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Volumn 21, Issue 7, 2002, Pages 567-577

Following matrix metalloproteinases activity near the cell boundary by infrared micro-spectroscopy

Author keywords

Extracellular matrix; Imaging; Infrared micro spectroscopy; Matrix metalloproteinases; Pericellular

Indexed keywords

COLLAGEN; MATRIGEL; MATRIX METALLOPROTEINASE; SCLEROPROTEIN; GELATIN; LAMININ; PROTEOGLYCAN;

EID: 1842856332     PISSN: 0945053X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0945-053X(02)00089-6     Document Type: Article
Times cited : (29)

References (52)
  • 1
    • 0031908852 scopus 로고    scopus 로고
    • Structure and biological activity of the extracellular matrix
    • Aumailley M., Gayraud B. Structure and biological activity of the extracellular matrix. J. Mol. Med. 76:1998;253-265.
    • (1998) J. Mol. Med. , vol.76 , pp. 253-265
    • Aumailley, M.1    Gayraud, B.2
  • 3
    • 0027354020 scopus 로고
    • Quantitative studies of the structure of proteins in solution by Fourier-transform infrared spectroscopy
    • Arrondo J.L.R., Muga A., Cartesana J., Goñi F.M. Quantitative studies of the structure of proteins in solution by Fourier-transform infrared spectroscopy. Prog. Biophys. Mol. Biol. 59:1993;23-56.
    • (1993) Prog. Biophys. Mol. Biol. , vol.59 , pp. 23-56
    • Arrondo, J.L.R.1    Muga, A.2    Cartesana, J.3    Goñi, F.M.4
  • 4
    • 0030271595 scopus 로고    scopus 로고
    • Focalized proteolysis: Spatial and temporal regulation of extracellular matrix degradation at the cell surface
    • Basbaum C.B., Werb Z. Focalized proteolysis: spatial and temporal regulation of extracellular matrix degradation at the cell surface. Curr. Opin. Cell Biol. 8:1996;731-738.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 731-738
    • Basbaum, C.B.1    Werb, Z.2
  • 5
    • 0027996196 scopus 로고
    • Crystal and molecular structure of a collagen-like peptide at 1.9 Å resolution
    • Bella J., Eaton M., Brodsky B., Berman H.M. Crystal and molecular structure of a collagen-like peptide at 1.9 Å resolution. Science. 266:1994;75-81.
    • (1994) Science , vol.266 , pp. 75-81
    • Bella, J.1    Eaton, M.2    Brodsky, B.3    Berman, H.M.4
  • 6
    • 0034424953 scopus 로고    scopus 로고
    • Crystal Structure of a Collagen-Like Polypeptide with Repeating Sequence Pro-Hyp-Gly at 1.4 Å Resolution: Implications for Collagen Hydration
    • Berisio R., Vitagliano L., Mazzarella L., Zagari A. Crystal Structure of a Collagen-Like Polypeptide with Repeating Sequence Pro-Hyp-Gly at 1.4 Å Resolution: Implications for Collagen Hydration. Biopolymers. 56:2001;8-13.
    • (2001) Biopolymers , vol.56 , pp. 8-13
    • Berisio, R.1    Vitagliano, L.2    Mazzarella, L.3    Zagari, A.4
  • 8
    • 0029658219 scopus 로고    scopus 로고
    • Integrin α3β1 participates in the phagocytosis of extracellular matrix molecules by human breast cancer cells
    • Coopman P.J., Thomas D.M., Gehlsen K.R., Mueller S.C. Integrin α3β1 participates in the phagocytosis of extracellular matrix molecules by human breast cancer cells. Mol. Biol. Cell. 7:1996;1789-1804.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1789-1804
    • Coopman, P.J.1    Thomas, D.M.2    Gehlsen, K.R.3    Mueller, S.C.4
  • 9
    • 0030293598 scopus 로고    scopus 로고
    • Matrix metalloproteinases and the development of cancer
    • Coussens L.M., Werb Z. Matrix metalloproteinases and the development of cancer. Chem. Biol. 3:1996;895-904.
    • (1996) Chem. Biol. , vol.3 , pp. 895-904
    • Coussens, L.M.1    Werb, Z.2
  • 10
    • 0032529241 scopus 로고    scopus 로고
    • Remodeling of collagen matrix by human tumor cells requires activation and cell surface association of matrix metalloproteinase-2
    • Deryugina E.I., Bourdon M.A., Reisfeld R.A., Strongin A. Remodeling of collagen matrix by human tumor cells requires activation and cell surface association of matrix metalloproteinase-2. Can. Res. 58:1998;3743-3750.
    • (1998) Can. Res. , vol.58 , pp. 3743-3750
    • Deryugina, E.I.1    Bourdon, M.A.2    Reisfeld, R.A.3    Strongin, A.4
  • 11
    • 0035864376 scopus 로고    scopus 로고
    • MT1-MMP initiates activation of pro-MMP-2 and integrin αvβ3 promotes maturation of MMP-2 in breast carcinoma cells
    • Deryugina E.I., Ratnikov N., Monosov E., Postnova T.I., DiScipio R., Smith J.W., et al. MT1-MMP initiates activation of pro-MMP-2 and integrin αvβ3 promotes maturation of MMP-2 in breast carcinoma cells. Exp. Cell Res. 263:2001;209-223.
    • (2001) Exp. Cell Res. , vol.263 , pp. 209-223
    • Deryugina, E.I.1    Ratnikov, N.2    Monosov, E.3    Postnova, T.I.4    DiScipio, R.5    Smith, J.W.6
  • 12
    • 0000103710 scopus 로고    scopus 로고
    • The tissue inhibitors of metalloproteinase (TIMPs)
    • N.J. Clendemin, & K. Appelt. Totowa, NJ: Humana Press
    • Edwards D.R. The tissue inhibitors of metalloproteinase (TIMPs). Clendemin N.J., Appelt K. Matrix Metalloproteinase Inhibitors in Cancer Therapy. 2001;67-84 Humana Press, Totowa, NJ.
    • (2001) Matrix Metalloproteinase Inhibitors in Cancer Therapy , pp. 67-84
    • Edwards, D.R.1
  • 13
    • 0025921568 scopus 로고
    • 2O demostrates that collagen monomers undergo a conformational transition prior to thermal self-assembly in vitro
    • 2O demostrates that collagen monomers undergo a conformational transition prior to thermal self-assembly in vitro. Biochemistry. 30:1991;2372-2377.
    • (1991) Biochemistry , vol.30 , pp. 2372-2377
    • George, A.1    Veis, A.2
  • 14
    • 0035044816 scopus 로고    scopus 로고
    • Human hepatocellular carcinoma (HCC) cells require both α3β1 integrin and matrix metalloproteinases activity for migration and invasion
    • Giannelli G., Bergamini C., Fransvea E., Marinosci F., Quaranta V., Antonaci S. Human hepatocellular carcinoma (HCC) cells require both α3β1 integrin and matrix metalloproteinases activity for migration and invasion. Lab. Invest. 81:2001;613-627.
    • (2001) Lab. Invest. , vol.81 , pp. 613-627
    • Giannelli, G.1    Bergamini, C.2    Fransvea, E.3    Marinosci, F.4    Quaranta, V.5    Antonaci, S.6
  • 15
    • 0023202438 scopus 로고
    • The collagen substrate specificity of human neutrophil collagenase
    • Hasty K., Jeffrey J., Hibbs M., Welgus H. The collagen substrate specificity of human neutrophil collagenase. J. Biol. Chem. 262:1987;10048-10052.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10048-10052
    • Hasty, K.1    Jeffrey, J.2    Hibbs, M.3    Welgus, H.4
  • 16
    • 0034697144 scopus 로고    scopus 로고
    • Binding of active (57 kDa) membrane type 1-Matrix Metalloproteinase (MT1-MMP) to tissue inhibitor of metalloproteinase (TIMP)-2 regulates MT1-MMP processing and pro-MMP-2 activation
    • Hernandez-Barrantes S., Toth M., Bernardo M.M., Yurkova M., Gervasi D.C., Raz Y., et al. Binding of active (57 kDa) membrane type 1-Matrix Metalloproteinase (MT1-MMP) to tissue inhibitor of metalloproteinase (TIMP)-2 regulates MT1-MMP processing and pro-MMP-2 activation. J. Biol. Chem. 275:2000;12080-12089.
    • (2000) J. Biol. Chem. , vol.275 , pp. 12080-12089
    • Hernandez-Barrantes, S.1    Toth, M.2    Bernardo, M.M.3    Yurkova, M.4    Gervasi, D.C.5    Raz, Y.6
  • 17
    • 0034641107 scopus 로고    scopus 로고
    • Regulation of cell invasion and morphogenesis in a three-dimensional type I collagen matrix by membrane-type matrix metalloproteinases 1, 2, and 3
    • Hotary K., Allen E., Punturieri A., Yana I., Weiss S.J. Regulation of cell invasion and morphogenesis in a three-dimensional type I collagen matrix by membrane-type matrix metalloproteinases 1, 2, and 3. J. Cell Biol. 149:2000;1309-1323.
    • (2000) J. Cell Biol. , vol.149 , pp. 1309-1323
    • Hotary, K.1    Allen, E.2    Punturieri, A.3    Yana, I.4    Weiss, S.J.5
  • 18
    • 0035801473 scopus 로고    scopus 로고
    • Homophilic complex formation of MT1-MMP facilitates pro-MMP-2 activation on the cell surface and promotes tumor cell invasion
    • Itoh Y., Takamura A., Ito N., Maru Y., Sato H., Suenaga N., et al. Homophilic complex formation of MT1-MMP facilitates pro-MMP-2 activation on the cell surface and promotes tumor cell invasion. EMBO J. 20:2001;4782-4793.
    • (2001) EMBO J. , vol.20 , pp. 4782-4793
    • Itoh, Y.1    Takamura, A.2    Ito, N.3    Maru, Y.4    Sato, H.5    Suenaga, N.6
  • 19
    • 0032574844 scopus 로고    scopus 로고
    • Highly resolved chemical imaging of living cells by using synchrotron infrared microspectrometry
    • Jamin N., Dumas P., Moncuit J., Fridman W.H., Teillaud J.L., Carr G.L., et al. Highly resolved chemical imaging of living cells by using synchrotron infrared microspectrometry. Proc. Natl. Acad. Sci. USA. 95:1998;4837-4840.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 4837-4840
    • Jamin, N.1    Dumas, P.2    Moncuit, J.3    Fridman, W.H.4    Teillaud, J.L.5    Carr, G.L.6
  • 20
    • 0034683146 scopus 로고    scopus 로고
    • Use of Edman degradation sequence analysis and matrix-assisted laser desorption/ionization mass spectroscopy in designing substrates for matrix metalloproteinases
    • Lauer-Fields J.L., Nagase H., Fields G.B. Use of Edman degradation sequence analysis and matrix-assisted laser desorption/ionization mass spectroscopy in designing substrates for matrix metalloproteinases. J. Chrom. A. 890:2000a;117-125.
    • (2000) J. Chrom. A , vol.890 , pp. 117-125
    • Lauer-Fields, J.L.1    Nagase, H.2    Fields, G.B.3
  • 22
    • 0022262782 scopus 로고
    • Amide I band of IR spectrum and structure of collagen and related polypeptides
    • Lazarev Y.A., Grishkovsky B.A., Khromova T.B. Amide I band of IR spectrum and structure of collagen and related polypeptides. Biopolymers. 24:1985;1449-1478.
    • (1985) Biopolymers , vol.24 , pp. 1449-1478
    • Lazarev, Y.A.1    Grishkovsky, B.A.2    Khromova, T.B.3
  • 23
    • 15444343493 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitors: A structure-activity study
    • Levy D.E., Lapierre F., Liang W., Ye W., Lange C.W., Li X., et al. Matrix metalloproteinase inhibitors: A structure-activity study. J. Med. Chem. 41:1998;199-223.
    • (1998) J. Med. Chem. , vol.41 , pp. 199-223
    • Levy, D.E.1    Lapierre, F.2    Liang, W.3    Ye, W.4    Lange, C.W.5    Li, X.6
  • 25
    • 0032211804 scopus 로고    scopus 로고
    • ECM signaling: Orchestrating cell behaviour and misbehavior
    • Lukashev M.E., Werb Z. ECM signaling: orchestrating cell behaviour and misbehavior. Trends. Cell Biol. 8:1998;437-441.
    • (1998) Trends. Cell Biol. , vol.8 , pp. 437-441
    • Lukashev, M.E.1    Werb, Z.2
  • 26
    • 0034176764 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Multifunctional contributors of tumor progression
    • McCawley L.J., Matrisian L.M. Matrix metalloproteinases: multifunctional contributors of tumor progression. Mol. Med. Today. 6:2000;149-156.
    • (2000) Mol. Med. Today , vol.6 , pp. 149-156
    • McCawley, L.J.1    Matrisian, L.M.2
  • 27
    • 85070133481 scopus 로고    scopus 로고
    • The impact of infrared synchrotron radiation in biology: Past, present and future
    • Miller L.M., Carr G.L., Jackson M., Dumas P., Williams G.P. The impact of infrared synchrotron radiation in biology: Past, present and future. Synch. Rad. News. 13:2000a;31-37.
    • (2000) Synch. Rad. News , vol.13 , pp. 31-37
    • Miller, L.M.1    Carr, G.L.2    Jackson, M.3    Dumas, P.4    Williams, G.P.5
  • 28
    • 0038263226 scopus 로고    scopus 로고
    • Examination of bone chemical composition in osteoporosis using fluorescence-assisted infrared microspectroscopy
    • Miller L.M., Tibrewala J., Carlson C.S. Examination of bone chemical composition in osteoporosis using fluorescence-assisted infrared microspectroscopy. Cell. Mol. Biol. 46:2000b;1035-1044.
    • (2000) Cell. Mol. Biol. , vol.46 , pp. 1035-1044
    • Miller, L.M.1    Tibrewala, J.2    Carlson, C.S.3
  • 30
    • 0033618337 scopus 로고    scopus 로고
    • Matrix Metalloproteinases
    • Nagase H., Woessner J.F.J. Matrix Metalloproteinases. J. Biol. Chem. 274:1999;21491-21494.
    • (1999) J. Biol. Chem. , vol.274 , pp. 21491-21494
    • Nagase, H.1    Woessner, J.F.J.2
  • 31
    • 0033564112 scopus 로고    scopus 로고
    • Infrared spectroscopy
    • Ng L.M., Simmons R. Infrared spectroscopy. Anal. Chem. 71:1999;343R-350R.
    • (1999) Anal. Chem. , vol.71
    • Ng, L.M.1    Simmons, R.2
  • 32
    • 0036741135 scopus 로고    scopus 로고
    • Molecular determinants of metalloproteinase substrate specificity
    • Overall C.M. Molecular determinants of metalloproteinase substrate specificity. Mol. Biotech. 22:2002;51-86.
    • (2002) Mol. Biotech. , vol.22 , pp. 51-86
    • Overall, C.M.1
  • 33
    • 0023691514 scopus 로고
    • Fourier transform IR spectroscopy of collagen and gelatin solutions: Deconvolution of the Amide I band for conformational studies
    • Payne K.J., Veis A. Fourier transform IR spectroscopy of collagen and gelatin solutions: Deconvolution of the Amide I band for conformational studies. Biopolymers. 27:1988;1749-1760.
    • (1988) Biopolymers , vol.27 , pp. 1749-1760
    • Payne, K.J.1    Veis, A.2
  • 34
    • 0034442555 scopus 로고    scopus 로고
    • Collagen model peptides: Sequence dependence of triple-helix stability
    • Persikov A.V., Ramshaw J.A.M., Brodsky B. Collagen model peptides: sequence dependence of triple-helix stability. Biopolymers. 55:2000;436-450.
    • (2000) Biopolymers , vol.55 , pp. 436-450
    • Persikov, A.V.1    Ramshaw, J.A.M.2    Brodsky, B.3
  • 35
    • 0030125019 scopus 로고    scopus 로고
    • Infrared study of gelatin conformations in the gel and sol states
    • Prystupa D.A., Donald A.M. Infrared study of gelatin conformations in the gel and sol states. Pol. Gels Netw. 4:1996;87-110.
    • (1996) Pol. Gels Netw. , vol.4 , pp. 87-110
    • Prystupa, D.A.1    Donald, A.M.2
  • 36
    • 0031671855 scopus 로고    scopus 로고
    • Matrix metalloproteinase degradation of extracellular matrix: Biological consequences
    • Shapiro S.D. Matrix metalloproteinase degradation of extracellular matrix: biological consequences. Curr. Opin. Cell Biol. 10:1998;602-608.
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 602-608
    • Shapiro, S.D.1
  • 37
    • 0028909764 scopus 로고
    • Infrared spectroscopy applied to biochemical and biological problems
    • Siebert F. Infrared spectroscopy applied to biochemical and biological problems. Meth. Enzymol. 246:1995;501-526.
    • (1995) Meth. Enzymol. , vol.246 , pp. 501-526
    • Siebert, F.1
  • 38
    • 0033597726 scopus 로고    scopus 로고
    • The stromal proteinase MMP3/Stromelysin-1 promotes mammary carcinogenesis
    • Sternlicht M.D., Lochter A., Sympson C.J., Huey B., Rougier J.P., Gray J.W., et al. The stromal proteinase MMP3/Stromelysin-1 promotes mammary carcinogenesis. Cell. 98:1999;137-146.
    • (1999) Cell , vol.98 , pp. 137-146
    • Sternlicht, M.D.1    Lochter, A.2    Sympson, C.J.3    Huey, B.4    Rougier, J.P.5    Gray, J.W.6
  • 39
    • 0035188727 scopus 로고    scopus 로고
    • How matrix metalloproteinases regulate cell behavior
    • Sternlicht M.D., Werb Z. How matrix metalloproteinases regulate cell behavior. Ann. Rev. Cell Dev. Biol. 17:2001;463-516.
    • (2001) Ann. Rev. Cell Dev. Biol. , vol.17 , pp. 463-516
    • Sternlicht, M.D.1    Werb, Z.2
  • 40
    • 0032842777 scopus 로고    scopus 로고
    • Extracellular matrix remodeling and cellular differentiation
    • Streuli C. Extracellular matrix remodeling and cellular differentiation. Curr. Opin. Cell Biol. 11:1999;634-640.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 634-640
    • Streuli, C.1
  • 42
    • 0346456087 scopus 로고    scopus 로고
    • Development of an infrared microscope with fluorescence capabilities
    • Tague T., Miller L.M. Development of an infrared microscope with fluorescence capabilities. Micros. Today. 2:2000;26-32.
    • (2000) Micros. Today , vol.2 , pp. 26-32
    • Tague, T.1    Miller, L.M.2
  • 44
    • 0034731479 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinase (TIMP)-2 acts sinergistically with synthetic matrix metalloproteinase (MMP) inhibitors but not with TIMP-4 to enhance the (membrane type 1)-MMP-dependent activation of Pro-MMP-2
    • Toth M., Bernardo M.M., Gervasi D.C., Soloway P.D., Wang Z., Bigg H.F., et al. Tissue inhibitor of metalloproteinase (TIMP)-2 acts sinergistically with synthetic matrix metalloproteinase (MMP) inhibitors but not with TIMP-4 to enhance the (membrane type 1)-MMP-dependent activation of Pro-MMP-2. J. Biol. Chem. 275:2000;41415-41423.
    • (2000) J. Biol. Chem. , vol.275 , pp. 41415-41423
    • Toth, M.1    Bernardo, M.M.2    Gervasi, D.C.3    Soloway, P.D.4    Wang, Z.5    Bigg, H.F.6
  • 45
    • 0027970351 scopus 로고
    • Expression of gelatinase A, a mediator of extracellular matrix remodeling, by tracheal gland serous cells in culture and in vivo
    • Tournier J.M., Polette M., Hinnrasky J., Beck J., Werb Z., Basbaum C. Expression of gelatinase A, a mediator of extracellular matrix remodeling, by tracheal gland serous cells in culture and in vivo. J. Biol. Chem. 41:1994;25454-25464.
    • (1994) J. Biol. Chem. , vol.41 , pp. 25454-25464
    • Tournier, J.M.1    Polette, M.2    Hinnrasky, J.3    Beck, J.4    Werb, Z.5    Basbaum, C.6
  • 47
    • 0035887070 scopus 로고    scopus 로고
    • Fourier transform infrared spectrometric analysis of protein conformation: Effect of sampling method and stress factors
    • van de Weert M., Haris P.I., Hennink W.E., Crommelin D.J.A. Fourier transform infrared spectrometric analysis of protein conformation: effect of sampling method and stress factors. Anal. Biochem. 297:2001;160-169.
    • (2001) Anal. Biochem. , vol.297 , pp. 160-169
    • Van de Weert, M.1    Haris, P.I.2    Hennink, W.E.3    Crommelin, D.J.A.4
  • 48
    • 0025025442 scopus 로고
    • The cystein switch: A principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family
    • van Wart H.E., Birkedal-Hansen H. The cystein switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family. Proc. Natl. Acad. Sci. USA. 87:1990;5578-5582.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 5578-5582
    • Van Wart, H.E.1    Birkedal-Hansen, H.2
  • 49
    • 0033848986 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Effectors of development and normal physiology
    • Vu T.H., Werb Z. Matrix metalloproteinases: effectors of development and normal physiology. Gen. Dev. 14:2000;2123-2133.
    • (2000) Gen. Dev. , vol.14 , pp. 2123-2133
    • Vu, T.H.1    Werb, Z.2
  • 50
    • 0030715322 scopus 로고    scopus 로고
    • ECM and cell surface proteolysis: Regulating cellular ecology
    • Werb Z. ECM and cell surface proteolysis: Regulating cellular ecology. Cell. 91:1997;439-442.
    • (1997) Cell , vol.91 , pp. 439-442
    • Werb, Z.1
  • 51
    • 0033588032 scopus 로고    scopus 로고
    • Imaging molecular chemistry with infrared microscopy
    • Wetzel D.L., LeVine S.M. Imaging molecular chemistry with infrared microscopy. Science. 285:1999;1224-1225.
    • (1999) Science , vol.285 , pp. 1224-1225
    • Wetzel, D.L.1    LeVine, S.M.2
  • 52
    • 0034650486 scopus 로고    scopus 로고
    • Cell surface-localized matrix metalloproteinase-9 proteolytically activates TGF-b and promotes tumor invasion and angiogenesis
    • Yu Q., Stamenkovic I. Cell surface-localized matrix metalloproteinase-9 proteolytically activates TGF-b and promotes tumor invasion and angiogenesis. Gen. Dev. 14:2000;163-176.
    • (2000) Gen. Dev. , vol.14 , pp. 163-176
    • Yu, Q.1    Stamenkovic, I.2


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