메뉴 건너뛰기




Volumn 19, Issue 3, 2000, Pages 267-273

A versatile assay for gelatinases using succinylated gelatin

Author keywords

MMP 2; MMP 9; Succinylated gelatin

Indexed keywords

BATIMASTAT; COLLAGENASE; GELATIN; GELATIN SUCCINATE; GELATINASE; GELATINASE A; GELATINASE B; MATRILYSIN; MATRIX METALLOPROTEINASE INHIBITOR; PD 171534; STROMELYSIN; UNCLASSIFIED DRUG;

EID: 0034233690     PISSN: 0945053X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0945-053X(00)00086-X     Document Type: Article
Times cited : (60)

References (31)
  • 1
    • 0027201881 scopus 로고
    • A high throughput flourogenic substrate for interstitialcollagenase (MMP-1) and gelatinase (MMP-9)
    • Bickett D.M., Green M.D., Berman J. et al. A high throughput flourogenic substrate for interstitialcollagenase (MMP-1) and gelatinase (MMP-9). Anal. Biochem. 212:1993;58-64.
    • (1993) Anal. Biochem. , vol.212 , pp. 58-64
    • Bickett, D.M.1    Green, M.D.2    Berman, J.3
  • 2
    • 0026614994 scopus 로고
    • The determination of epsilon-amino groups in soluble and poorly soluble proteinaceous materials by a spectrophotometric method using trinitrobenzenesulfonic acid
    • Bubnis W.A., Ofner C.M. The determination of epsilon-amino groups in soluble and poorly soluble proteinaceous materials by a spectrophotometric method using trinitrobenzenesulfonic acid. Anal. Biochem. 207:1992;129-133.
    • (1992) Anal. Biochem. , vol.207 , pp. 129-133
    • Bubnis, W.A.1    Ofner, C.M.2
  • 3
    • 0023919959 scopus 로고
    • Hras oncogene-trasnformed human bronchial epitheleal cells (TBE-1) secrete a single metalloproteinase capable of degrading basement membrane collagen
    • Collier I.E., Wilhelm S.M., Eisen A.Z. et al. Hras oncogene-trasnformed human bronchial epitheleal cells (TBE-1) secrete a single metalloproteinase capable of degrading basement membrane collagen. J. Biol. Chem. 263:1988;6579-6587.
    • (1988) J. Biol. Chem. , vol.263 , pp. 6579-6587
    • Collier, I.E.1    Wilhelm, S.M.2    Eisen, A.Z.3
  • 4
    • 0026630048 scopus 로고
    • Interaction of 92-Kda type IV collagenase with the tissue inhibitor of metalloproteinases prevents dimerizatio, complex formation with interstitial collagenase and activation of the proenzyme with stromelysin
    • Goldberg G.I., Strongin A., Collier I.E., Genrich L.T., Marmer B.L. Interaction of 92-Kda type IV collagenase with the tissue inhibitor of metalloproteinases prevents dimerizatio, complex formation with interstitial collagenase and activation of the proenzyme with stromelysin. J. Biol. Chem. 267:1992;4582-4591.
    • (1992) J. Biol. Chem. , vol.267 , pp. 4582-4591
    • Goldberg, G.I.1    Strongin, A.2    Collier, I.E.3    Genrich, L.T.4    Marmer, B.L.5
  • 5
    • 0020032754 scopus 로고
    • Characterization of vertebrate collagenase activity by high performance liquid chromatography using synthetic substrates
    • Gray R.D., Saneii H.H. Characterization of vertebrate collagenase activity by high performance liquid chromatography using synthetic substrates. Anal. Biochem. 120:1982;339-346.
    • (1982) Anal. Biochem. , vol.120 , pp. 339-346
    • Gray, R.D.1    Saneii, H.H.2
  • 6
    • 0018854046 scopus 로고
    • Electrophoretic analysis of plasminogen activators in polyacrylamide gels containing sodium dodecyl sulfate and copolymerized substrates
    • Heussen C., Dowdle E.B. Electrophoretic analysis of plasminogen activators in polyacrylamide gels containing sodium dodecyl sulfate and copolymerized substrates. Anal. Biochem. 102:1980;196-202.
    • (1980) Anal. Biochem. , vol.102 , pp. 196-202
    • Heussen, C.1    Dowdle, E.B.2
  • 7
    • 0021918104 scopus 로고
    • Biochemical and immunological characterization of the secreted forms of human neutrophil gelatinase
    • Hibbs M.S., Hasty K.A., Seyer J.M., Kang A.H., Mainardi C.L. Biochemical and immunological characterization of the secreted forms of human neutrophil gelatinase. J. Bol. Chem. 260:1985;2493-2500.
    • (1985) J. Bol. Chem. , vol.260 , pp. 2493-2500
    • Hibbs, M.S.1    Hasty, K.A.2    Seyer, J.M.3    Kang, A.H.4    Mainardi, C.L.5
  • 8
    • 0028345645 scopus 로고
    • Quantitaive zymography: Detection of picogram quantities of gelatinases
    • Kleiner D.E., Stetler-Stevenson W.G. Quantitaive zymography: detection of picogram quantities of gelatinases. Anal. Biochem. 218:1994;325-329.
    • (1994) Anal. Biochem. , vol.218 , pp. 325-329
    • Kleiner, D.E.1    Stetler-Stevenson, W.G.2
  • 9
    • 0026505650 scopus 로고
    • A novel coumarin-labelled peptide for sensitive continuous assays of the matrix metalloproteinases
    • Knight C.G., Willenbrock F., Murphy G. A novel coumarin-labelled peptide for sensitive continuous assays of the matrix metalloproteinases. FEBS Lett. 296:1992;263-266.
    • (1992) FEBS Lett. , vol.296 , pp. 263-266
    • Knight, C.G.1    Willenbrock, F.2    Murphy, G.3
  • 10
    • 0031570725 scopus 로고    scopus 로고
    • Zymography: A single step staining method for quantitation of proteolytic activity on substrate gels
    • Leber T.M., Balkwill F.R. Zymography: a single step staining method for quantitation of proteolytic activity on substrate gels. Anal. Biochem. 249:1997;24-28.
    • (1997) Anal. Biochem. , vol.249 , pp. 24-28
    • Leber, T.M.1    Balkwill, F.R.2
  • 11
    • 0021732056 scopus 로고
    • Purification of a type V collagen degrading metalloproteinase from rabbit alveolar macrophages
    • Mainardi C.L., Hibbs M.S., Hasty K.A., Seyer J.M. Purification of a type V collagen degrading metalloproteinase from rabbit alveolar macrophages. Coll. Rel. Res. 4:1984;479-492.
    • (1984) Coll. Rel. Res. , vol.4 , pp. 479-492
    • Mainardi, C.L.1    Hibbs, M.S.2    Hasty, K.A.3    Seyer, J.M.4
  • 13
    • 0015856509 scopus 로고
    • Gelatin: A poor substrate for mammalian collagenase
    • McCroskery P.A., Harris E.D. Jr. Gelatin: a poor substrate for mammalian collagenase. Science. 182:1973;70-71.
    • (1973) Science , vol.182 , pp. 70-71
    • McCroskery, P.A.1    Harris E.D., Jr.2
  • 14
    • 0028567973 scopus 로고
    • Characterization of the peptide substrate specificities of interstitial collagenase and 92 Kda gelatinase. Implications for substrate optimization
    • McGeehan G.M., Bickett D.M., Green M., Kassel D., Wiseman J.S., Berman J. Characterization of the peptide substrate specificities of interstitial collagenase and 92 Kda gelatinase. Implications for substrate optimization. Biol. Chem. 269:1994;32814-32820.
    • (1994) Biol. Chem. , vol.269 , pp. 32814-32820
    • McGeehan, G.M.1    Bickett, D.M.2    Green, M.3    Kassel, D.4    Wiseman, J.S.5    Berman, J.6
  • 16
    • 0029758751 scopus 로고    scopus 로고
    • Human matrix metalloproteinase specificity studies using collagen sequence-based synthetic peptides
    • Nagase H., Fields G.B. Human matrix metalloproteinase specificity studies using collagen sequence-based synthetic peptides. Biopolymers. 40:1996;399-416.
    • (1996) Biopolymers , vol.40 , pp. 399-416
    • Nagase, H.1    Fields, G.B.2
  • 17
    • 0032412281 scopus 로고    scopus 로고
    • Expression of gelatinase A and B, stromelysin-3 and matrilysin genes in breast carcinoma: Clinico pathological correlations
    • Pacheco M.M. et al. Expression of gelatinase A and B, stromelysin-3 and matrilysin genes in breast carcinoma: clinico pathological correlations. Clin. Exp. Metastasis. 7:1998;577-585.
    • (1998) Clin. Exp. Metastasis , vol.7 , pp. 577-585
    • Pacheco, M.M.1
  • 19
    • 0019508077 scopus 로고
    • Purification and properties of a gelatin-specific neutral protease from human skin
    • Seltzer J.L., Adams S.A., Grant G.A., Eisen A.Z. Purification and properties of a gelatin-specific neutral protease from human skin. J. Biol. Chem. 256:1981;4662-4668.
    • (1981) J. Biol. Chem. , vol.256 , pp. 4662-4668
    • Seltzer, J.L.1    Adams, S.A.2    Grant, G.A.3    Eisen, A.Z.4
  • 21
    • 0028932675 scopus 로고
    • Activation of the 92 Kda gelatinase by stromelysin and 4-aminophenylmercuric acetate. Differential processing of the carboxyl terminal domain by tissue inhibitors of matrix metalloproteinases (TIMP)
    • Shapiro S.D., Fliszar C.J., Broekelmann T.J., Mecham R.P., Senior R.M., Welgus H.G. Activation of the 92 Kda gelatinase by stromelysin and 4-aminophenylmercuric acetate. Differential processing of the carboxyl terminal domain by tissue inhibitors of matrix metalloproteinases (TIMP). J. Biol. Chem. 270:1995;6351-6356.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6351-6356
    • Shapiro, S.D.1    Fliszar, C.J.2    Broekelmann, T.J.3    Mecham, R.P.4    Senior, R.M.5    Welgus, H.G.6
  • 22
    • 0030068937 scopus 로고    scopus 로고
    • The structural basis for the elastolytic activity of the 92 Kda and 72 Kda gelatinases. Role of fibronectin type II-like repeats
    • Shipley J.M., Doyle G.A.R., Fliszar C.J., Ye Q.-Z., Johnson L.L., Shapiro S.D., Welgus H.G., Senior R.M. The structural basis for the elastolytic activity of the 92 Kda and 72 Kda gelatinases. Role of fibronectin type II-like repeats. J. Biol. Chem. 271:1996;4335-4341.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4335-4341
    • Shipley, J.M.1    Doyle, G.A.R.2    Fliszar, C.J.3    Ye, Q.-Z.4    Johnson, L.L.5    Shapiro, S.D.6    Welgus, H.G.7    Senior, R.M.8
  • 23
    • 0024564708 scopus 로고
    • Comparison of vertebrate collagenase and gelatinase using a new fluorogenic substrate peptide
    • Stack M.S., Gray R.D. Comparison of vertebrate collagenase and gelatinase using a new fluorogenic substrate peptide. J. Biol. Chem. 264:1989;4277-4281.
    • (1989) J. Biol. Chem. , vol.264 , pp. 4277-4281
    • Stack, M.S.1    Gray, R.D.2
  • 24
    • 0027333411 scopus 로고
    • Tumor cell interactions with the extracellular matrix during invasion and metastasis
    • Stetler-Stevenson W.G., Aznavoorian S., Liotta L.A. Tumor cell interactions with the extracellular matrix during invasion and metastasis. Annu. Rev. Cell Biol. 9:1993;541-573.
    • (1993) Annu. Rev. Cell Biol. , vol.9 , pp. 541-573
    • Stetler-Stevenson, W.G.1    Aznavoorian, S.2    Liotta, L.A.3
  • 25
    • 0022387489 scopus 로고
    • Synthetic substrates for vertebrate collagenases
    • Weingarten H., Martin R., Feder J. Synthetic substrates for vertebrate collagenases. Biochemistry. 24:1985;6730-6734.
    • (1985) Biochemistry , vol.24 , pp. 6730-6734
    • Weingarten, H.1    Martin, R.2    Feder, J.3
  • 26
    • 0022477681 scopus 로고
    • 12-o-tetradecanoyl-phorbol-13-acetate differentiated U937 cells express a macrophage like profile of neutral proteinases. High levels of secreted collagenase and collagenase inhibitor accompany low levels of intracellular elastase and cathepsin G
    • Welgus H.G., Connolly N.L., Senior R.M. 12-o-tetradecanoyl-phorbol-13-acetate differentiated U937 cells express a macrophage like profile of neutral proteinases. High levels of secreted collagenase and collagenase inhibitor accompany low levels of intracellular elastase and cathepsin G. J. Clin. Invest. 77:1986;1675-1681.
    • (1986) J. Clin. Invest. , vol.77 , pp. 1675-1681
    • Welgus, H.G.1    Connolly, N.L.2    Senior, R.M.3
  • 27
    • 0024330327 scopus 로고
    • SV40-transformed human lung fibroblasts secrete a 92 KDa type IV collagenase which is identical to that secreted by normal human macrophage
    • Wilhelm S.M., Collier I.E., Marmer B.L., Eisen A.Z., Grant G., Goldberg G.I. SV40-transformed human lung fibroblasts secrete a 92 KDa type IV collagenase which is identical to that secreted by normal human macrophage. J. Biol. Chem. 264:1989;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.5    Goldberg, G.I.6
  • 28
    • 0029880229 scopus 로고    scopus 로고
    • Comparison of the cleavage site specificity of gelatinase A and B using collagenase peptides
    • Xia T., Akers K., Eisen A.Z., Seltzer J.L. Comparison of the cleavage site specificity of gelatinase A and B using collagenase peptides. Biochim. Biophys. Acta. 1293:1996;259-266.
    • (1996) Biochim. Biophys. Acta , vol.1293 , pp. 259-266
    • Xia, T.1    Akers, K.2    Eisen, A.Z.3    Seltzer, J.L.4
  • 29
    • 0018388950 scopus 로고
    • Comparison of vertebrate collagenase and gelatinase using a new flourogenic substrate
    • Yaron A., Carmel A., Katchalski-Katzir E. Comparison of vertebrate collagenase and gelatinase using a new flourogenic substrate. Anal. Biochem. 95:1979;228-235.
    • (1979) Anal. Biochem. , vol.95 , pp. 228-235
    • Yaron, A.1    Carmel, A.2    Katchalski-Katzir, E.3
  • 30
    • 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., Baragi V. Purification and characterization of the human stromelysin catalytic domain expressed in Escherichia coli. Biochemistry. 31:1992;11231-11235.
    • (1992) Biochemistry , vol.31 , pp. 11231-11235
    • Ye, Q.-Z.1    Johnson, L.L.2    Hupe, D.J.3    Baragi, V.4
  • 31
    • 0027954350 scopus 로고
    • Comparison of techniques for measurement of gelatinases/type IV collagenases: Enzyme-linked immunoassays versus substrate degradation assays
    • Zucker S., Mancuso P., DiMassimo B., Lysik R.M., Conner C., Wu C.-L. Comparison of techniques for measurement of gelatinases/type IV collagenases: enzyme-linked immunoassays versus substrate degradation assays. Clin. Exp. Metastasis. 12:1994;13-23.
    • (1994) Clin. Exp. Metastasis , vol.12 , pp. 13-23
    • Zucker, S.1    Mancuso, P.2    Dimassimo, B.3    Lysik, R.M.4    Conner, C.5    Wu, C.-L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.