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Volumn 338, Issue 1, 2005, Pages 151-158

Optical zymography for specific detection of urokinase plasminogen activator activity in biological samples

Author keywords

Fluorescence; Optical zymography; Probe; Urokinase

Indexed keywords

CELL CULTURE; ELECTROPHORESIS; FLUORESCENCE; PROBES; SULFUR COMPOUNDS;

EID: 13644263240     PISSN: 00032697     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ab.2004.11.039     Document Type: Article
Times cited : (17)

References (36)
  • 1
    • 0030788411 scopus 로고    scopus 로고
    • The urokinase-type plasminogen activator system in cancer metastasis: A review
    • P.A. Andreasen, L. Kjoller, L. Christensen, and M.J. Duffy The urokinase-type plasminogen activator system in cancer metastasis: a review Int. J. Cancer 72 1997 1 22
    • (1997) Int. J. Cancer , vol.72 , pp. 1-22
    • Andreasen, P.A.1    Kjoller, L.2    Christensen, L.3    Duffy, M.J.4
  • 2
    • 0036516460 scopus 로고    scopus 로고
    • Matrix metalloproteinases: A tail of a frog that became a prince
    • C.E. Brinckerhoff, and L.M. Matrisian Matrix metalloproteinases: a tail of a frog that became a prince Nat. Rev. Mol. Cell Biol. 3 2002 207 214
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 207-214
    • Brinckerhoff, C.E.1    Matrisian, L.M.2
  • 3
    • 0036582601 scopus 로고    scopus 로고
    • Matrix metalloproteinases (MMP) in lung cancer
    • K. Nabeshima, Y. Shimao, T. Inoue, and T. Sameshima Matrix metalloproteinases (MMP) in lung cancer Nippon Rinsho 60 Suppl. 5 2002 103 109
    • (2002) Nippon Rinsho , vol.60 , Issue.SUPPL. 5 , pp. 103-109
    • Nabeshima, K.1    Shimao, Y.2    Inoue, T.3    Sameshima, T.4
  • 4
    • 0035990901 scopus 로고    scopus 로고
    • Matrix metalloproteinases in tumor invasion: Role for cell migration
    • K. Nabeshima, T. Inoue, Y. Shimao, and T. Sameshima Matrix metalloproteinases in tumor invasion: role for cell migration Pathol. Int. 52 2002 255 264
    • (2002) Pathol. Int. , vol.52 , pp. 255-264
    • Nabeshima, K.1    Inoue, T.2    Shimao, Y.3    Sameshima, T.4
  • 7
    • 0018854046 scopus 로고
    • Electrophoretic analysis of plasminogen activators in polyacrylamide gels containing sodium dodecyl sulfate and copolymerized substrates
    • C. Heussen, and E.B. Dowdle 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
  • 8
    • 0022979424 scopus 로고
    • Secretion of metalloproteinases by stimulated capillary endothelial cells: II. Expression of collagenase and stromelysin activities is regulated by endogenous inhibitors
    • G.S. Herron, M.J. Banda, E.J. Clark, J. Gavrilovic, and Z. Werb Secretion of metalloproteinases by stimulated capillary endothelial cells: II. Expression of collagenase and stromelysin activities is regulated by endogenous inhibitors J. Biol. Chem. 261 1986 2814 2818
    • (1986) J. Biol. Chem. , vol.261 , pp. 2814-2818
    • Herron, G.S.1    Banda, M.J.2    Clark, E.J.3    Gavrilovic, J.4    Werb, Z.5
  • 9
    • 0031024924 scopus 로고    scopus 로고
    • Quantitative reverse zymography: Analysis of picogram amounts of metalloproteinase inhibitors using gelatinase a and B reverse zymograms
    • G.W. Oliver, J.D. Leferson, W.G. Stetler-Stevenson, and D.E. Kleiner Quantitative reverse zymography: analysis of picogram amounts of metalloproteinase inhibitors using gelatinase A and B reverse zymograms Anal. Biochem. 244 1997 161 166
    • (1997) Anal. Biochem. , vol.244 , pp. 161-166
    • Oliver, G.W.1    Leferson, J.D.2    Stetler-Stevenson, W.G.3    Kleiner, D.E.4
  • 10
    • 0028345645 scopus 로고
    • Quantitative zymography: Detection of picogram quantities of gelatinases
    • D.E. Kleiner, and W.G. Stetler-Stevenson Quantitative 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
  • 11
    • 0028934954 scopus 로고
    • Analysis of glycosaminoglycan-degrading enzymes by substrate gel electrophoresis (zymography)
    • R.O. Miura, S. Yamagata, Y. Miura, T. Harada, and T. Yamagata Analysis of glycosaminoglycan-degrading enzymes by substrate gel electrophoresis (zymography) Anal. Biochem. 225 1995 333 340
    • (1995) Anal. Biochem. , vol.225 , pp. 333-340
    • Miura, R.O.1    Yamagata, S.2    Miura, Y.3    Harada, T.4    Yamagata, T.5
  • 12
    • 0034045641 scopus 로고    scopus 로고
    • Detection of proteolytic activity by fluorescent zymogram in-gel assays
    • S. Yasothornsrikul, and V.Y. Hook Detection of proteolytic activity by fluorescent zymogram in-gel assays BioTechniques 28 2000 1166 1173
    • (2000) BioTechniques , vol.28 , pp. 1166-1173
    • Yasothornsrikul, S.1    Hook, V.Y.2
  • 13
    • 0033737383 scopus 로고    scopus 로고
    • Sensitive method to identify and characterize proteinases in situ after SDS-PAGE
    • J. Williams, W.J. McGrath, and W.F. Mangel Sensitive method to identify and characterize proteinases in situ after SDS-PAGE BioTechniques 29 2000 1108 1113
    • (2000) BioTechniques , vol.29 , pp. 1108-1113
    • Williams, J.1    McGrath, W.J.2    Mangel, W.F.3
  • 14
    • 0347764627 scopus 로고    scopus 로고
    • Trypsin activity assay in substrate-specific one- and two-dimensional gels: A powerful method to separate and characterize novel proteases in active form in biological samples
    • Z. Zhao, and P.J. Russell Trypsin activity assay in substrate-specific one- and two-dimensional gels: a powerful method to separate and characterize novel proteases in active form in biological samples Electrophoresis 24 2003 3284 3288
    • (2003) Electrophoresis , vol.24 , pp. 3284-3288
    • Zhao, Z.1    Russell, P.J.2
  • 15
    • 2342478508 scopus 로고    scopus 로고
    • Application of in-gel protease assay in a biological sample: Characterization and identification of urokinase-type plasminogen activator (uPA) in secreted proteins from a prostate cancer cell line PC-3
    • Z. Zhao, M.J. Raftery, X.M. Niu, M.M. Daja, and P.J. Russell Application of in-gel protease assay in a biological sample: characterization and identification of urokinase-type plasminogen activator (uPA) in secreted proteins from a prostate cancer cell line PC-3 Electrophoresis 25 2004 1142 1148
    • (2004) Electrophoresis , vol.25 , pp. 1142-1148
    • Zhao, Z.1    Raftery, M.J.2    Niu, X.M.3    Daja, M.M.4    Russell, P.J.5
  • 16
    • 1142306153 scopus 로고    scopus 로고
    • Design, synthesis, and characterization of urokinase plasminogen activator-sensitive near-infrared reporter
    • B. Law, A. Curino, T.H. Bugge, R. Weissleder, and C.H. Tung Design, synthesis, and characterization of urokinase plasminogen activator-sensitive near-infrared reporter Chem. Biol. 11 2004 99 106
    • (2004) Chem. Biol. , vol.11 , pp. 99-106
    • Law, B.1    Curino, A.2    Bugge, T.H.3    Weissleder, R.4    Tung, C.H.5
  • 17
    • 0032697682 scopus 로고    scopus 로고
    • Near-infrared optical imaging of protease activity for tumor detection
    • U. Mahmood, C.H. Tung, A. Bogdanov Jr., and R. Weissleder Near-infrared optical imaging of protease activity for tumor detection Radiology 213 1999 866 870
    • (1999) Radiology , vol.213 , pp. 866-870
    • Mahmood, U.1    Tung, C.H.2    Bogdanov Jr., A.3    Weissleder, R.4
  • 18
    • 0023031062 scopus 로고
    • Plasminogen activators, plasminogen activator inhibitors, and procoagulant analyzed in twenty human tumor cell lines
    • J.F. Cajot, E.K. Kruithof, W.D. Schleuning, B. Sordat, and F. Bachmann Plasminogen activators, plasminogen activator inhibitors, and procoagulant analyzed in twenty human tumor cell lines Int. J. Cancer 38 1986 719 727
    • (1986) Int. J. Cancer , vol.38 , pp. 719-727
    • Cajot, J.F.1    Kruithof, E.K.2    Schleuning, W.D.3    Sordat, B.4    Bachmann, F.5
  • 19
    • 0028228422 scopus 로고
    • The state of differentiation of HT-29 colon carcinoma cells alters the secretion of cathepsin D and of plasminogen activator
    • G. Huet, F. Zerimech, M.C. Dieu, B. Hemon, G. Grard, M. Balduyck, A. Janin, R. Lafyatis, and P. Degand The state of differentiation of HT-29 colon carcinoma cells alters the secretion of cathepsin D and of plasminogen activator Int. J. Cancer 57 1994 875 882
    • (1994) Int. J. Cancer , vol.57 , pp. 875-882
    • Huet, G.1    Zerimech, F.2    Dieu, M.C.3    Hemon, B.4    Grard, G.5    Balduyck, M.6    Janin, A.7    Lafyatis, R.8    Degand, P.9
  • 20
    • 0027408681 scopus 로고
    • The role of the urokinase receptor in extracellular matrix degradation by HT29 human colon carcinoma cells
    • L.S. Reiter, E.K. Kruithof, J.F. Cajot, and B. Sordat The role of the urokinase receptor in extracellular matrix degradation by HT29 human colon carcinoma cells Int. J. Cancer 53 1993 444 450
    • (1993) Int. J. Cancer , vol.53 , pp. 444-450
    • Reiter, L.S.1    Kruithof, E.K.2    Cajot, J.F.3    Sordat, B.4
  • 21
    • 0032518450 scopus 로고    scopus 로고
    • Collagen zymography as a sensitive and specific technique for the determination of subpicogram levels of interstitial collagenase
    • B. Gogly, N. Groult, W. Hornebeck, G. Godeau, and B. Pellat Collagen zymography as a sensitive and specific technique for the determination of subpicogram levels of interstitial collagenase Anal. Biochem. 255 1998 211 216
    • (1998) Anal. Biochem. , vol.255 , pp. 211-216
    • Gogly, B.1    Groult, N.2    Hornebeck, W.3    Godeau, G.4    Pellat, B.5
  • 22
    • 0029048989 scopus 로고
    • Casein zymography: A method to study mu-calpain, m-calpain, and their inhibitory agents
    • K.J. Raser, A. Posner, and K.K. Wang Casein zymography: a method to study mu-calpain, m-calpain, and their inhibitory agents Arch. Biochem. Biophys. 319 1995 211 216
    • (1995) Arch. Biochem. Biophys. , vol.319 , pp. 211-216
    • Raser, K.J.1    Posner, A.2    Wang, K.K.3
  • 23
    • 0032190365 scopus 로고    scopus 로고
    • Fibrin zymography: A direct analysis of fibrinolytic enzymes on gels
    • S.H. Kim, N.S. Choi, and W.Y. Lee Fibrin zymography: a direct analysis of fibrinolytic enzymes on gels Anal. Biochem. 263 1998 115 116
    • (1998) Anal. Biochem. , vol.263 , pp. 115-116
    • Kim, S.H.1    Choi, N.S.2    Lee, W.Y.3
  • 24
    • 0031570725 scopus 로고    scopus 로고
    • Zymography: A single-step staining method for quantitation of proteolytic activity on substrate gels
    • T.M. Leber, and F.R. Balkwill 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
  • 25
    • 0033200238 scopus 로고    scopus 로고
    • Preparation of a cathepsin D sensitive near-infrared fluorescence probe for imaging
    • C.H. Tung, S. Bredow, U. Mahmood, and R. Weissleder Preparation of a cathepsin D sensitive near-infrared fluorescence probe for imaging Bioconjug. Chem. 10 1999 892 896
    • (1999) Bioconjug. Chem. , vol.10 , pp. 892-896
    • Tung, C.H.1    Bredow, S.2    Mahmood, U.3    Weissleder, R.4
  • 26
    • 0030878999 scopus 로고    scopus 로고
    • Optimal subsite occupancy and design of a selective inhibitor of urokinase
    • S.H. Ke, G.S. Coombs, K. Tachias, D.R. Corey, and E.L. Madison Optimal subsite occupancy and design of a selective inhibitor of urokinase J. Biol. Chem. 272 1997 20456 20462
    • (1997) J. Biol. Chem. , vol.272 , pp. 20456-20462
    • Ke, S.H.1    Coombs, G.S.2    Tachias, K.3    Corey, D.R.4    Madison, E.L.5
  • 27
    • 0021337125 scopus 로고
    • Detection of proteases in polyacrylamide gels containing covalently bound substrates
    • P.J. Kelleher, and R.L. Juliano Detection of proteases in polyacrylamide gels containing covalently bound substrates Anal. Biochem. 136 1984 470 475
    • (1984) Anal. Biochem. , vol.136 , pp. 470-475
    • Kelleher, P.J.1    Juliano, R.L.2
  • 28
    • 0020494591 scopus 로고
    • Detergent-activation of latent collagenase and resolution of its component molecules
    • H. Birkedal-Hansen, and R.E. Taylor Detergent-activation of latent collagenase and resolution of its component molecules Biochem. Biophys. Res. Commun. 107 1982 1173 1178
    • (1982) Biochem. Biophys. Res. Commun. , vol.107 , pp. 1173-1178
    • Birkedal-Hansen, H.1    Taylor, R.E.2
  • 29
    • 0347087452 scopus 로고    scopus 로고
    • Chemical strategies for activity-based proteomics
    • A.E. Speers, and B.F. Cravatt Chemical strategies for activity-based proteomics ChemBioChem 5 2004 41 47
    • (2004) ChemBioChem , vol.5 , pp. 41-47
    • Speers, A.E.1    Cravatt, B.F.2
  • 30
    • 9144270498 scopus 로고    scopus 로고
    • Fluorescent peptide probes for in vivo diagnostic imaging
    • C.H. Tung Fluorescent peptide probes for in vivo diagnostic imaging Biopolymers 76 2004 391 403
    • (2004) Biopolymers , vol.76 , pp. 391-403
    • Tung, C.H.1
  • 31
    • 0032951071 scopus 로고    scopus 로고
    • In vivo imaging of tumors with protease-activated near-infrared fluorescent probes
    • R. Weissleder, C.H. Tung, U. Mahmood, and A. Bogdanov Jr. In vivo imaging of tumors with protease-activated near-infrared fluorescent probes Nat. Biotechnol. 17 1999 375 378
    • (1999) Nat. Biotechnol. , vol.17 , pp. 375-378
    • Weissleder, R.1    Tung, C.H.2    Mahmood, U.3    Bogdanov Jr., A.4
  • 32
    • 0034954524 scopus 로고    scopus 로고
    • In vivo molecular target assessment of matrix metalloproteinase inhibition
    • C. Bremer, C.H. Tung, and R. Weissleder In vivo molecular target assessment of matrix metalloproteinase inhibition Nat. Med. 7 2001 743 748
    • (2001) Nat. Med. , vol.7 , pp. 743-748
    • Bremer, C.1    Tung, C.H.2    Weissleder, R.3
  • 35
    • 2342583529 scopus 로고    scopus 로고
    • Inducible release of TRAIL fusion proteins from a proapoptotic form for tumor therapy
    • K. Shah, C.H. Tung, K. Yang, R. Weissleder, and X.O. Breakefield Inducible release of TRAIL fusion proteins from a proapoptotic form for tumor therapy Cancer Res. 64 2004 3236 3242
    • (2004) Cancer Res. , vol.64 , pp. 3236-3242
    • Shah, K.1    Tung, C.H.2    Yang, K.3    Weissleder, R.4    Breakefield, X.O.5
  • 36
    • 0036523372 scopus 로고    scopus 로고
    • A novel near-infrared fluorescence sensor for detection of thrombin activation in blood
    • C.H. Tung, R.E. Gerszten, F.A. Jaffer, and R. Weissleder A novel near-infrared fluorescence sensor for detection of thrombin activation in blood ChemBioChem 3 2002 207 211
    • (2002) ChemBioChem , vol.3 , pp. 207-211
    • Tung, C.H.1    Gerszten, R.E.2    Jaffer, F.A.3    Weissleder, R.4


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