메뉴 건너뛰기




Volumn 379, Issue 2, 1998, Pages 185-191

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)

Author keywords

Extracellular matrix; Stromelysin; TIMP; Zymogen activation

Indexed keywords

CALCIUM ION; METALLOPROTEINASE; STROMELYSIN; TISSUE INHIBITOR OF METALLOPROTEINASE; ZINC ION;

EID: 0031883960     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/bchm.1998.379.2.185     Document Type: Article
Times cited : (51)

References (35)
  • 2
    • 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., Buttice, 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    Buttice, G.2    Nagase, H.3    Kurkinen, M.4
  • 3
    • 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
  • 4
    • 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
  • 5
    • 0028556638 scopus 로고
    • Reciprocated matrix metalloproteinases activation: A process performed by interstitial collagenase and progelatinase A
    • Crabbe, T., O'Connell, J., Smith, B.J., and Docherty, A.J.P. (1994). Reciprocated matrix metalloproteinases 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
  • 6
    • 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
  • 7
    • 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
  • 8
    • 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
  • 9
    • 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
  • 10
    • 0027516637 scopus 로고
    • Recombinant Chinese hamster ovary cell matrix metalloprotease-3 (MMP-3, stromelysin-1). Role of calcium in promatrix metalloprotease-3 (pro-MMP-3, prostromelysin-1) activation and thermostability of the low mass catalytic domain of MMP-3
    • Housley, T.J., Baumann, A.P., Braun, I.D., Davis, G., Seperack, P.K., and Wilhelm, S.M. (1993). Recombinant Chinese hamster ovary cell matrix metalloprotease-3 (MMP-3, stromelysin-1). Role of calcium in promatrix metalloprotease-3 (pro-MMP-3, prostromelysin-1) activation and thermostability of the low mass catalytic domain of MMP-3. J. Biol. Chem. 268, 4481-4487.
    • (1993) J. Biol. Chem. , vol.268 , pp. 4481-4487
    • Housley, T.J.1    Baumann, A.P.2    Braun, I.D.3    Davis, G.4    Seperack, P.K.5    Wilhelm, S.M.6
  • 11
    • 0029876136 scopus 로고    scopus 로고
    • Folding and characterization of the amino-terminal domain of human tissue inhibitor of metalloproteinases-1 (TIMP-1) expressed at high yield in e coli
    • Huang, W., Suzuki, K., Nagase, H., Arumugam, S., Van Doren, S.R., and Brew, K. (1996). Folding and characterization of the amino-terminal domain of human tissue inhibitor of metalloproteinases-1 (TIMP-1) expressed at high yield in E coli. FEBS Lett. 384, 155-161.
    • (1996) FEBS Lett. , vol.384 , pp. 155-161
    • Huang, W.1    Suzuki, K.2    Nagase, H.3    Arumugam, S.4    Van Doren, S.R.5    Brew, K.6
  • 12
    • 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., Nakanashi, 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    Nakanashi, I.3    Ohuchi, E.4    Fujii, Y.5    Nakai, N.6    Okada, Y.7
  • 13
    • 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-aminophyenylmercuric 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-aminophyenylmercuric acetate. Biochem. J. 308, 645-651.
    • (1995) Biochem. J. , vol.308 , pp. 645-651
    • Itoh, Y.1    Binner, S.2    Nagase, H.3
  • 14
    • 0026494632 scopus 로고
    • Heterologous expression and purification of active human phosphoribosylglycinamide formyl-transferase as a single domain
    • Kan, C.C., Gehring, M.R., Nodes, B.R., Janson, C.A., Almassy, R.J., and Hostomska, Z. (1992). Heterologous expression and purification of active human phosphoribosylglycinamide formyl-transferase as a single domain. J. Protein Chem. 11, 467-473.
    • (1992) J. Protein Chem. , vol.11 , pp. 467-473
    • Kan, C.C.1    Gehring, M.R.2    Nodes, B.R.3    Janson, C.A.4    Almassy, R.J.5    Hostomska, Z.6
  • 15
    • 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
  • 16
    • 0023664635 scopus 로고
    • Sequence from picomole quantities of proteins electroblotted onto polyvinylidene dif luoride membranes
    • Matsudaira, P. (1987). Sequence from picomole quantities of proteins electroblotted onto polyvinylidene dif luoride membranes. J. Biol. Chem. 262, 10035-10038.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10035-10038
    • Matsudaira, P.1
  • 17
    • 0029022713 scopus 로고
    • Tissue inhibitors of matrix metalloendopeptidases
    • Murphy, G., and Willenbrock, F. (1995). Tissue inhibitors of matrix metalloendopeptidases. Methods Enzymol. 248, 496-510.
    • (1995) Methods Enzymol. , vol.248 , pp. 496-510
    • Murphy, G.1    Willenbrock, F.2
  • 18
    • 0029006135 scopus 로고
    • Human stromelysin 1 and 2
    • Nagase, H. (1995). Human stromelysin 1 and 2. Methods Enzymol. 248, 449-470.
    • (1995) Methods Enzymol. , vol.248 , pp. 449-470
    • Nagase, H.1
  • 19
    • 0000736684 scopus 로고    scopus 로고
    • Matrix metalloproteinases
    • N.M. Hooper, ed. (London, England: Taylor and Francis)
    • Nagase, H. (1996). Matrix metalloproteinases. In: Zinc Metalloproteases in Health and Disease, N.M. Hooper, ed. (London, England: Taylor and Francis), pp. 153-204.
    • (1996) Zinc Metalloproteases in Health and Disease , pp. 153-204
    • Nagase, H.1
  • 20
    • 0030957218 scopus 로고    scopus 로고
    • Activation mechanisms of matrix metalloproteinases
    • Nagase, H. (1997). Activation mechanisms of matrix metalloproteinases. Biol. Chem. 378, 151-160.
    • (1997) Biol. Chem. , vol.378 , pp. 151-160
    • Nagase, H.1
  • 21
    • 0025335183 scopus 로고
    • Stepwise activation 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 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
  • 22
    • 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
  • 23
    • 0023024460 scopus 로고
    • A metalloproteinase from human rheumatoid synovial fibroblasts that digests connective tissue matrix components. Purification and characterization
    • Okada, Y., Nagase, H., and Harris, E.D., Jr. (1986). A metalloproteinase from human rheumatoid synovial fibroblasts that digests connective tissue matrix components. Purification and characterization. J. Biol. Chem. 261, 14245-14255.
    • (1986) J. Biol. Chem. , vol.261 , pp. 14245-14255
    • Okada, Y.1    Nagase, H.2    Harris Jr., E.D.3
  • 24
    • 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., 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. 254, 731-741.
    • (1988) Biochem. , vol.254 , pp. 731-741
    • Okada, Y.1    Harris Jr., E.D.2    Nagase, H.3
  • 25
    • 0018416496 scopus 로고
    • Ellman's Reagent: 5,5′-Dithiobis(2-nitrobenzoic acid)-a reexamination
    • Riddles, P.W., Blakeley, R.L., and Zerner, B. (1979). Ellman's Reagent: 5,5′-Dithiobis(2-nitrobenzoic acid)-a reexamination. Anal. Biochem. 94, 75-81.
    • (1979) Anal. Biochem. , vol.94 , pp. 75-81
    • Riddles, P.W.1    Blakeley, R.L.2    Zerner, B.3
  • 26
    • 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
  • 28
    • 0023942417 scopus 로고
    • The complete primary structure of human matrix metalloproteinase-3. Identity with stromelysin
    • Saus J., Quinones, S., Otani, Y., Nagase, H., Harris, E.D., Jr., and Kurkinen, M. (1988). The complete primary structure of human matrix metalloproteinase-3. Identity with stromelysin. J. Biol. Chem. 263, 6742-6745.
    • (1988) J. Biol. Chem. , vol.263 , pp. 6742-6745
    • Saus, J.1    Quinones, S.2    Otani, Y.3    Nagase, H.4    Harris Jr., E.D.5    Kurkinen, M.6
  • 29
    • 1842330739 scopus 로고
    • Translation of a synthetic two-cistron mRNA in Escherichia coli
    • Schoner, B.E., Belagaje, R.M., and Schoner, R.G. (1986). Translation of a synthetic two-cistron mRNA in Escherichia coli. Proc. Natl. Acad. Sci. USA 83, 8506-8510.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 8506-8510
    • Schoner, B.E.1    Belagaje, R.M.2    Schoner, R.G.3
  • 31
    • 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
  • 32
    • 0025834914 scopus 로고
    • The purification of tissue inhibitor of metalloproteinases-2 from its 72 kDa progelatinasecomplex
    • Ward, R.V., Hembry, R.H., Reynolds, J.J., and Murphy, G. (1991). The purification of tissue inhibitor of metalloproteinases-2 from its 72 kDa progelatinasecomplex. 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
  • 33
    • 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
  • 34
    • 0026447262 scopus 로고
    • Purification and characterization of the human stromelysin catalytic domain expressed in Escherichia coli
    • Ye, Q.-Z., Johnson, L.L., Hupe, D.J., and Baragi, V. (1992). Purification and characterization of the human stromelysin catalytic domain expressed in Escherichia coli. Biochemistry 31, 11231-11235.
    • (1992) Biochemistry , vol.31 , pp. 11231-11235
    • Ye, Q.-Z.1    Johnson, L.L.2    Hupe, D.J.3    Baragi, V.4
  • 35
    • 0024409494 scopus 로고
    • Pro-sequence of subtilisin can guide the refolding of denatured subtilisin in an intermolecular process
    • Zhu, X.L., Ohta, Y., Jordan, F.,and Inouye, M. (1989). Pro-sequence of subtilisin can guide the refolding of denatured subtilisin in an intermolecular process. Nature 339, 483-484.
    • (1989) Nature , vol.339 , pp. 483-484
    • Zhu, X.L.1    Ohta, Y.2    Jordan, F.3    Inouye, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.