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Volumn 17, Issue 6, 2012, Pages 1113-1119

Recent development of highly sensitive Protease assay methods: Signal amplification through enzyme cascades

Author keywords

Enzyme cascade; Protease assay; Resonance energy transfer; Signal amplification

Indexed keywords

ASSAYS; DIAGNOSIS; ENERGY TRANSFER; ENZYMES; RESONANCE; SIGNAL PROCESSING;

EID: 84879924939     PISSN: 12268372     EISSN: 19763816     Source Type: Journal    
DOI: 10.1007/s12257-012-0545-9     Document Type: Review
Times cited : (20)

References (43)
  • 1
    • 52949151513 scopus 로고    scopus 로고
    • Protease proteomics: Revealing protease in vivo functions using systems biology approaches
    • Doucet, A. and C. M. Overall (2008) Protease proteomics: Revealing protease in vivo functions using systems biology approaches. Mol. Aspects Med. 29:339-358.
    • (2008) Mol. Aspects Med. , vol.29 , pp. 339-358
    • Doucet, A.1    Overall, C.M.2
  • 2
    • 33748308883 scopus 로고    scopus 로고
    • Targeting proteases: Successes, failures and future prospects
    • Turk, B. (2006) Targeting proteases: Successes, failures and future prospects. Nature Rev. Drug Discovery 5:785-799.
    • (2006) Nature Rev. Drug Discovery , vol.5 , pp. 785-799
    • Turk, B.1
  • 4
    • 0032490741 scopus 로고    scopus 로고
    • Cancer. Proteases-invasion and more
    • Edwards, D. R. and G Murphy (1998) Cancer. Proteases-invasion and more. Nature 394:527-528.
    • (1998) Nature , vol.394 , pp. 527-528
    • Edwards, D.R.1    Murphy, G.2
  • 5
    • 36849043984 scopus 로고    scopus 로고
    • Protease-sensitive fluorescent nanofibers
    • Law, B., R. Weissleder, and C. H. Tung (2007) Protease-sensitive fluorescent nanofibers. Bioconjugate Chem. 18:1701-1704.
    • (2007) Bioconjugate Chem. , vol.18 , pp. 1701-1704
    • Law, B.1    Weissleder, R.2    Tung, C.H.3
  • 6
    • 0035398526 scopus 로고    scopus 로고
    • A genomic perspective on human proteases as drug targets
    • Southan, C. (2001) A genomic perspective on human proteases as drug targets. Drug Discovery Today 6:681-688.
    • (2001) Drug Discovery Today , vol.6 , pp. 681-688
    • Southan, C.1
  • 8
    • 0034176764 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Multifunctional contributors to tumor progression
    • McCawley, L. J. and L. M. Matrisian (2000) Matrix metalloproteinases: Multifunctional contributors to tumor progression. Mol. Med. Today 6:149-156.
    • (2000) Mol. Med. Today , vol.6 , pp. 149-156
    • McCawley, L.J.1    Matrisian, L.M.2
  • 9
    • 43749107913 scopus 로고    scopus 로고
    • Application of activitybased probes to the study of enzymes involved in cancer progression
    • Paulick, M. G and M. Bogyo (2008) Application of activitybased probes to the study of enzymes involved in cancer progression. Curr. Opin. Gen. Develop. 18:97-106.
    • (2008) Curr. Opin. Gen. Develop. , vol.18 , pp. 97-106
    • Paulick, M.G.1    Bogyo, M.2
  • 11
    • 0035101380 scopus 로고    scopus 로고
    • The control of prostate-specific antigen expression and gene regulation by pharmacological agents
    • Dixon, S. C., K. B. Knopf, and W. D. Figg (2001) The control of prostate-specific antigen expression and gene regulation by pharmacological agents. Pharmacol. Rev. 53:73-91.
    • (2001) Pharmacol. Rev. , vol.53 , pp. 73-91
    • Dixon, S.C.1    Knopf, K.B.2    Figg, W.D.3
  • 13
    • 9144270498 scopus 로고    scopus 로고
    • Fluorescent peptide probes for in vivo diagnostic imaging
    • Tung, C. H. (2004) Fluorescent peptide probes for in vivo diagnostic imaging. Biopol. 76:391-403.
    • (2004) Biopol. , vol.76 , pp. 391-403
    • Tung, C.H.1
  • 15
    • 0030021904 scopus 로고    scopus 로고
    • A one-step sandwich enzyme immunoassay for human matrix metalloproteinase 7 (matrilysin) using monoclonal antibodies
    • Ohuchi, E., I. Azumano, S. Yoshida, K. Iwata, and Y. Okada (1996) A one-step sandwich enzyme immunoassay for human matrix metalloproteinase 7 (matrilysin) using monoclonal antibodies. Clin. Chim. Acta Intern. J. Clin. Chem. 244:181-198.
    • (1996) Clin. Chim. Acta Intern. J. Clin. Chem. , vol.244 , pp. 181-198
    • Ohuchi, E.1    Azumano, I.2    Yoshida, S.3    Iwata, K.4    Okada, Y.5
  • 16
    • 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
    • Zhao, Z., M. J. Raftery, X. M. Niu, M. M. Daja, and P. J. Russell (2004) 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 25:1142-1148.
    • (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
  • 17
    • 84864418602 scopus 로고    scopus 로고
    • Analysis of protease activity using quantum dots and resonance energy transfer
    • Kim, G B. and Y. P. Kim (2012) Analysis of protease activity using quantum dots and resonance energy transfer. Theranostics 2:127-138.
    • (2012) Theranostics , vol.2 , pp. 127-138
    • Kim, G.B.1    Kim, Y.P.2
  • 18
    • 78649840996 scopus 로고    scopus 로고
    • Protease sensing with nanoparticle based platforms
    • Welser, K., R. Adsley, B. M. Moore, W. C. Chan, and J. W. Aylott (2011) Protease sensing with nanoparticle based platforms. Anal. 136:29-41.
    • (2011) Anal. , vol.136 , pp. 29-41
    • Welser, K.1    Adsley, R.2    Moore, B.M.3    Chan, W.C.4    Aylott, J.W.5
  • 21
    • 34247526918 scopus 로고    scopus 로고
    • Activity based fingerprinting of proteases using FRET peptides
    • Sun, H., R. C. Panicker, and S. Q. Yao (2007) Activity based fingerprinting of proteases using FRET peptides. Biopol. 88:141-149.
    • (2007) Biopol. , vol.88 , pp. 141-149
    • Sun, H.1    Panicker, R.C.2    Yao, S.Q.3
  • 22
    • 34147186116 scopus 로고    scopus 로고
    • Activity-based fingerprinting and inhibitor discoveiy of cysteine proteases in a microarray
    • Uttamchandani, M., K. Liu, R. C. Panicker, and S. Q. Yao (2007) Activity-based fingerprinting and inhibitor discoveiy of cysteine proteases in a microarray. Chem. Commun. 15:1518-1520.
    • (2007) Chem. Commun. , vol.15 , pp. 1518-1520
    • Uttamchandani, M.1    Liu, K.2    Panicker, R.C.3    Yao, S.Q.4
  • 23
    • 18744388856 scopus 로고    scopus 로고
    • Engineering of protease variants exhibiting high catalytic activity and exquisite substrate selectivity
    • Varadarajan, N., J. Gam, M. J. Olsen, G Georgiou, and B. L. Iverson (2005) Engineering of protease variants exhibiting high catalytic activity and exquisite substrate selectivity. Proc. Nat. Acad. Sci. 102:6855-6860.
    • (2005) Proc. Nat. Acad. Sci. , vol.102 , pp. 6855-6860
    • Varadarajan, N.1    Gam, J.2    Olsen, M.J.3    Georgiou, G.4    Iverson, B.L.5
  • 25
    • 58949098779 scopus 로고    scopus 로고
    • Using specificity to strategically target proteases
    • Lim, M. D. and C. S. Craik (2009) Using specificity to strategically target proteases. Bioorg. Med. Chem. 17:1094-1100.
    • (2009) Bioorg. Med. Chem. , vol.17 , pp. 1094-1100
    • Lim, M.D.1    Craik, C.S.2
  • 26
    • 0033083490 scopus 로고    scopus 로고
    • Using GFP in FRET-based applications
    • Pollok, B. A. and R. Heim (1999) Using GFP in FRET-based applications. Trends Cell Biol. 9:57-60.
    • (1999) Trends Cell Biol. , vol.9 , pp. 57-60
    • Pollok, B.A.1    Heim, R.2
  • 27
    • 84856247987 scopus 로고    scopus 로고
    • Highly adaptable and sensitive protease assay based on fluorescence resonance energy transfer
    • Zauner, T., R. Berger-Hoffrnann, K. Muller, R. Hoffmann, and T. Zuchner (2011) Highly adaptable and sensitive protease assay based on fluorescence resonance energy transfer. Anal. Chem. 83:7356-7363.
    • (2011) Anal. Chem. , vol.83 , pp. 7356-7363
    • Zauner, T.1    Berger-Hoffrnann, R.2    Muller, K.3    Hoffmann, R.4    Zuchner, T.5
  • 28
    • 0030921002 scopus 로고    scopus 로고
    • Modified proenzymes as artificial substrates for proteolytic enzymes: Colorimetric assay of bacterial collagenase and matrix metalloproteinase activity using modified pro-urokinase
    • Verheijen, J. H., N. M. Nieuwenbroek, B. Beekman, R. Hanemaaijer, H. W. Verspaget, H. K. Ronday, and A. H. Bakker (1997) Modified proenzymes as artificial substrates for proteolytic enzymes: Colorimetric assay of bacterial collagenase and matrix metalloproteinase activity using modified pro-urokinase. Biochem. J. 323:603-609.
    • (1997) Biochem. J. , vol.323 , pp. 603-609
    • Verheijen, J.H.1    Nieuwenbroek, N.M.2    Beekman, B.3    Hanemaaijer, R.4    Verspaget, H.W.5    Ronday, H.K.6    Bakker, A.H.7
  • 31
    • 34547627492 scopus 로고    scopus 로고
    • Redshifted Renilla reniformis luciferase variants for imaging in living subjects
    • Loening, A. M., A. M. Wu, and S. S. Gambhir (2007) Redshifted Renilla reniformis luciferase variants for imaging in living subjects. Nature Meth. 4:641-643.
    • (2007) Nature Meth. , vol.4 , pp. 641-643
    • Loening, A.M.1    Wu, A.M.2    Gambhir, S.S.3
  • 32
    • 3943099375 scopus 로고    scopus 로고
    • Protein modification by SUMO
    • Johnson, E. S. (2004) Protein modification by SUMO. Annu. Rev. Biochem. 73:355-382.
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 355-382
    • Johnson, E.S.1
  • 33
    • 0019504493 scopus 로고
    • Active site and catalytic mechanism of phospholipase A2
    • Dijkstra, B. W., J. Drenth, and K. H. Kalk (1981) Active site and catalytic mechanism of phospholipase A2. Nature 289:604-606.
    • (1981) Nature , vol.289 , pp. 604-606
    • Dijkstra, B.W.1    Drenth, J.2    Kalk, K.H.3
  • 34
    • 59249109127 scopus 로고    scopus 로고
    • Detection and characterization of SUMO protease activity using a sensitive enzyme-based reporter assay
    • Leach, C. A., X. Tian, M. R. Mattem, and B. Nicholson (2009) Detection and characterization of SUMO protease activity using a sensitive enzyme-based reporter assay. Methods Mol. Biol. 497:269-281.
    • (2009) Methods Mol. Biol. , vol.497 , pp. 269-281
    • Leach, C.A.1    Tian, X.2    Mattem, M.R.3    Nicholson, B.4
  • 35
    • 0035984722 scopus 로고    scopus 로고
    • Beta-lactamase protein fragment complementation assays as in vivo and in vitro sensors of protein protein interactions
    • Galameau, A., M. Primeau, L. E. Trudeau, and S. W. Michnick (2002) Beta-lactamase protein fragment complementation assays as in vivo and in vitro sensors of protein protein interactions. Nat. Biotechnol. 20:619-622.
    • (2002) Nat. Biotechnol. , vol.20 , pp. 619-622
    • Galameau, A.1    Primeau, M.2    Trudeau, L.E.3    Michnick, S.W.4
  • 36
    • 0028080090 scopus 로고
    • Split ubiquitin as a sensor of protein interactions in vivo
    • Johnsson, N. and A. Varshavsky (1994) Split ubiquitin as a sensor of protein interactions in vivo. Proc. Nat. Acad. Sci. 91:10340-10344.
    • (1994) Proc. Nat. Acad. Sci. , vol.91 , pp. 10340-10344
    • Johnsson, N.1    Varshavsky, A.2
  • 37
    • 4344656346 scopus 로고    scopus 로고
    • Kinetics of regulated protein-protein interactions revealed with firefly luciferase complementation imaging in cells and living animals
    • Luker, K. E., M. C. Smith, G D. Luker, S. T. Gammon, H. Piwnica-Worms, and D. Piwnica-Worms (2004) Kinetics of regulated protein-protein interactions revealed with firefly luciferase complementation imaging in cells and living animals. Proc. Nat. Acad. Sci. 101:12288-12293.
    • (2004) Proc. Nat. Acad. Sci. , vol.101 , pp. 12288-12293
    • Luker, K.E.1    Smith, M.C.2    Luker, G.D.3    Gammon, S.T.4    Piwnica-Worms, H.5    Piwnica-Worms, D.6
  • 38
    • 0141757323 scopus 로고    scopus 로고
    • Reprogramming control of an allosteric signaling switch through modular recombination
    • Dueber, J. E., B. J. Yeh, K. Chak, and W. A. Lim (2003) Reprogramming control of an allosteric signaling switch through modular recombination. Science 301:1904-1908.
    • (2003) Science , vol.301 , pp. 1904-1908
    • Dueber, J.E.1    Yeh, B.J.2    Chak, K.3    Lim, W.A.4
  • 39
    • 0036441510 scopus 로고    scopus 로고
    • Autoinhibitoiy domains: Modular effectors of cellular regulation
    • Pufall, M. A. and B. J. Graves (2002) Autoinhibitoiy domains: modular effectors of cellular regulation. Annu. Rev. Cell Develop. Biol. 18:421-462.
    • (2002) Annu. Rev. Cell Develop. Biol. , vol.18 , pp. 421-462
    • Pufall, M.A.1    Graves, B.J.2
  • 40
    • 70350329253 scopus 로고    scopus 로고
    • An autoinhibited coiled-coil design strategy for split-protein protease sensors
    • Shekhawat, S. S., J. R. Porter, A. Sriprasad, and I. Ghosh (2009) An autoinhibited coiled-coil design strategy for split-protein protease sensors. J. American Chem. Soc. 131:15284-15290.
    • (2009) J. American Chem. Soc. , vol.131 , pp. 15284-15290
    • Shekhawat, S.S.1    Porter, J.R.2    Sriprasad, A.3    Ghosh, I.4
  • 41
    • 80053600864 scopus 로고    scopus 로고
    • A Comprehensive panel of turn-on caspase biosensors for investigating caspase specificity and caspase activation pathways
    • Shekhawat, S. S., S. T. Campbell, and I. Ghosh (2011) A Comprehensive panel of turn-on caspase biosensors for investigating caspase specificity and caspase activation pathways. Chem. Bio-Chem. 12:2353-2364.
    • (2011) Chem. Bio-Chem. , vol.12 , pp. 2353-2364
    • Shekhawat, S.S.1    Campbell, S.T.2    Ghosh, I.3
  • 42
    • 38949201630 scopus 로고    scopus 로고
    • Specific and sensitive detection of nucleic acids and RNases using gold nanoparticle-RNA-fluorescent dye conjugates
    • Kim, J. H., R. A. Estabrook, G Braun, B. R. Lee, and N. O. Reich (2007) Specific and sensitive detection of nucleic acids and RNases using gold nanoparticle-RNA-fluorescent dye conjugates. Chem. Commun. 42:4342-4344.
    • (2007) Chem. Commun. , vol.42 , pp. 4342-4344
    • Kim, J.H.1    Estabrook, R.A.2    Braun, G.3    Lee, B.R.4    Reich, N.O.5
  • 43
    • 73949112081 scopus 로고    scopus 로고
    • Proteolytic fluorescent signal amplification on gold nanoparticles for a highly sensitive and rapid protease assay
    • Kim, J. H. and B. H. Chung (2010) Proteolytic fluorescent signal amplification on gold nanoparticles for a highly sensitive and rapid protease assay. Small 6:126-131.
    • (2010) Small , vol.6 , pp. 126-131
    • Kim, J.H.1    Chung, B.H.2


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