinetics of enzymes and subcellular particles interacting with tightly bound inhibitors Biochem. J. 127 1972 321 333
    • (1972) Biochem. J. , vol.127 , pp. 321-333
    • Henderson, P.J.1
  • 51
    • 0028904148 scopus 로고
    • Autolytic activation of recombinant human 72 kilodalton type IV collagenase
    • U. Bergmann, A. Tuuttila, W.G. Stetler-Stevenson, and K. Tryggvason Autolytic activation of recombinant human 72 kilodalton type IV collagenase Biochemistry 34 1995 2819 2825
    • (1995) Biochemistry , vol.34 , pp. 2819-2825
    • Bergmann, U.1    Tuuttila, A.2    Stetler-Stevenson, W.G.3    Tryggvason, K.4
  • 52
    • 0030907533 scopus 로고    scopus 로고
    • Binding of 92 kDa and 72 kDa progelatinases to insoluble elastin modulates their proteolytic activation
    • H. Emonard, and W. Hornebeck Binding of 92 kDa and 72 kDa progelatinases to insoluble elastin modulates their proteolytic activation Biol. Chem. 378 1997 265 271
    • (1997) Biol. Chem. , vol.378 , pp. 265-271
    • Emonard, H.1    Hornebeck, W.2
  • 53
    • 0025922923 scopus 로고
    • 2+ and other ions as extracellular (first) messengers
    • 2+ and other ions as extracellular (first) messengers Physiol. Rev. 71 1991 371 411
    • (1991) Physiol. Rev. , vol.71 , pp. 371-411
    • Brown, E.M.1
  • 54
    • 0033548069 scopus 로고    scopus 로고
    • Identification of the tissue inhibitor of metalloproteinases-2 (TIMP-2) binding site on the hemopexin carboxyl domain of human gelatinase a by site-directed mutagenesis. the hierarchical role in binding TIMP-2 of the unique cationic clusters of hemopexin modules III and IV
    • C.M. Overall, A.E. King, D.K. Sam, A.D. Ong, T.T. Lau, and U.M. Wallon Identification of the tissue inhibitor of metalloproteinases-2 (TIMP-2) binding site on the hemopexin carboxyl domain of human gelatinase A by site-directed mutagenesis. The hierarchical role in binding TIMP-2 of the unique cationic clusters of hemopexin modules III and IV J. Biol. Chem. 274 1999 4421 4429
    • (1999) J. Biol. Chem. , vol.274 , pp. 4421-4429
    • Overall, C.M.1    King, A.E.2    Sam, D.K.3    Ong, A.D.4    Lau, T.T.5    Wallon, U.M.6
  • 55
    • 9644266658 scopus 로고    scopus 로고
    • Drosophila alcohol dehydrogenase: Acetate-enzyme interactions and novel insights into the effects of electrostatics on catalysis
    • J. Benach, J.O. Winberg, J.S. Svendsen, S. Atrian, R. Gonzalez-Duarte, and R. Ladenstein Drosophila alcohol dehydrogenase: acetate-enzyme interactions and novel insights into the effects of electrostatics on catalysis J. Mol. Biol. 345 2005 579 598
    • (2005) J. Mol. Biol. , vol.345 , pp. 579-598
    • Benach, J.1    Winberg, J.O.2    Svendsen, J.S.3    Atrian, S.4    Gonzalez-Duarte, R.5    Ladenstein, R.6
  • 56
    • 0029610231 scopus 로고
    • Intermolecular autolytic cleavage can contribute to the activation of progelatinase a by cell membranes
    • S.J. Atkinson, T. Crabbe, S. Cowell, R.V. Ward, M.J. Butler, and H. Sato Intermolecular autolytic cleavage can contribute to the activation of progelatinase A by cell membranes J. Biol. Chem. 270 1995 30479 30485
    • (1995) J. Biol. Chem. , vol.270 , pp. 30479-30485
    • Atkinson, S.J.1    Crabbe, T.2    Cowell, S.3    Ward, R.V.4    Butler, M.J.5    Sato, H.6
  • 57
    • 1642279517 scopus 로고    scopus 로고
    • Protease-activated receptors: Contribution to physiology and disease
    • V.S. Ossovskaya, and N.W. Bunnett Protease-activated receptors: contribution to physiology and disease Physiol. Rev. 84 2004 579 621
    • (2004) Physiol. Rev. , vol.84 , pp. 579-621
    • Ossovskaya, V.S.1    Bunnett, N.W.2
  • 58
    • 0033636735 scopus 로고    scopus 로고
    • The role of up-regulated serine proteases and matrix metalloproteinases in the pathogenesis of a murine model of colitis
    • J.F. Tarlton, C.V. Whiting, D. Tunmore, S. Bregenholt, J. Reimann, M.H. Claesson, and P.W. Bland The role of up-regulated serine proteases and matrix metalloproteinases in the pathogenesis of a murine model of colitis Am. J. Pathol. 157 2000 1927 1935
    • (2000) Am. J. Pathol. , vol.157 , pp. 1927-1935
    • Tarlton, J.F.1    Whiting, C.V.2    Tunmore, D.3    Bregenholt, S.4    Reimann, J.5    Claesson, M.H.6    Bland, P.W.7
  • 59
    • 0035906848 scopus 로고    scopus 로고
    • The levels of trypsinogen isoenzymes in ovarian tumour cyst fluids are associated with promatrix metalloproteinase-9 but not promatrix metalloproteinase-2 activation
    • A. Paju, T. Sorsa, T. Tervahartiala, E. Koivunen, C. Haglund, and A. Leminen The levels of trypsinogen isoenzymes in ovarian tumour cyst fluids are associated with promatrix metalloproteinase-9 but not promatrix metalloproteinase-2 activation Br. J. Cancer 84 2001 1363 1371
    • (2001) Br. J. Cancer , vol.84 , pp. 1363-1371
    • Paju, A.1    Sorsa, T.2    Tervahartiala, T.3    Koivunen, E.4    Haglund, C.5    Leminen, A.6
  • 60
    • 0030998651 scopus 로고    scopus 로고
    • Detection of matrix metalloproteinase activity in human pancreatic cancer
    • T. Koshiba, R. Hosotani, M. Wada, K. Fujimoto, J.U. Lee, and R. Doi Detection of matrix metalloproteinase activity in human pancreatic cancer Surg. Today 27 1997 302 304
    • (1997) Surg. Today , vol.27 , pp. 302-304
    • Koshiba, T.1    Hosotani, R.2    Wada, M.3    Fujimoto, K.4    Lee, J.U.5    Doi, R.6
  • 62
    • 0028113717 scopus 로고
    • Increased gelatinase a (MMP-2) and cathepsin B activity in invasive tumor regions of human colon cancer samples
    • M.R. Emmert-Buck, M.J. Roth, Z. Zhuang, E. Campo, J. Rozhin, and B.F. Sloane Increased gelatinase A (MMP-2) and cathepsin B activity in invasive tumor regions of human colon cancer samples Am. J. Pathol. 145 1994 1285 1290
    • (1994) Am. J. Pathol. , vol.145 , pp. 1285-1290
    • Emmert-Buck, M.R.1    Roth, M.J.2    Zhuang, Z.3    Campo, E.4    Rozhin, J.5    Sloane, B.F.6
  • 63
    • 0025209835 scopus 로고
    • Cyst fluid of ovarian cancer patients contains high concentrations of trypsinogen-2
    • E. Koivunen, O. Itkonen, H. Halila, and U.H. Stenman Cyst fluid of ovarian cancer patients contains high concentrations of trypsinogen-2 Cancer Res. 50 1990 2375 2378
    • (1990) Cancer Res. , vol.50 , pp. 2375-2378
    • Koivunen, E.1    Itkonen, O.2    Halila, H.3    Stenman, U.H.4
  • 64
    • 0027963508 scopus 로고
    • Identification of one- and two-chain forms of trypsinogen 1 produced by a human gastric adenocarcinoma cell line
    • N. Koshikawa, H. Yasumitsu, Y. Nagashima, M. Umeda, and K. Miyazaki Identification of one- and two-chain forms of trypsinogen 1 produced by a human gastric adenocarcinoma cell line Biochem. J. 303 1994 187 190
    • (1994) Biochem. J. , vol.303 , pp. 187-190
    • Koshikawa, N.1    Yasumitsu, H.2    Nagashima, Y.3    Umeda, M.4    Miyazaki, K.5
  • 65
    • 0032519608 scopus 로고    scopus 로고
    • Involvement of matrix metalloproteinase-2 activity in invasion and metastasis of pancreatic carcinoma
    • T. Koshiba, R. Hosotani, M. Wada, Y. Miyamoto, K. Fujimoto, and J.U. Lee Involvement of matrix metalloproteinase-2 activity in invasion and metastasis of pancreatic carcinoma Cancer 82 1998 642 650
    • (1998) Cancer , vol.82 , pp. 642-650
    • Koshiba, T.1    Hosotani, R.2    Wada, M.3    Miyamoto, Y.4    Fujimoto, K.5    Lee, J.U.6
  • 67
    • 0023778982 scopus 로고
    • Biochemical justification of drainage of the thoracic duct in acute necrotic-hemorrhagic pancreatitis
    • G. Deby-Dupont, M. Reynaert, P. Damas, M. Lamy, and P. Franchimont Biochemical justification of drainage of the thoracic duct in acute necrotic-hemorrhagic pancreatitis Acta. Gastroenterol. Belg. 51 1988 31 40
    • (1988) Acta. Gastroenterol. Belg. , vol.51 , pp. 31-40
    • Deby-Dupont, G.1    Reynaert, M.2    Damas, P.3    Lamy, M.4    Franchimont, P.5
  • 69
    • 0034758720 scopus 로고    scopus 로고
    • Increased matrix metalloproteinase expression and activation following experimental acute pancreatitis
    • B.E. Muhs, S. Patel, H. Yee, S. Marcus, and P. Shamamian Increased matrix metalloproteinase expression and activation following experimental acute pancreatitis J. Surg. Res. 101 2001 21 28
    • (2001) J. Surg. Res. , vol.101 , pp. 21-28
    • Muhs, B.E.1    Patel, S.2    Yee, H.3    Marcus, S.4    Shamamian, P.5
  • 70
    • 0034235034 scopus 로고    scopus 로고
    • Diagnosis and management of acute pancreatitis
    • A. Munoz, and D.A. Katerndahl Diagnosis and management of acute pancreatitis Am. Fam. Physician 62 2000 164 174
    • (2000) Am. Fam. Physician , vol.62 , pp. 164-174
    • Munoz, A.1    Katerndahl, D.A.2
  • 71
    • 0034651865 scopus 로고    scopus 로고
    • Proteases in the evaluation of pancreatic function and pancreatic disease
    • D.M. Goldberg Proteases in the evaluation of pancreatic function and pancreatic disease Clin. Chim. Acta 291 2000 201 221
    • (2000) Clin. Chim. Acta , vol.291 , pp. 201-221
    • Goldberg, D.M.1
  • 72
    • 0015935029 scopus 로고
    • On the physiological role of 2 -macroglobulin
    • H. Rinderknecht, and M.C. Geokas On the physiological role of 2 -macroglobulin Biochim. Biophys. Acta 295 1973 233 244
    • (1973) Biochim. Biophys. Acta , vol.295 , pp. 233-244
    • Rinderknecht, H.1    Geokas, M.C.2
  • 73
    • 0019877193 scopus 로고
    • Inhibition of alpha 2-macroglobulin-bound trypsin by soybean trypsin inhibitor
    • J.G. Bieth, M. Tourbez-Perrin, and F. Pochon Inhibition of alpha 2-macroglobulin-bound trypsin by soybean trypsin inhibitor J. Biol. Chem. 256 1981 7954 7957
    • (1981) J. Biol. Chem. , vol.256 , pp. 7954-7957
    • Bieth, J.G.1    Tourbez-Perrin, M.2    Pochon, F.3
  • 75
    • 0344154301 scopus 로고    scopus 로고
    • Colchicine induces membrane-associated activation of matrix metalloproteinase-2 in osteosarcoma cells in an S100A4-independent manner
    • T. Loennechen, B. Mathisen, J. Hansen, R.I. Lindstad, S.A. El-Gewely, and K. Andersen Colchicine induces membrane-associated activation of matrix metalloproteinase-2 in osteosarcoma cells in an S100A4-independent manner Biochem. Pharmacol. 66 2003 2341 2353
    • (2003) Biochem. Pharmacol. , vol.66 , pp. 2341-2353
    • Loennechen, T.1    Mathisen, B.2    Hansen, J.3    Lindstad, R.I.4    El-Gewely, S.A.5    Andersen, K.6
  • 76
    • 0026505650 scopus 로고
    • A novel coumarin-labelled peptide for sensitive continuous assays of the matrix metalloproteinases
    • C.G. Knight, F. Willenbrock, and G. Murphy A novel coumarin-labelled peptide for sensitive continuous assays of the matrix metalloproteinases FEBS Letters 296 1992 263 266
    • (1992) FEBS Letters , vol.296 , pp. 263-266
    • Knight, C.G.1    Willenbrock, F.2    Murphy, G.3
  • 77
    • 0034624033 scopus 로고    scopus 로고
    • Macrophages secrete matrix metalloproteinase 9 covalently linked to the core protein of chondroitin sulphate proteoglycans
    • J.O. Winberg, S.O. Kolset, E. Berg, and L. Uhlin-Hansen Macrophages secrete matrix metalloproteinase 9 covalently linked to the core protein of chondroitin sulphate proteoglycans J. Mol. Biol. 304 2000 669 680
    • (2000) J. Mol. Biol. , vol.304 , pp. 669-680
    • Winberg, J.O.1    Kolset, S.O.2    Berg, E.3    Uhlin-Hansen, L.4
  • 78
    • 0141704099 scopus 로고    scopus 로고
    • Calcium-induced activation and truncation of promatrix metalloproteinase-9 linked to the core protein of chondroitin sulfate proteoglycans
    • J.O. Winberg, E. Berg, S.O. Kolset, and L. Uhlin-Hansen Calcium-induced activation and truncation of promatrix metalloproteinase-9 linked to the core protein of chondroitin sulfate proteoglycans Eur. J. Biochem. 270 2003 3996 4007
    • (2003) Eur. J. Biochem. , vol.270 , pp. 3996-4007
    • Winberg, J.O.1    Berg, E.2    Kolset, S.O.3    Uhlin-Hansen, L.4
  • 79
    • 0020533455 scopus 로고
    • Drosophila melanogaster alcohol dehydrogenase: An electrophoretic study of the AdhS, AdhF, and AdhUF alleloenzymes
    • J.O. Winberg, D.R. Thatcher, and J.S. McKinley-McKee Drosophila melanogaster alcohol dehydrogenase: an electrophoretic study of the AdhS, AdhF, and AdhUF alleloenzymes Biochem. Genet. 21 1983 63 80
    • (1983) Biochem. Genet. , vol.21 , pp. 63-80
    • Winberg, J.O.1    Thatcher, D.R.2    McKinley-Mckee, J.S.3
  • 80
    • 0037090502 scopus 로고    scopus 로고
    • Optimization of guanidination procedures for MALDI mass mapping
    • R.L. Beardsley, and J.P. Reilly Optimization of guanidination procedures for MALDI mass mapping Anal. Chem. 74 2002 1884 1890
    • (2002) Anal. Chem. , vol.74 , pp. 1884-1890
    • Beardsley, R.L.1    Reilly, J.P.2
  • 81
    • 84986522918 scopus 로고
    • ICM-a new method for protein modelling and design. Application to docking and structure prediction from the distroed native conformation
    • R.A. Abagyan, M.M. Totrov, and D.N. Kuznetsov ICM-a new method for protein modelling and design. Application to docking and structure prediction from the distroed native conformation J. Comput. Chem. 15 1994 488 506
    • (1994) J. Comput. Chem. , vol.15 , pp. 488-506
    • Abagyan, R.A.1    Totrov, M.M.2    Kuznetsov, D.N.3
  • 82
    • 0027955787 scopus 로고
    • Biased probability Monte Carlo conformational searches and electrostatic calculations for peptides and proteins
    • R. Abagyan, and M. Totrov Biased probability Monte Carlo conformational searches and electrostatic calculations for peptides and proteins J. Mol. Biol. 235 1994 983 1002
    • (1994) J. Mol. Biol. , vol.235 , pp. 983-1002
    • Abagyan, R.1    Totrov, M.2
  • 83
    • 1842377505 scopus 로고    scopus 로고
    • Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1
    • F.X. Gomis-Ruth, K. Maskos, M. Betz, A. Bergner, R. Huber, and K. Suzuki Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1 Nature 389 1997 77 81
    • (1997) Nature , vol.389 , pp. 77-81
    • Gomis-Ruth, F.X.1    Maskos, K.2    Betz, M.3    Bergner, A.4    Huber, R.5    Suzuki, K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.