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Volumn 335, Issue 1-2, 2003, Pages 49-57

An ELISA for the detection of TIMP-1 based on recombinant single chain Fv fusion proteins

Author keywords

Alkaline phosphatase; ELISA; Fusion protein; Phage display; Single chain Fv; TIMP 1

Indexed keywords

SINGLE CHAIN FRAGMENT VARIABLE ANTIBODY; TISSUE INHIBITOR OF METALLOPROTEINASE 1;

EID: 0242285710     PISSN: 00098981     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0009-8981(03)00281-X     Document Type: Article
Times cited : (3)

References (32)
  • 1
    • 0025230509 scopus 로고
    • Metalloproteinases and their inhibitors in matrix remodeling
    • Matrisian L.M. Metalloproteinases and their inhibitors in matrix remodeling. Trends Genet. 6:1990;121-125.
    • (1990) Trends Genet. , vol.6 , pp. 121-125
    • Matrisian, L.M.1
  • 2
    • 0029022713 scopus 로고
    • Tissue inhibitors of matrix metalloendopeptidases
    • Murphy G., Willenbrock F. Tissue inhibitors of matrix metalloendopeptidases. Methods Enzymol. 248:1995;496-510.
    • (1995) Methods Enzymol. , vol.248 , pp. 496-510
    • Murphy, G.1    Willenbrock, F.2
  • 3
    • 0019195010 scopus 로고
    • Metastatic potential correlates with enzymatic degradation of basement membrane collagen
    • Liotta L.A., Tryggvason K., Garbisa S., Hart I., Foltz C.M., Shafie S. Metastatic potential correlates with enzymatic degradation of basement membrane collagen. Nature. 284:1980;67-68.
    • (1980) Nature , vol.284 , pp. 67-68
    • Liotta, L.A.1    Tryggvason, K.2    Garbisa, S.3    Hart, I.4    Foltz, C.M.5    Shafie, S.6
  • 4
    • 0023270938 scopus 로고
    • Degradation of basement membrane type IV collagen and lung subendothelial matrix by rat mammary adenocarcinoma cell clones of differing metastatic potentials
    • Nakajima M., Welch D.R., Belloni P.N., Nicolson G.L. Degradation of basement membrane type IV collagen and lung subendothelial matrix by rat mammary adenocarcinoma cell clones of differing metastatic potentials. Cancer Res. 47:1987;4869-4876.
    • (1987) Cancer Res. , vol.47 , pp. 4869-4876
    • Nakajima, M.1    Welch, D.R.2    Belloni, P.N.3    Nicolson, G.L.4
  • 5
    • 0024421549 scopus 로고
    • Metalloproteinases and cancer invasion and metastasis
    • Murphy G., Reynolds J.J., Hembry R.M. Metalloproteinases and cancer invasion and metastasis. Int. J. Cancer. 44:1989;757-760.
    • (1989) Int. J. Cancer , vol.44 , pp. 757-760
    • Murphy, G.1    Reynolds, J.J.2    Hembry, R.M.3
  • 6
    • 0027140406 scopus 로고
    • Extracellular matrix 6: Role of matrix metalloproteinases in tumor invasion and metastasis
    • Stetler-Stevenson W.G., Liotta L.A., Kleiner D.E. Jr. Extracellular matrix 6: role of matrix metalloproteinases in tumor invasion and metastasis. FASEB J. 7:1993;1434-1441.
    • (1993) FASEB J. , vol.7 , pp. 1434-1441
    • Stetler-Stevenson, W.G.1    Liotta, L.A.2    Kleiner D.E., Jr.3
  • 7
    • 0030806173 scopus 로고    scopus 로고
    • Changing views of the role of matrix metalloproteinases in metastasis
    • Chambers A.F., Matrisian L.M. Changing views of the role of matrix metalloproteinases in metastasis. J. Natl. Cancer Inst. 89:1997;1260-1270.
    • (1997) J. Natl. Cancer Inst. , vol.89 , pp. 1260-1270
    • Chambers, A.F.1    Matrisian, L.M.2
  • 8
    • 0029113115 scopus 로고
    • MMP-9 (gelatinase B) mRNA is expressed during mouse neurogenesis and may be associated with vascularization
    • Canete Soler R., Gui Y.H., Linask K.K., Muschel R.J. MMP-9 (gelatinase B) mRNA is expressed during mouse neurogenesis and may be associated with vascularization. Brain Res. Dev. Brain Res. 88:1995;37-52.
    • (1995) Brain Res. Dev. Brain Res. , vol.88 , pp. 37-52
    • Canete Soler, R.1    Gui, Y.H.2    Linask, K.K.3    Muschel, R.J.4
  • 9
    • 0346963598 scopus 로고    scopus 로고
    • MMP-9/gelatinase B is a key regulator of growth plate angiogenesis and apoptosis of hypertrophic chondrocytes
    • Vu T.H., Shipley J.M., Bergers G., Berger J.E., Helms J.A., Hanahan D.et al. MMP-9/gelatinase B is a key regulator of growth plate angiogenesis and apoptosis of hypertrophic chondrocytes. Cell. 93:1998;411-422.
    • (1998) Cell , vol.93 , pp. 411-422
    • Vu, T.H.1    Shipley, J.M.2    Bergers, G.3    Berger, J.E.4    Helms, J.A.5    Hanahan, D.6
  • 10
    • 0020601072 scopus 로고
    • Production of collagenase and inhibitor (TIMP) by intracranial tumors and dura in vitro
    • Halaka A.N., Bunning R.A., Bird C.C., Gibson M., Reynolds J.J. Production of collagenase and inhibitor (TIMP) by intracranial tumors and dura in vitro. J. Neurosurg. 59:1983;461-466.
    • (1983) J. Neurosurg. , vol.59 , pp. 461-466
    • Halaka, A.N.1    Bunning, R.A.2    Bird, C.C.3    Gibson, M.4    Reynolds, J.J.5
  • 11
    • 0021280626 scopus 로고
    • A fibrosarcoma model derived from mouse embryo cells: Growth properties and secretion of collagenase and metalloproteinase inhibitor (TIMP) by tumour cell lines
    • Hicks N.J., Ward R.V., Reynolds J.J. A fibrosarcoma model derived from mouse embryo cells: growth properties and secretion of collagenase and metalloproteinase inhibitor (TIMP) by tumour cell lines. Int. J. Cancer. 33:1984;835-844.
    • (1984) Int. J. Cancer , vol.33 , pp. 835-844
    • Hicks, N.J.1    Ward, R.V.2    Reynolds, J.J.3
  • 12
    • 0034296445 scopus 로고    scopus 로고
    • Expression of matrix metalloproteinases (MMP-2, MMP-9, MT1-MMP) and their inhibitors (TIMP-1, TIMP-2) in common epithelial tumors of the ovary
    • Sakata K., Shigemasa K., Nagai N., Ohama K. Expression of matrix metalloproteinases (MMP-2, MMP-9, MT1-MMP) and their inhibitors (TIMP-1, TIMP-2) in common epithelial tumors of the ovary. Int. J. Oncol. 17:2000;673-681.
    • (2000) Int. J. Oncol. , vol.17 , pp. 673-681
    • Sakata, K.1    Shigemasa, K.2    Nagai, N.3    Ohama, K.4
  • 13
    • 0032895321 scopus 로고    scopus 로고
    • Expression of collagenases-1 and -3 and their inhibitors TIMP-1 and -3 correlates with the level of invasion in malignant melanomas
    • Airola K., Karonen T., Vaalamo M., Lehti K., Lohi J., Kariniemi A.L.et al. Expression of collagenases-1 and -3 and their inhibitors TIMP-1 and -3 correlates with the level of invasion in malignant melanomas. Br. J. Cancer. 80:1999;733-743.
    • (1999) Br. J. Cancer , vol.80 , pp. 733-743
    • Airola, K.1    Karonen, T.2    Vaalamo, M.3    Lehti, K.4    Lohi, J.5    Kariniemi, A.L.6
  • 14
    • 0028130051 scopus 로고
    • Serum metalloproteinases and their inhibitors: Markers for malignant potential
    • Baker T., Tickle S., Wasan H., Docherty A., Isenberg D., Waxman J. Serum metalloproteinases and their inhibitors: markers for malignant potential. Br. J. Cancer. 70:1994;506-512.
    • (1994) Br. J. Cancer , vol.70 , pp. 506-512
    • Baker, T.1    Tickle, S.2    Wasan, H.3    Docherty, A.4    Isenberg, D.5    Waxman, J.6
  • 16
    • 0025057488 scopus 로고
    • Rapid one-step sandwich enzyme immunoassay for tissue inhibitor of metalloproteinases. An application for rheumatoid arthritis serum and plasma
    • Kodama S., Iwata K., Iwata H., Yamashita K., Hayakawa T. Rapid one-step sandwich enzyme immunoassay for tissue inhibitor of metalloproteinases. An application for rheumatoid arthritis serum and plasma. J. Immunol. Methods. 127:1990;103-108.
    • (1990) J. Immunol. Methods , vol.127 , pp. 103-108
    • Kodama, S.1    Iwata, K.2    Iwata, H.3    Yamashita, K.4    Hayakawa, T.5
  • 17
    • 0025001756 scopus 로고
    • Immunoassays for the detection of human collagenase, stromelysin, tissue inhibitor of metalloproteinases (TIMP) and enzyme-inhibitor complexes
    • Cooksley S., Hipkiss J.B., Tickle S.P., Holmes-Ievers E., Docherty A.J., Murphy G.et al. Immunoassays for the detection of human collagenase, stromelysin, tissue inhibitor of metalloproteinases (TIMP) and enzyme-inhibitor complexes. Matrix. 10:1990;285-291.
    • (1990) Matrix , vol.10 , pp. 285-291
    • Cooksley, S.1    Hipkiss, J.B.2    Tickle, S.P.3    Holmes-Ievers, E.4    Docherty, A.J.5    Murphy, G.6
  • 18
    • 0025827840 scopus 로고
    • Polyclonal and monoclonal antibodies against human tissue inhibitor of metalloproteinases (TIMP) and the design of an enzyme-linked immunosorbent assay to measure TIMP
    • Clark I.M., Powell L.K., Wright J.K., Cawston T.E. Polyclonal and monoclonal antibodies against human tissue inhibitor of metalloproteinases (TIMP) and the design of an enzyme-linked immunosorbent assay to measure TIMP. Matrix. 11:1991;76-85.
    • (1991) Matrix , vol.11 , pp. 76-85
    • Clark, I.M.1    Powell, L.K.2    Wright, J.K.3    Cawston, T.E.4
  • 19
    • 0028837706 scopus 로고
    • Development of an enzyme-linked immunosorbent assay to measure total TIMP-1 (free TIMP-1 and TIMP-1 in combination with matrix-metalloproteinases) and measurement of TIMP 1 and CRP in serum
    • Plumpton T.A., Clark I.M., Plumpton C., Calvin J., Cawston T.E. Development of an enzyme-linked immunosorbent assay to measure total TIMP-1 (free TIMP-1 and TIMP-1 in combination with matrix-metalloproteinases) and measurement of TIMP 1 and CRP in serum. Clin. Chim. Acta. 240:1995;137-154.
    • (1995) Clin. Chim. Acta , vol.240 , pp. 137-154
    • Plumpton, T.A.1    Clark, I.M.2    Plumpton, C.3    Calvin, J.4    Cawston, T.E.5
  • 20
    • 0025944065 scopus 로고
    • The N-terminal domain of tissue inhibitor of metalloproteinases retains metalloproteinase inhibitory activity
    • Murphy G., Houbrechts A., Cockett M.I., Williamson R.A., O'Shea M., Docherty A.J. The N-terminal domain of tissue inhibitor of metalloproteinases retains metalloproteinase inhibitory activity. Biochemistry. 30:1991;8097-8102.
    • (1991) Biochemistry , vol.30 , pp. 8097-8102
    • Murphy, G.1    Houbrechts, A.2    Cockett, M.I.3    Williamson, R.A.4    O'Shea, M.5    Docherty, A.J.6
  • 21
    • 13144261717 scopus 로고    scopus 로고
    • Efficient construction of a large nonimmune phage antibody library: The production of high-affinity human single-chain antibodies to protein antigens
    • Sheets M.D., Amersdorfer P., Finnern R., Sargent P., Lindquist E., Schier R.et al. Efficient construction of a large nonimmune phage antibody library: the production of high-affinity human single-chain antibodies to protein antigens. Proc. Natl. Acad. Sci. U. S. A. 95:1998;6157-6162.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 6157-6162
    • Sheets, M.D.1    Amersdorfer, P.2    Finnern, R.3    Sargent, P.4    Lindquist, E.5    Schier, R.6
  • 22
    • 0037212887 scopus 로고    scopus 로고
    • Expression of TIMP-1 in Pichia pastoris. Selection of an anti-TIMP-1 specific single-chain Fv antibody from a large non-immune library
    • Wozniak G., Obermayr E., Jeras M., Knezevic M., Rüker F. Expression of TIMP-1 in Pichia pastoris. Selection of an anti-TIMP-1 specific single-chain Fv antibody from a large non-immune library. Clin. Chim. Acta. 327:2003;171-179.
    • (2003) Clin. Chim. Acta , vol.327 , pp. 171-179
    • Wozniak, G.1    Obermayr, E.2    Jeras, M.3    Knezevic, M.4    Rüker, F.5
  • 23
    • 0031194670 scopus 로고    scopus 로고
    • Single-chain Fv fusion proteins suitable as coating and detecting reagents in a double antibody sandwich enzyme-linked immunosorbent assay
    • Kerschbaumer R.J., Hirschl S., Kaufmann A., Ibl M., Koenig R., Himmler G. Single-chain Fv fusion proteins suitable as coating and detecting reagents in a double antibody sandwich enzyme-linked immunosorbent assay. Anal. Biochem. 249:1997;219-227.
    • (1997) Anal. Biochem. , vol.249 , pp. 219-227
    • Kerschbaumer, R.J.1    Hirschl, S.2    Kaufmann, A.3    Ibl, M.4    Koenig, R.5    Himmler, G.6
  • 24
    • 0026044557 scopus 로고
    • Mutagenesis of conserved residues within the active site of Escherichia coli alkaline phosphatase yields enzymes with increased kcat
    • Mandecki W., Shallcross M.A., Sowadski J., Tomazic-Allen S. Mutagenesis of conserved residues within the active site of Escherichia coli alkaline phosphatase yields enzymes with increased kcat. Protein Eng. 4:1991;801-804.
    • (1991) Protein Eng. , vol.4 , pp. 801-804
    • Mandecki, W.1    Shallcross, M.A.2    Sowadski, J.3    Tomazic-Allen, S.4
  • 25
    • 0031022084 scopus 로고    scopus 로고
    • High level production of soluble single chain antibodies in small-scale Escherichia coli cultures
    • Kipriyanov S.M., Moldenhauer G., Little M. High level production of soluble single chain antibodies in small-scale Escherichia coli cultures. J. Immunol. Methods. 200:1997;69-77.
    • (1997) J. Immunol. Methods , vol.200 , pp. 69-77
    • Kipriyanov, S.M.1    Moldenhauer, G.2    Little, M.3
  • 27
    • 14744267241 scopus 로고
    • The functional expression of antibody Fv fragments in Escherichia coli: Improved vectors and a generally applicable purification technique
    • Skerra A., Pfitzinger I., Pluckthun A. The functional expression of antibody Fv fragments in Escherichia coli: improved vectors and a generally applicable purification technique. Biotechnology (NY). 9:1991;273-278.
    • (1991) Biotechnology (NY) , vol.9 , pp. 273-278
    • Skerra, A.1    Pfitzinger, I.2    Pluckthun, A.3
  • 29
    • 0022340978 scopus 로고
    • Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product
    • Evan G.I., Lewis G.K., Ramsay G., Bishop J.M. Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product. Mol. Cell Biol. 5:1985;3610-3616.
    • (1985) Mol. Cell Biol. , vol.5 , pp. 3610-3616
    • Evan, G.I.1    Lewis, G.K.2    Ramsay, G.3    Bishop, J.M.4
  • 30
    • 0026528230 scopus 로고
    • Miniantibodies: Use of amphipathic helices to produce functional, flexibly linked dimeric FV fragments with high avidity in Escherichia coli
    • Pack P., Pluckthun A. Miniantibodies: use of amphipathic helices to produce functional, flexibly linked dimeric FV fragments with high avidity in Escherichia coli. Biochemistry. 31:1992;1579-1584.
    • (1992) Biochemistry , vol.31 , pp. 1579-1584
    • Pack, P.1    Pluckthun, A.2
  • 31
    • 0029294084 scopus 로고
    • In vitro and in vivo characterization of a human anti-c-erbB-2 single-chain Fv isolated from a filamentous phage antibody library
    • Schier R., Marks J.D., Wolf E.J., Apell G., Wong C., McCartney J.E.et al. In vitro and in vivo characterization of a human anti-c-erbB-2 single-chain Fv isolated from a filamentous phage antibody library. Immunotechnology. 1:1995;73-81.
    • (1995) Immunotechnology , vol.1 , pp. 73-81
    • Schier, R.1    Marks, J.D.2    Wolf, E.J.3    Apell, G.4    Wong, C.5    McCartney, J.E.6
  • 32
    • 0028175749 scopus 로고
    • Two-step cloning of antibody variable domains in a phage display vector
    • Engelhardt O., Grabherr R., Himmler G., Rüker F. Two-step cloning of antibody variable domains in a phage display vector. Biotechniques. 17:1994;44-46.
    • (1994) Biotechniques , vol.17 , pp. 44-46
    • Engelhardt, O.1    Grabherr, R.2    Himmler, G.3    Rüker, F.4


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