메뉴 건너뛰기




Volumn 378, Issue 3-4, 1997, Pages 151-160

Activation mechanisms of matrix metalloproteinases

Author keywords

Activation; Extracellular matrix; Matrix metalloproteinases; Matrixins; Proteinases; TIMPs

Indexed keywords

CELL ENZYME; CELL SURFACE PROTEIN; COLLAGENASE; CYSTEINE; ENZYME PRECURSOR; GELATINASE A; MATRIX METALLOPROTEINASE; METALLOPROTEINASE; PROTEINASE; STROMELYSIN;

EID: 0030957218     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (1067)

References (73)
  • 5
    • 17544378260 scopus 로고    scopus 로고
    • Characterization of the 46-kDa intermediates of matrix metalloproteinase 3 (stromelysin 1) obtained by site-directed mutation of phenylalanine 83
    • Benbow, U., Butticè, G., Nagase, H., and Kurkinen, M. (1996). Characterization of the 46-kDa intermediates of matrix metalloproteinase 3 (stromelysin 1) obtained by site-directed mutation of phenylalanine 83. J. Biol. Chem. 271, 10715-10722.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10715-10722
    • Benbow, U.1    Butticè, G.2    Nagase, H.3    Kurkinen, M.4
  • 6
    • 0028324076 scopus 로고
    • The X-ray crystal structure of the catalytic domain of human neutrophil collagenase inhibited by a substrate analogue reveals the essentials for catalysis and specificity
    • Bode, W., Reinemer, P., Huber, R., Kleine, T., Schnierer, S., and Tschesche, H. (1994). The X-ray crystal structure of the catalytic domain of human neutrophil collagenase inhibited by a substrate analogue reveals the essentials for catalysis and specificity. EMBO J. 13, 1263-1269.
    • (1994) EMBO J. , vol.13 , pp. 1263-1269
    • Bode, W.1    Reinemer, P.2    Huber, R.3    Kleine, T.4    Schnierer, S.5    Tschesche, H.6
  • 8
    • 0029560995 scopus 로고
    • Use of an active-site inhibitor of stromelysin to elucidate the mechanism of prostromelysin activation
    • Cameron, P.M., Marcy, A.I., Rokosz, L.L., and Hermes, J.D. (1995). Use of an active-site inhibitor of stromelysin to elucidate the mechanism of prostromelysin activation. Bioorg. Chem. 23, 415-426.
    • (1995) Bioorg. Chem. , vol.23 , pp. 415-426
    • Cameron, P.M.1    Marcy, A.I.2    Rokosz, L.L.3    Hermes, J.D.4
  • 9
    • 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, L.-C., Noelken, M.E., and Nagase, H. (1993). Disruption of the cysteine-75 and zinc ion coordination is not sufficient to activate the precursor of human matrix metalloproteinase 3 (stromelysin 1). Biochemistry 32, 10289-10295.
    • (1993) Biochemistry , vol.32 , pp. 10289-10295
    • Chen, L.-C.1    Noelken, M.E.2    Nagase, H.3
  • 11
    • 0028556638 scopus 로고
    • Reciprocated matrix metalloproteinase activation: A process performed by interstitial collagenase and progelatinase A
    • Crabbe, T., O'Connell, J., Smith, B.J., and Docherty, A.J.P. (1994a). Reciprocated matrix metalloproteinase activation: A process performed by interstitial collagenase and progelatinase A. Biochemistry 33, 14419-14425.
    • (1994) Biochemistry , vol.33 , pp. 14419-14425
    • Crabbe, T.1    O'Connell, J.2    Smith, B.J.3    Docherty, A.J.P.4
  • 12
    • 0028291374 scopus 로고
    • Human progelatinase A can be activated by matrilysin
    • Crabbe, T., Smith, B., O'Connell, J., and Docherty, A. (1994b). Human progelatinase A can be activated by matrilysin. FEBS Lett. 345, 14-16.
    • (1994) FEBS Lett. , vol.345 , pp. 14-16
    • Crabbe, T.1    Smith, B.2    O'Connell, J.3    Docherty, A.4
  • 13
    • 0025809874 scopus 로고
    • Inhibition of autoproteolytic activation of interstitial procollagenase by recombinant metalloproteinase inhibitor MI/TIMP-2
    • DeClerck, Y.A., Yean, T.-D., Lu, H.S., Ting, J., and Langley, K.E. (1991). Inhibition of autoproteolytic activation of interstitial procollagenase by recombinant metalloproteinase inhibitor MI/TIMP-2. J. Biol. Chem. 266, 3892-3899.
    • (1991) J. Biol. Chem. , vol.266 , pp. 3892-3899
    • DeClerck, Y.A.1    Yean, T.-D.2    Lu, H.S.3    Ting, J.4    Langley, K.E.5
  • 14
    • 0025883277 scopus 로고
    • Plasminogen activation by receptor-bound urokinase. A kinetic study with both cell-associated and isolated receptor
    • Ellis, V., Behrendt, N., and Dano, K. (1991). Plasminogen activation by receptor-bound urokinase. A kinetic study with both cell-associated and isolated receptor. J. Biol. Chem. 266, 12752-12758.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12752-12758
    • Ellis, V.1    Behrendt, N.2    Dano, K.3
  • 15
    • 0027076170 scopus 로고
    • The urokinase receptor: Involvement in cell surface proteolysis and cancer invasion
    • Ellis, V., Pyke, C., Eriksen, J., Solberg, H., and Dano, K. (1992). The urokinase receptor: Involvement in cell surface proteolysis and cancer invasion. Ann. N.Y. Acad. Sci. 667, 13-31.
    • (1992) Ann. N.Y. Acad. Sci. , vol.667 , pp. 13-31
    • Ellis, V.1    Pyke, C.2    Eriksen, J.3    Solberg, H.4    Dano, K.5
  • 16
    • 0027967779 scopus 로고
    • Multiple sites of the propeptide region of human stromelysin-1 are required for maintaining a latent form of the enzyme
    • Freimark, B.D., Feeser, W.S., and Rosenfeld, S.A. (1994). Multiple sites of the propeptide region of human stromelysin-1 are required for maintaining a latent form of the enzyme. J. Biol. Chem. 269, 26982-26987.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26982-26987
    • Freimark, B.D.1    Feeser, W.S.2    Rosenfeld, S.A.3
  • 17
    • 0029034457 scopus 로고
    • Activation of progelatinase B (MMP-9) by gelatinase A (MMP-2)
    • Fridman, R., Toth, M., Peña, D., and Mobashery, S. (1995). Activation of progelatinase B (MMP-9) by gelatinase A (MMP-2). Cancer Res. 55, 2548-2555.
    • (1995) Cancer Res. , vol.55 , pp. 2548-2555
    • Fridman, R.1    Toth, M.2    Peña, D.3    Mobashery, S.4
  • 18
    • 0029774746 scopus 로고    scopus 로고
    • APMA (4-aminophenylmercuric acetate) activation of stromelysin-1 involves protein interactions in addition to those with cysteine-75 in the propeptide
    • Galazka, G., Windsor, L.J., Birkedal-Hansen, H., and Engler, J.A. (1996). APMA (4-aminophenylmercuric acetate) activation of stromelysin-1 involves protein interactions in addition to those with cysteine-75 in the propeptide. Biochemistry 35, 11221-11227.
    • (1996) Biochemistry , vol.35 , pp. 11221-11227
    • Galazka, G.1    Windsor, L.J.2    Birkedal-Hansen, H.3    Engler, J.A.4
  • 19
    • 0026630048 scopus 로고
    • Interaction of 92-kDa type IV collagenase with the tissue inhibitor of metalloproteinases prevents dimerization, complex formation with interstitial collagenase, and activation of the proenzyme with stromelysin
    • Goldberg, G.I., Strongin, A., Collier, I.E., Genrich, L.T., and Marmer, B.L. (1992). Interaction of 92-kDa type IV collagenase with the tissue inhibitor of metalloproteinases prevents dimerization, complex formation with interstitial collagenase, and activation of the proenzyme with stromelysin. J. Biol. Chem. 267, 4583-4591.
    • (1992) J. Biol. Chem. , vol.267 , pp. 4583-4591
    • Goldberg, G.I.1    Strongin, A.2    Collier, I.E.3    Genrich, L.T.4    Marmer, B.L.5
  • 20
    • 0011891457 scopus 로고
    • EXAFS evidence for a 'cysteine switch' in the activation of prostromelysin
    • Holz, R.C., Salowe, S.P., Smith, C.K., Cuca, G.C., and Que, L. Jr. (1992). EXAFS evidence for a 'cysteine switch' in the activation of prostromelysin. J. Am. Chem. Soc. 114, 9611-9614.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 9611-9614
    • Holz, R.C.1    Salowe, S.P.2    Smith, C.K.3    Cuca, G.C.4    Que Jr., L.5
  • 21
    • 0028913443 scopus 로고
    • Matrix metalloproteinase 7 (matrilysin) from human rectal carcinoma cells. Activation of the precursor, interaction with other matrix metalloproteinases and enzymic properties
    • Imai, K., Yokohama, Y., Nakanishi, I., Ohuchi, E., Fujii, Y., Nakai, N., and Okada, Y. (1995). Matrix metalloproteinase 7 (matrilysin) from human rectal carcinoma cells. Activation of the precursor, interaction with other matrix metalloproteinases and enzymic properties. J. Biol. Chem. 270, 6691-6697.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6691-6697
    • Imai, K.1    Yokohama, Y.2    Nakanishi, I.3    Ohuchi, E.4    Fujii, Y.5    Nakai, N.6    Okada, Y.7
  • 22
    • 0029019838 scopus 로고
    • Preferential inactivation of tissue inhibitor of metalloproteinases-1 that is bound to the precursor of matrix metalloproteinase 9 (progelatinase B) by human neutrophil elastase
    • Itoh, Y., and Nagase, H. (1995). Preferential inactivation of tissue inhibitor of metalloproteinases-1 that is bound to the precursor of matrix metalloproteinase 9 (progelatinase B) by human neutrophil elastase. J. Biol. Chem. 270, 16518-16521.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16518-16521
    • Itoh, Y.1    Nagase, H.2
  • 23
    • 0029031780 scopus 로고
    • Steps involved in activation of the complex of pro-matrix metalloproteinase 2 (progelatinase A) and tissue inhibitor of metalloproteinases (TIMP)-2 by 4-aminophenylmercuric acetate
    • Itoh, Y., Binner S., and Nagase, H. (1995). Steps involved in activation of the complex of pro-matrix metalloproteinase 2 (progelatinase A) and tissue inhibitor of metalloproteinases (TIMP)-2 by 4-aminophenylmercuric acetate. Biochem. J. 308, 645-651.
    • (1995) Biochem. J. , vol.308 , pp. 645-651
    • Itoh, Y.1    Binner, S.2    Nagase, H.3
  • 25
    • 0030025404 scopus 로고    scopus 로고
    • Activation of human neutrophil procollagenase by stromelysin 2
    • Knäuper, V., Murphy, G., and Tschesche, H. (1996a). Activation of human neutrophil procollagenase by stromelysin 2. Eur. J. Biochem. 235, 187-191.
    • (1996) Eur. J. Biochem. , vol.235 , pp. 187-191
    • Knäuper, V.1    Murphy, G.2    Tschesche, H.3
  • 27
    • 0025831535 scopus 로고
    • r active forms, and a comparison of recombinant with natural stromelysin activities
    • r active forms, and a comparison of recombinant with natural stromelysin activities. Biochem. J. 276, 217-221.
    • (1991) Biochem. J. , vol.276 , pp. 217-221
    • Koklitis, P.A.1    Murphy, G.2    Sutton, C.3    Angal, S.4
  • 28
    • 0025822038 scopus 로고
    • The complex between a tissue inhibitor of metalloproteinases (TIMP-2) and 72-kDa progelatinase is a metalloproteinase inhibitor
    • Kolkenbrock, H., Orgel, D., Hecker-Kia, A., Noack, W., and Ulbrich, N. (1991). The complex between a tissue inhibitor of metalloproteinases (TIMP-2) and 72-kDa progelatinase is a metalloproteinase inhibitor. Eur. J. Biochem. 198, 775-781.
    • (1991) Eur. J. Biochem. , vol.198 , pp. 775-781
    • Kolkenbrock, H.1    Orgel, D.2    Hecker-Kia, A.3    Noack, W.4    Ulbrich, N.5
  • 30
    • 0030592783 scopus 로고    scopus 로고
    • The recombinant catalytic domain of membrane-type matrix metalloproteinase-1 (MT1-MMP) induces activation of progelatinase A and progelatinase A complexed with TIMP-2
    • Uchte, A., Kolkenbrock, H., and Tschesche, H. (1996). The recombinant catalytic domain of membrane-type matrix metalloproteinase-1 (MT1-MMP) induces activation of progelatinase A and progelatinase A complexed with TIMP-2. FEBS Lett. 397, 277-282.
    • (1996) FEBS Lett. , vol.397 , pp. 277-282
    • Uchte, A.1    Kolkenbrock, H.2    Tschesche, H.3
  • 32
    • 0026521973 scopus 로고
    • The C-terminal domain of 72 kDa gelatinase A is not required for catalysis, but is essential for membrane activation and modulates interactions with tissue inhibitors of metalloproteinases
    • Murphy, G., Willenbrock, F., Ward, R.V., Cockett, M.I., Eaton, D., and Docherty, A.J. (1992b). The C-terminal domain of 72 kDa gelatinase A is not required for catalysis, but is essential for membrane activation and modulates interactions with tissue inhibitors of metalloproteinases. Biochem. J. 283, 637-641.
    • (1992) Biochem. J. , vol.283 , pp. 637-641
    • Murphy, G.1    Willenbrock, F.2    Ward, R.V.3    Cockett, M.I.4    Eaton, D.5    Docherty, A.J.6
  • 33
    • 0025335183 scopus 로고
    • Stepwise activation of mechanisms of the precursor of matrix metalloproteinase 3 (stromelysin) by proteinases and (4-aminophenyl) mercuric acetate
    • Nagase, H., Enghild, J.J., Suzuki, K., and Salvesen, G. (1990). Stepwise activation of mechanisms of the precursor of matrix metalloproteinase 3 (stromelysin) by proteinases and (4-aminophenyl) mercuric acetate. Biochemistry 29, 5783-5789.
    • (1990) Biochemistry , vol.29 , pp. 5783-5789
    • Nagase, H.1    Enghild, J.J.2    Suzuki, K.3    Salvesen, G.4
  • 34
    • 0000736684 scopus 로고    scopus 로고
    • Matrix Metalloproteinases
    • N.M. Hooper, ed. (London, England: Taylor and Francis)
    • Nagase, H. (1996). Matrix Metalloproteinases. In: Zinc Metalloproteinases in Health and Disease, N.M. Hooper, ed. (London, England: Taylor and Francis), pp. 153-204.
    • (1996) Zinc Metalloproteinases in Health and Disease , pp. 153-204
    • Nagase, H.1
  • 35
    • 0000702015 scopus 로고    scopus 로고
    • Proteinases and matrix degradation
    • W.N. Kelley, E.D. Harris, Jr., S. Ruddy, C.B. Sledge, eds. (Philadelphia, PA, USA: W.B. Saunders Co.)
    • Nagase, H., and Okada, Y. (1996). Proteinases and matrix degradation. In: The Textbook of Rheumatology (5th Edition), W.N. Kelley, E.D. Harris, Jr., S. Ruddy, C.B. Sledge, eds. (Philadelphia, PA, USA: W.B. Saunders Co.), pp. 323-341.
    • (1996) The Textbook of Rheumatology (5th Edition) , pp. 323-341
    • Nagase, H.1    Okada, Y.2
  • 36
    • 0029103339 scopus 로고
    • Expression of membrane-type matrix metalloproteinase in human gastric carcinomas
    • Nomura, H., Sato, H., Seiki, M., Mai, M., and Okada, Y. (1995). Expression of membrane-type matrix metalloproteinase in human gastric carcinomas. Cancer Res. 55, 3263-3266.
    • (1995) Cancer Res. , vol.55 , pp. 3263-3266
    • Nomura, H.1    Sato, H.2    Seiki, M.3    Mai, M.4    Okada, Y.5
  • 37
    • 0026660964 scopus 로고
    • Matrix metalloproteinase 3 (stromelysin) activates the precursor for the human matrix metalloproteinase 9
    • Ogata, Y., Enghild, J.J., and Nagase, H. (1992). Matrix metalloproteinase 3 (stromelysin) activates the precursor for the human matrix metalloproteinase 9. J. Bio. Chem. 267, 3581-3584.
    • (1992) J. Bio. Chem. , vol.267 , pp. 3581-3584
    • Ogata, Y.1    Enghild, J.J.2    Nagase, H.3
  • 38
    • 0029147750 scopus 로고
    • Steps involved in activation of the pro-matrix metalloproteinase 9 (progelatinase B)-tissue inhibitor of metalloproteinases-1 complex by 4-aminophenylmercuric acetate and proteinases
    • Ogata, Y., Itoh, Y., and Nagase, H. (1995). Steps involved in activation of the pro-matrix metalloproteinase 9 (progelatinase B)-tissue inhibitor of metalloproteinases-1 complex by 4-aminophenylmercuric acetate and proteinases. J. Biol. Chem. 270, 18506-18511.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18506-18511
    • Ogata, Y.1    Itoh, Y.2    Nagase, H.3
  • 39
    • 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., and Okada, Y. (1997). Membrane type I matrix metalloproteinase digests interstitial collagens and other extracellular matrix macromolecules. J. Biol. Chem. 272, 2446-2451.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2446-2451
    • Ohuchi, E.1    Imai, K.2    Fujii, Y.3    Sato, H.4    Seiki, M.5    Okada, Y.6
  • 40
    • 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, E.D., Jr., and Nagase, H. (1988). The precursor of a metalloendopeptidase from human rheumatoid synovial fibroblasts. Purification and mechanisms of activation by endopeptidases and 4-aminophenylmercuric acetate. Biochem. J. 254, 731-741.
    • (1988) Biochem. J. , vol.254 , pp. 731-741
    • Okada, Y.1    Harris Jr., E.D.2    Nagase, H.3
  • 41
    • 0025616093 scopus 로고
    • Matrix metalloproteinase 2 from human rheumatoid synovial fibroblasts. Purification and activation of the precursor and enzymic properties
    • Okada, Y., Morodomi, T., Enghild, J.J., Suzuki, K., Yasui, A., Nakanishi, I., Salvesen, G., and Nagase, H. (1990). Matrix metalloproteinase 2 from human rheumatoid synovial fibroblasts. Purification and activation of the precursor and enzymic properties. Eur. J. Biochem. 194, 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    Salvesen, G.7    Nagase, H.8
  • 42
    • 0026795140 scopus 로고
    • Matrix metalloproteinase 9 (92-kDa gelatinase/type IV collagenase) from HT 1080 human fibrosarcoma cells. Purification and activation of the precursor and enzymic properties
    • Okada, Y., Gonoji, Y., Naka, K., Tomita, K., Nakanishi, I., Iwata, K., Yamashita, K., and Hayakawa, T. (1992). Matrix metalloproteinase 9 (92-kDa gelatinase/type IV collagenase) from HT 1080 human fibrosarcoma cells. Purification and activation of the precursor and enzymic properties. J. Biol. Chem. 267, 21712-21719.
    • (1992) J. Biol. Chem. , vol.267 , pp. 21712-21719
    • Okada, Y.1    Gonoji, Y.2    Naka, K.3    Tomita, K.4    Nakanishi, I.5    Iwata, K.6    Yamashita, K.7    Hayakawa, T.8
  • 43
    • 0025676432 scopus 로고
    • Concanavalin A produces a matrix-degradative phenotype in human fibroblasts. Induction and endogenous activation of collagenase, 72-kDa gelatinase, and Pump-1 is accompanied by the suppression of the tissue inhibitor of matrix metalloproteinases
    • Overall, C.M., and Sodek, J. (1990). Concanavalin A produces a matrix-degradative phenotype in human fibroblasts. Induction and endogenous activation of collagenase, 72-kDa gelatinase, and Pump-1 is accompanied by the suppression of the tissue inhibitor of matrix metalloproteinases. J. Biol. Chem. 265, 21141-21151.
    • (1990) J. Biol. Chem. , vol.265 , pp. 21141-21151
    • Overall, C.M.1    Sodek, J.2
  • 44
    • 0029014101 scopus 로고
    • Furin-dependent intracellular activation of the human stromelysin-3 zymogen
    • Pei, D., and Weiss, S.J. (1995). Furin-dependent intracellular activation of the human stromelysin-3 zymogen. Nature 375, 244-247.
    • (1995) Nature , vol.375 , pp. 244-247
    • Pei, D.1    Weiss, S.J.2
  • 45
    • 0029885707 scopus 로고    scopus 로고
    • Transmembrane-deletion mutants of the membrane-type matrix metalloproteinase-1 process progelatinase A and express intrinsic matrix-degrading activity
    • Pei, D., and Weiss, S.J. (1996). Transmembrane-deletion mutants of the membrane-type matrix metalloproteinase-1 process progelatinase A and express intrinsic matrix-degrading activity. J. Biol. Chem. 271, 9135-9140.
    • (1996) J. Biol. Chem. , vol.271 , pp. 9135-9140
    • Pei, D.1    Weiss, S.J.2
  • 47
    • 0030022539 scopus 로고    scopus 로고
    • Molecular cloning of a novel membrane-type matrix metalloproteinase from a human breast carcinoma
    • Puente, X.S., Pendás, A.M., Llano, E., Velasco, G., and López-Otín, C. (1996). Molecular cloning of a novel membrane-type matrix metalloproteinase from a human breast carcinoma. Cancer Res. 56, 944-949.
    • (1996) Cancer Res. , vol.56 , pp. 944-949
    • Puente, X.S.1    Pendás, A.M.2    Llano, E.3    Velasco, G.4    López-Otín, C.5
  • 48
    • 0028040070 scopus 로고
    • Structural implications for the role of the N-terminus in the 'superactivation' of collagenases. A crystallographic study
    • Reinemer, P., Grams, F., Huber, R., Kleine, T., Schnierer, S., Piper, M., Tschesche, H., and Bode, W. (1994). Structural implications for the role of the N-terminus in the 'superactivation' of collagenases. A crystallographic study. FEBS Lett. 338, 227-233.
    • (1994) FEBS Lett. , vol.338 , pp. 227-233
    • Reinemer, P.1    Grams, F.2    Huber, R.3    Kleine, T.4    Schnierer, S.5    Piper, M.6    Tschesche, H.7    Bode, W.8
  • 50
    • 0024146930 scopus 로고
    • Cell-associated plasminogen activation: Regulation and physiological functions
    • Saksela, O., and Rifkin, D.B. (1988). Cell-associated plasminogen activation: Regulation and physiological functions. Annu. Rev. Cell. Biol. 4, 93-126.
    • (1988) Annu. Rev. Cell. Biol. , vol.4 , pp. 93-126
    • Saksela, O.1    Rifkin, D.B.2
  • 51
    • 0026750383 scopus 로고
    • Characterization of zinc-binding sites in human stromelysin-1: Stoichiometry of the catalytic domain and identification of a cysteine ligand in the proenzyme
    • Salowe, S.P., Marcy, A.I., Cuca, G.C., Smith, C.K., Kopka, I.E., Hagmann, W.K., and Hermes, J.D. (1992). Characterization of zinc-binding sites in human stromelysin-1: stoichiometry of the catalytic domain and identification of a cysteine ligand in the proenzyme. Biochemistry 31, 4535-4540.
    • (1992) Biochemistry , vol.31 , pp. 4535-4540
    • Salowe, S.P.1    Marcy, A.I.2    Cuca, G.C.3    Smith, C.K.4    Kopka, I.E.5    Hagmann, W.K.6    Hermes, J.D.7
  • 52
    • 0030014349 scopus 로고    scopus 로고
    • Activation of human progelatinase A by collagenase and matrilysin: Activation of procollagenase by matrilysin
    • Sang, Q.A., Bodden, M.K., and Windsor, L.J. (1996). Activation of human progelatinase A by collagenase and matrilysin: Activation of procollagenase by matrilysin. J. Pro. Chem. 15, 243-253.
    • (1996) J. Pro. Chem. , vol.15 , pp. 243-253
    • Sang, Q.A.1    Bodden, M.K.2    Windsor, L.J.3
  • 53
    • 0029103394 scopus 로고
    • Proteolytic and non-proteolytic activation of human neutrophil progelatinase B
    • Sang, Q.-X., Birkedal-Hansen, H., and Van Wart, H.E. (1995). Proteolytic and non-proteolytic activation of human neutrophil progelatinase B. Biochim. Biophys. Acta 1251, 99-108.
    • (1995) Biochim. Biophys. Acta , vol.1251 , pp. 99-108
    • Sang, Q.-X.1    Birkedal-Hansen, H.2    Van Wart, H.E.3
  • 54
    • 0029932452 scopus 로고    scopus 로고
    • Characterization of structural determinants and molecular mechanisms involved in pro-stromelysin-3 activation by 4-aminophenylmercuric acetate and furin-type convertases
    • Santavicca, M., Noel, A., Angliker, H., Stoll, I., Segain, J.-P., Anglard, P., Chretien, M., Seidah, N., and Bassett, P. (1996). Characterization of structural determinants and molecular mechanisms involved in pro-stromelysin-3 activation by 4-aminophenylmercuric acetate and furin-type convertases. Biochemistry J. 315, 953-958.
    • (1996) Biochemistry J. , vol.315 , pp. 953-958
    • Santavicca, M.1    Noel, A.2    Angliker, H.3    Stoll, I.4    Segain, J.-P.5    Anglard, P.6    Chretien, M.7    Seidah, N.8    Bassett, P.9
  • 55
    • 0028291737 scopus 로고
    • A matrix metalloproteinase expressed on the surface of invasive tumour cells
    • Sato, H., Takino, T., Okada, Y., Cao, J., Shinagawa, A., Yamamoto, E., and Seiki, M. (1994). A matrix metalloproteinase expressed on the surface of invasive tumour cells. Nature 370, 61-65.
    • (1994) Nature , vol.370 , pp. 61-65
    • Sato, H.1    Takino, T.2    Okada, Y.3    Cao, J.4    Shinagawa, A.5    Yamamoto, E.6    Seiki, M.7
  • 56
    • 0030577022 scopus 로고    scopus 로고
    • Activation of a recombinant membrane type 1-matrix metalloproteinase (MT1-MMP) by furin and its interaction with tissue inhibitor of metalloproteinases (TIMP)-2
    • Sato, H., Kinoshita, T., Takino, T., Nakayama, K., and Seiki, M. (1996). Activation of a recombinant membrane type 1-matrix metalloproteinase (MT1-MMP) by furin and its interaction with tissue inhibitor of metalloproteinases (TIMP)-2. FEBS Lett. 393, 101-104.
    • (1996) FEBS Lett. , vol.393 , pp. 101-104
    • Sato, H.1    Kinoshita, T.2    Takino, T.3    Nakayama, K.4    Seiki, M.5
  • 58
    • 0029010660 scopus 로고
    • Extracellular matrix binding properties of recombinant fibronectin type II-like modules of human 72-kDa gelatinase/type IV collagenase. High affinity binding to native type I collagen but not native type IV collagen
    • Steffensen, B., Wallon, U.M., and Overall, C.M. (1995). Extracellular matrix binding properties of recombinant fibronectin type II-like modules of human 72-kDa gelatinase/type IV collagenase. High affinity binding to native type I collagen but not native type IV collagen. J. Biol. Chem. 270, 11555-11566.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11555-11566
    • Steffensen, B.1    Wallon, U.M.2    Overall, C.M.3
  • 59
    • 0024394212 scopus 로고
    • Tissue inhibitors of metalloproteinase (TIMP-2): A new member of the metalloproteinase inhibitor family
    • Stetler-Stevenson, W.G., Krutzsch, H.C., and Liotta, L.A. (1989). Tissue inhibitors of metalloproteinase (TIMP-2): a new member of the metalloproteinase inhibitor family. J. Biol. Chem. 264, 17374-17378.
    • (1989) J. Biol. Chem. , vol.264 , pp. 17374-17378
    • Stetler-Stevenson, W.G.1    Krutzsch, H.C.2    Liotta, L.A.3
  • 60
    • 0029825963 scopus 로고    scopus 로고
    • Identification and characterization of a novel collagenase in Xenopus laevis: Possible roles during frog development
    • Stolow, M., Bauzon, D.D., Li, J., Sedgwick, T., Liang, V.C.-T., Sang, Q.A., and Shi, Y. (1996). Identification and characterization of a novel collagenase in Xenopus laevis: possible roles during frog development. Mol. Biol. Cell 7, 1471-1483.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1471-1483
    • Stolow, M.1    Bauzon, D.D.2    Li, J.3    Sedgwick, T.4    Liang, V.C.-T.5    Sang, Q.A.6    Shi, Y.7
  • 61
    • 0027172634 scopus 로고
    • Plasma membrane-dependent activation of the 72-kDa type IV collagenase is prevented by complex formation with TIMP-2
    • Strongin, A.Y., Marmer, B.L., Grant, G.A., and Goldberg, G.I. (1993). Plasma membrane-dependent activation of the 72-kDa type IV collagenase is prevented by complex formation with TIMP-2. J. Biol. Chem. 268, 14033-14039.
    • (1993) J. Biol. Chem. , vol.268 , pp. 14033-14039
    • Strongin, A.Y.1    Marmer, B.L.2    Grant, G.A.3    Goldberg, G.I.4
  • 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, A.Y., Collier, I., Bannikov, G., Marmer, B.L., Grant, G.A., and Goldberg, G.I. (1995). Mechanism of cell surface activation of 72-kDa type IV collagenase. Isolation of the activated form of the membrane metalloprotease. J. Biol. Chem. 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
  • 63
    • 0025026410 scopus 로고
    • Mechanisms of activation of tissue procollagenase by matrix metalloproteinase 3 (stromelysin)
    • Suzuki, K., Enghild, J.J., Morodomi, T., Salvesen, G., and Nagase, H. (1990). Mechanisms of activation of tissue procollagenase by matrix metalloproteinase 3 (stromelysin). Biochemistry 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
  • 64
    • 0028794828 scopus 로고
    • Activation of precursors for matrix metalloproteinases 1 (interstitial collagenase) and 3 (stromelysin) by rat mast-cell proteinases I and II
    • Suzuki, K., Lees, M., Newlands, G.F.J., Nagase, H., and Woolley, D.E. (1995). Activation of precursors for matrix metalloproteinases 1 (interstitial collagenase) and 3 (stromelysin) by rat mast-cell proteinases I and II. Biochem. J. 305, 301-306.
    • (1995) Biochem. J. , vol.305 , pp. 301-306
    • Suzuki, K.1    Lees, M.2    Newlands, G.F.J.3    Nagase, H.4    Woolley, D.E.5
  • 65
    • 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., and Seiki, M. (1995). 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. 270, 23013-23020.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23013-23020
    • Takino, T.1    Sato, H.2    Shinagawa, A.3    Seiki, M.4
  • 66
    • 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, H.E., and Birkedal-Hansen, H. (1990). 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 87, 5578-5582.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 5578-5582
    • Van Wart, H.E.1    Birkedal-Hansen, H.2
  • 67
    • 0025831950 scopus 로고
    • Tissue inhibitor of metalloproteinases-2 inhibits the activation of 72 kDa progelatinase by fibroblast membranes
    • Ward, R.V., Atkinson, S.J., Slocombe, P.M., Docherty, A.J.P., Reynolds, J.J., and Murphy, G. (1991a). Tissue inhibitor of metalloproteinases-2 inhibits the activation of 72 kDa progelatinase by fibroblast membranes. Biochim. Biophys. Acta 1079, 242-246.
    • (1991) Biochim. Biophys. Acta , vol.1079 , pp. 242-246
    • Ward, R.V.1    Atkinson, S.J.2    Slocombe, P.M.3    Docherty, A.J.P.4    Reynolds, J.J.5    Murphy, G.6
  • 68
    • 0025834914 scopus 로고
    • The purification of tissue inhibitor of metalloproteinases-2 from its 72 kDa progelatinase complex
    • Ward, R.V., Hembry, R.H., Reynolds, J.J., and Murphy, G. (1991b). The purification of tissue inhibitor of metalloproteinases-2 from its 72 kDa progelatinase complex. Biochem. J. 278, 179-187.
    • (1991) Biochem. J. , vol.278 , pp. 179-187
    • Ward, R.V.1    Hembry, R.H.2    Reynolds, J.J.3    Murphy, G.4
  • 69
    • 0028077527 scopus 로고
    • Cell surface-mediated activation of progelatinase A: Demonstration of the involvement of the C-terminal domain of progelatinase A in cell surface binding and activation of progelatinase A by primary fibroblasts
    • Ward, R.V., Atkinson, S.J., Reynolds, J.J., and Murphy, G. (1994). Cell surface-mediated activation of progelatinase A: demonstration of the involvement of the C-terminal domain of progelatinase A in cell surface binding and activation of progelatinase A by primary fibroblasts. Biochem. J. 304, 263-269.
    • (1994) Biochem. J. , vol.304 , pp. 263-269
    • Ward, R.V.1    Atkinson, S.J.2    Reynolds, J.J.3    Murphy, G.4
  • 70
    • 0024330327 scopus 로고
    • SV40-transformed human lung fibroblasts secrete a 92-kDa type IV collagenase which is identical to that secreted by normal human macrophages
    • Wilhelm, S.M., Collier, I.E., Marmer, B.L., Eisen, A.Z., Grant, G.A., and Goldberg, G.I. (1989). SV40-transformed human lung fibroblasts secrete a 92-kDa type IV collagenase which is identical to that secreted by normal human macrophages. J. Biol. Chem. 264, 17213-17221.
    • (1989) J. Biol. Chem. , vol.264 , pp. 17213-17221
    • Wilhelm, S.M.1    Collier, I.E.2    Marmer, B.L.3    Eisen, A.Z.4    Grant, G.A.5    Goldberg, G.I.6
  • 71
    • 0029133344 scopus 로고
    • cDNA sequence and mRNA tissue distribution of a novel human matrix metalloproteinase with a potential transmembrane segment
    • Will, H., and Hinzmann, B. (1995). cDNA sequence and mRNA tissue distribution of a novel human matrix metalloproteinase with a potential transmembrane segment. Eur. J. Biochem. 231, 602-608.
    • (1995) Eur. J. Biochem. , vol.231 , pp. 602-608
    • Will, H.1    Hinzmann, B.2
  • 72
    • 0030016342 scopus 로고    scopus 로고
    • The soluble catalytic domain of membrane type 1 matrix metalloproteinase cleaves the propeptide of progelatinase A and initiates autoproteolytic activation. Regulation by TIMP-2 and TIMP-3
    • Will, H., Atkinson, S.J., Butler, G.S., Smith, B., and Murphy, G. (1996). The soluble catalytic domain of membrane type 1 matrix metalloproteinase cleaves the propeptide of progelatinase A and initiates autoproteolytic activation. Regulation by TIMP-2 and TIMP-3. J. Biol. Chem. 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
  • 73
    • 0028625739 scopus 로고
    • The family of matrix metalloproteinases
    • Woessner, J.F., Jr. (1994). The family of matrix metalloproteinases. Ann. N.Y. Acad. Sci. 732, 11-21.
    • (1994) Ann. N.Y. Acad. Sci. , vol.732 , pp. 11-21
    • Woessner Jr., J.F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.