메뉴 건너뛰기




Volumn 157, Issue 1, 2012, Pages 20-24

Expression of soluble and functional full-length human matrix metalloproteinase-2 in Escherichia coli

Author keywords

Bacteria; Escherichia coli; Gelatinase A; Matrix metalloproteinase 2; Protein expression

Indexed keywords

BIOLOGICAL ACTIVITIES; E. COLI; EUKARYOTIC PROTEINS; EUKARYOTIC TISSUE; FLUORIMETRIC ASSAYS; GELATINASE-A; HUMAN MATRIX; MATRIX METALLOPROTEINASE-2; METALLOPROTEINASES; MMP INHIBITOR; PROTEIN EXPRESSION; SOLUBLE FRACTION; WESTERN BLOTTING;

EID: 84855232393     PISSN: 01681656     EISSN: 18734863     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2011.09.030     Document Type: Article
Times cited : (25)

References (32)
  • 1
    • 78549277458 scopus 로고    scopus 로고
    • Titin is a target of matrix metalloproteinase-2: implications in myocardial ischemia/reperfusion njury
    • Ali M.A., Cho W.J., Hudson B., Kassiri Z., Granzier H., Schulz R. Titin is a target of matrix metalloproteinase-2: implications in myocardial ischemia/reperfusion njury. Circulation 2010, 122:2039-2047.
    • (2010) Circulation , vol.122 , pp. 2039-2047
    • Ali, M.A.1    Cho, W.J.2    Hudson, B.3    Kassiri, Z.4    Granzier, H.5    Schulz, R.6
  • 3
    • 8344256552 scopus 로고    scopus 로고
    • Recombinant protein folding and misfolding in Escherichia coli
    • Baneyx F., Mujacic M. Recombinant protein folding and misfolding in Escherichia coli. Nat. Biotechnol. 2004, 22:1399-1408.
    • (2004) Nat. Biotechnol. , vol.22 , pp. 1399-1408
    • Baneyx, F.1    Mujacic, M.2
  • 4
    • 0028326269 scopus 로고
    • The gelatin-binding site of human 72kDa type IV collagenase (gelatinase A)
    • Banyai L., Tordai H., Patthy L. The gelatin-binding site of human 72kDa type IV collagenase (gelatinase A). Biochem. J 1994, 298(Pt 2):403-407.
    • (1994) Biochem. J , vol.298 , Issue.PART 2 , pp. 403-407
    • Banyai, L.1    Tordai, H.2    Patthy, L.3
  • 5
    • 71549172508 scopus 로고    scopus 로고
    • Refolding solubilized inclusion body proteins
    • Burgess R.R. Refolding solubilized inclusion body proteins. Methods Enzymol. 2009, 463:259-282.
    • (2009) Methods Enzymol. , vol.463 , pp. 259-282
    • Burgess, R.R.1
  • 7
    • 77950864155 scopus 로고    scopus 로고
    • Imbalance between matrix metalloproteinases and tissue inhibitor of metalloproteinases in hypertensive vascular remodeling
    • Castro M.M., Rizzi E., Prado C.M., Rossi M.A., Tanus-Santos J.E., Gerlach R.F. Imbalance between matrix metalloproteinases and tissue inhibitor of metalloproteinases in hypertensive vascular remodeling. Matrix Biol. 2010, 29:194-201.
    • (2010) Matrix Biol. , vol.29 , pp. 194-201
    • Castro, M.M.1    Rizzi, E.2    Prado, C.M.3    Rossi, M.A.4    Tanus-Santos, J.E.5    Gerlach, R.F.6
  • 8
    • 0025728412 scopus 로고
    • Isolation and characterization of a 70-kDa metalloprotease (gelatinase) that is elevated in Rous sarcoma virus-transformed chicken embryo fibroblasts
    • Chen J.M., Aimes R.T., Ward G.R., Youngleib G.L., Quigley J.P. Isolation and characterization of a 70-kDa metalloprotease (gelatinase) that is elevated in Rous sarcoma virus-transformed chicken embryo fibroblasts. J. Biol. Chem. 1991, 266:5113-5121.
    • (1991) J. Biol. Chem. , vol.266 , pp. 5113-5121
    • Chen, J.M.1    Aimes, R.T.2    Ward, G.R.3    Youngleib, G.L.4    Quigley, J.P.5
  • 9
    • 0042284093 scopus 로고    scopus 로고
    • Purification and characterization of catalytic domains of gelatinase A with or without fibronectin insert for high-throughput inhibitor screening
    • Cheng D., Shen Q., Nan F., Qian Z., Ye Q.Z. Purification and characterization of catalytic domains of gelatinase A with or without fibronectin insert for high-throughput inhibitor screening. Protein Expr. Purif. 2003, 27:63-74.
    • (2003) Protein Expr. Purif. , vol.27 , pp. 63-74
    • Cheng, D.1    Shen, Q.2    Nan, F.3    Qian, Z.4    Ye, Q.Z.5
  • 10
    • 0032719798 scopus 로고    scopus 로고
    • Vascular matrix metalloproteinase-2 cleaves big endothelin-1 yielding a novel vasoconstrictor
    • Fernandez-Patron C., Radomski M.W., Davidge S.T. Vascular matrix metalloproteinase-2 cleaves big endothelin-1 yielding a novel vasoconstrictor. Circ. Res. 1999, 85:906-911.
    • (1999) Circ. Res. , vol.85 , pp. 906-911
    • Fernandez-Patron, C.1    Radomski, M.W.2    Davidge, S.T.3
  • 11
    • 0026753677 scopus 로고
    • Domain structure of human 72-kDa gelatinase/type IV collagenase. Characterization of proteolytic activity and identification of the tissue inhibitor of metalloproteinase-2 (TIMP-2) binding regions
    • Fridman R., Fuerst T.R., Bird R.E., Hoyhtya M., Oelkuct M., Kraus S., Komarek D., Liotta L.A., Berman M.L., Stetler-Stevenson W.G. Domain structure of human 72-kDa gelatinase/type IV collagenase. Characterization of proteolytic activity and identification of the tissue inhibitor of metalloproteinase-2 (TIMP-2) binding regions. J. Biol. Chem. 1992, 267:15398-15405.
    • (1992) J. Biol. Chem. , vol.267 , pp. 15398-15405
    • Fridman, R.1    Fuerst, T.R.2    Bird, R.E.3    Hoyhtya, M.4    Oelkuct, M.5    Kraus, S.6    Komarek, D.7    Liotta, L.A.8    Berman, M.L.9    Stetler-Stevenson, W.G.10
  • 13
    • 0032518307 scopus 로고    scopus 로고
    • Calmodulin antagonists increase the expression of membrane-type-1 matrix metalloproteinase in human uterine cervical fibroblasts
    • Ito A., Yamada M., Sato T., Sanekata K., Sato H., Seiki M., Nagase H., Mori Y. Calmodulin antagonists increase the expression of membrane-type-1 matrix metalloproteinase in human uterine cervical fibroblasts. Eur. J. Biochem. 1998, 251:353-358.
    • (1998) Eur. J. Biochem. , vol.251 , pp. 353-358
    • Ito, A.1    Yamada, M.2    Sato, T.3    Sanekata, K.4    Sato, H.5    Seiki, M.6    Nagase, H.7    Mori, Y.8
  • 14
    • 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., Nagase H. 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. 1995, 308(Pt 2):645-651.
    • (1995) Biochem. J. , vol.308 , Issue.PART 2 , pp. 645-651
    • Itoh, Y.1    Binner, S.2    Nagase, H.3
  • 15
    • 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 J.A., Schulze C.J., Wang W., Leon H., Sariahmetoglu M., Sung M., Sawicka J., Sims D.E., 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
    • 0026736594 scopus 로고
    • Purification and characterization of matrix metalloproteinase 9 from U937 monocytic leukaemia and HT1080 fibrosarcoma cells
    • Morodomi T., Ogata Y., Sasaguri Y., Morimatsu M., Nagase H. Purification and characterization of matrix metalloproteinase 9 from U937 monocytic leukaemia and HT1080 fibrosarcoma cells. Biochem. J. 1992, 285(Pt 2):603-611.
    • (1992) Biochem. J. , vol.285 , Issue.PART 2 , pp. 603-611
    • Morodomi, T.1    Ogata, Y.2    Sasaguri, Y.3    Morimatsu, M.4    Nagase, H.5
  • 17
    • 0035861560 scopus 로고    scopus 로고
    • Cellular activation of MMP-2 (gelatinase A) by MT2-MMP occurs via a TIMP-2-independent pathway
    • Morrison C.J., Butler G.S., Bigg H.F., Roberts C.R., Soloway P.D., Overall C.M. Cellular activation of MMP-2 (gelatinase A) by MT2-MMP occurs via a TIMP-2-independent pathway. J. Biol. Chem. 2001, 276:47402-47410.
    • (2001) J. Biol. Chem. , vol.276 , pp. 47402-47410
    • Morrison, C.J.1    Butler, G.S.2    Bigg, H.F.3    Roberts, C.R.4    Soloway, P.D.5    Overall, C.M.6
  • 18
    • 31344458952 scopus 로고    scopus 로고
    • Structure and function of matrix metalloproteinases and TIMPs
    • Nagase H., Visse R., Murphy G. Structure and function of matrix metalloproteinases and TIMPs. Cardiovasc. Res. 2006, 69:562-573.
    • (2006) Cardiovasc. Res. , vol.69 , pp. 562-573
    • Nagase, H.1    Visse, R.2    Murphy, G.3
  • 19
    • 33847195428 scopus 로고    scopus 로고
    • Matrix metalloproteinases and the regulation of tissue remodelling
    • Page-McCaw A., Ewald A.J., Werb Z. Matrix metalloproteinases and the regulation of tissue remodelling. Nat. Rev. Mol. Cell Biol. 2007, 8:221-233.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 221-233
    • Page-McCaw, A.1    Ewald, A.J.2    Werb, Z.3
  • 20
    • 33847115217 scopus 로고    scopus 로고
    • High-level expression of a soluble and functional fibronectin type II domain from MMP-2 in the Escherichia coli cytoplasm for solution NMR studies
    • Peisley A.A., Gooley P.R. High-level expression of a soluble and functional fibronectin type II domain from MMP-2 in the Escherichia coli cytoplasm for solution NMR studies. Protein Expr. Purif. 2007, 53:124-131.
    • (2007) Protein Expr. Purif. , vol.53 , pp. 124-131
    • Peisley, A.A.1    Gooley, P.R.2
  • 21
    • 36549085160 scopus 로고    scopus 로고
    • Control of matrix metalloproteinase catalytic activity
    • Ra H.J., Parks W.C. Control of matrix metalloproteinase catalytic activity. Matrix Biol. 2007, 26:587-596.
    • (2007) Matrix Biol. , vol.26 , pp. 587-596
    • Ra, H.J.1    Parks, W.C.2
  • 25
    • 0030946445 scopus 로고    scopus 로고
    • Release of gelatinase A during platelet activation mediates aggregation
    • Sawicki G., Salas E., Murat J., Miszta-Lane H., Radomski M.W. Release of gelatinase A during platelet activation mediates aggregation. Nature 1997, 386:616-619.
    • (1997) Nature , vol.386 , pp. 616-619
    • Sawicki, G.1    Salas, E.2    Murat, J.3    Miszta-Lane, H.4    Radomski, M.W.5
  • 27
    • 78951486815 scopus 로고    scopus 로고
    • Fragmentation of fibronectin by inherent autolytic and matrix metalloproteinase activities
    • Steffensen B., Chen Z., Pal S., Mikhailova M., Su J., Wang Y., Xu X. Fragmentation of fibronectin by inherent autolytic and matrix metalloproteinase activities. Matrix Biol. 2011, 30:34-42.
    • (2011) Matrix Biol. , vol.30 , pp. 34-42
    • Steffensen, B.1    Chen, Z.2    Pal, S.3    Mikhailova, M.4    Su, J.5    Wang, Y.6    Xu, X.7
  • 28
    • 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., Overall C.M. 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. 1995, 270:11555-11566.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11555-11566
    • Steffensen, B.1    Wallon, U.M.2    Overall, C.M.3
  • 29
    • 33747666218 scopus 로고    scopus 로고
    • Overview of bacterial expression systems for heterologous protein production: from molecular and biochemical fundamentals to commercial systems
    • Terpe K. Overview of bacterial expression systems for heterologous protein production: from molecular and biochemical fundamentals to commercial systems. Appl. Microbiol. Biotechnol. 2006, 72:211-222.
    • (2006) Appl. Microbiol. Biotechnol. , vol.72 , pp. 211-222
    • Terpe, K.1
  • 30
    • 0037693895 scopus 로고    scopus 로고
    • Matrix metalloproteinases and tissue inhibitors of metalloproteinases: structure, function, and biochemistry
    • Visse R., Nagase H. Matrix metalloproteinases and tissue inhibitors of metalloproteinases: structure, function, and biochemistry. Circ. Res. 2003, 92:827-839.
    • (2003) Circ. Res. , vol.92 , pp. 827-839
    • Visse, R.1    Nagase, H.2
  • 31
    • 77950343512 scopus 로고    scopus 로고
    • Expression of recombinant matrix metalloproteinases in Escherichia coli
    • Windsor L.J., Steele D.L. Expression of recombinant matrix metalloproteinases in Escherichia coli. Methods Mol. Biol. 2010, 622:67-81.
    • (2010) Methods Mol. Biol. , vol.622 , pp. 67-81
    • Windsor, L.J.1    Steele, D.L.2
  • 32
    • 0028914517 scopus 로고
    • Reconstructed 19kDa catalytic domain of gelatinase A is an active proteinase
    • Ye Q.Z., Johnson L.L., Yu A.E., Hupe D. Reconstructed 19kDa catalytic domain of gelatinase A is an active proteinase. Biochemistry 1995, 34:4702-4708.
    • (1995) Biochemistry , vol.34 , pp. 4702-4708
    • Ye, Q.Z.1    Johnson, L.L.2    Yu, A.E.3    Hupe, D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.