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Volumn 424, Issue 2, 2012, Pages 130-136

Fluorometric detection of protein kinase Cα activity based on phosphorylation-induced dissociation of a polyion complex

Author keywords

Cell based assay; Fluorometric detection; Polyion complex; Protein kinase

Indexed keywords

DISSOCIATION; ENERGY TRANSFER; ENZYMES; FLUORESCENCE QUENCHING; INFRARED DEVICES; PEPTIDES; PHOSPHORYLATION; SULFUR COMPOUNDS;

EID: 84859042294     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2012.01.036     Document Type: Article
Times cited : (6)

References (43)
  • 1
    • 0034614490 scopus 로고    scopus 로고
    • Signaling - 2000 and beyond
    • T. Hunter Signaling - 2000 and beyond Cell 100 2000 113 127 (Pubitemid 30046300)
    • (2000) Cell , vol.100 , Issue.1 , pp. 113-127
    • Hunter, T.1
  • 2
    • 0034797512 scopus 로고    scopus 로고
    • The role of protein phosphorylation in human health and disease
    • P. Cohen The role of protein phosphorylation in human health and disease Eur. J. Biochem. 268 2001 5001 5010
    • (2001) Eur. J. Biochem. , vol.268 , pp. 5001-5010
    • Cohen, P.1
  • 3
    • 57749188299 scopus 로고    scopus 로고
    • Targeting cancer with small molecule kinase inhibitors
    • J. Zhang, P.L. Yang, and N.S. Gray Targeting cancer with small molecule kinase inhibitors Nat. Rev. Cancer 9 2009 28 39
    • (2009) Nat. Rev. Cancer , vol.9 , pp. 28-39
    • Zhang, J.1    Yang, P.L.2    Gray, N.S.3
  • 4
    • 75149130051 scopus 로고    scopus 로고
    • Targeting the cancer kinome through polypharmacology
    • Z.A. Knight, H. Lin, and K.M. Shokat Targeting the cancer kinome through polypharmacology Nat. Rev. Cancer 10 2010 130 137
    • (2010) Nat. Rev. Cancer , vol.10 , pp. 130-137
    • Knight, Z.A.1    Lin, H.2    Shokat, K.M.3
  • 5
    • 67650073265 scopus 로고    scopus 로고
    • Cell cycle kinases as therapeutic targets for cancer
    • S. Lapenna, and A. Giordano Cell cycle kinases as therapeutic targets for cancer Nat. Rev. Drug Discov. 8 2009 547 566
    • (2009) Nat. Rev. Drug Discov. , vol.8 , pp. 547-566
    • Lapenna, S.1    Giordano, A.2
  • 8
    • 70849083521 scopus 로고    scopus 로고
    • Plasma protein kinase C (PKC) α as a biomarker for the diagnosis of cancers
    • J.H. Kang, D. Asai, R. Toita, H. Kitazaki, and Y. Katayama Plasma protein kinase C (PKC) α as a biomarker for the diagnosis of cancers Carcinogenesis 30 2009 1927 1931
    • (2009) Carcinogenesis , vol.30 , pp. 1927-1931
    • Kang, J.H.1    Asai, D.2    Toita, R.3    Kitazaki, H.4    Katayama, Y.5
  • 9
    • 0037620455 scopus 로고    scopus 로고
    • A homogeneous, nonradioactive high-throughput fluorogenic protein kinase assay
    • DOI 10.1016/S0003-2697(03)00094-0
    • K. Kupcho, R. Somberg, B. Bulleit, and S.A. Goueli A homogeneous, nonradioactive high-throughput fluorogenic protein kinase assay Anal. Biochem. 317 2003 210 217 (Pubitemid 36577630)
    • (2003) Analytical Biochemistry , vol.317 , Issue.2 , pp. 210-217
    • Kupcho, K.1    Somberg, R.2    Bulleit, B.3    Goueli, S.A.4
  • 11
    • 0033541662 scopus 로고    scopus 로고
    • Homogeneous proximity tyrosine kinase assays: Scintillation proximity assay versus homogeneous time-resolved fluorescence
    • DOI 10.1006/abio.1999.4029
    • Y.W. Park, R.T. Cummings, L. Wu, S. Zheng, P.M. Cameron, A. Woods, D.M. Zaller, A.I. Marcy, and J.D. Hermes Homogeneous proximity tyrosine kinase assays: scintillation proximity assay versus homogeneous time-resolved fluorescence Anal. Biochem. 269 1999 94 104 (Pubitemid 29174266)
    • (1999) Analytical Biochemistry , vol.269 , Issue.1 , pp. 94-104
    • Park, Y.-W.1    Cummings, R.T.2    Wu, L.3    Zheng, S.4    Cameron, P.M.5    Woods, A.6    Zaller, D.M.7    Marcy, A.I.8    Hermes, J.D.9
  • 12
    • 2442521478 scopus 로고    scopus 로고
    • Use of red-shifted dyes in a fluorescence polarization AKT kinase assay for detection of biological activity in natural product extracts
    • T.C. Turek-Etienne, M. Lei, J.S. Terracciano, E.F. Langsdorf, R.W. Bryant, R.F. Hart, and A.C. Horan Use of red-shifted dyes in a fluorescence polarization AKT kinase assay for detection of biological activity in natural product extracts J. Biomol. Screen. 9 2004 52 61
    • (2004) J. Biomol. Screen. , vol.9 , pp. 52-61
    • Turek-Etienne, T.C.1    Lei, M.2    Terracciano, J.S.3    Langsdorf, E.F.4    Bryant, R.W.5    Hart, R.F.6    Horan, A.C.7
  • 13
    • 18644384952 scopus 로고    scopus 로고
    • An evaluation of fluorescence polarization and lifetime discriminated polarization for high throughput screening of serine/threonine kinases
    • DOI 10.1016/S0003-2697(02)00245-2, PII S0003269702002452
    • A. Fowler, D. Swift, E. Longman, A. Acornley, P. Hemsley, D. Murray, J. Unitt, I. Dale, E. Sullivan, and M. Coldwell An evaluation of fluorescence polarization and lifetime discriminated polarization for high throughput screening of serine/threonine kinases Anal. Biochem. 308 2002 223 231 (Pubitemid 35177133)
    • (2002) Analytical Biochemistry , vol.308 , Issue.2 , pp. 223-231
    • Fowler, A.1    Swift, D.2    Longman, E.3    Acornley, A.4    Hemsley, P.5    Murray, D.6    Unitt, J.7    Dale, I.8    Sullivan, E.9    Coldwell, M.10
  • 14
    • 0035576787 scopus 로고    scopus 로고
    • Development and validation of a competitive AKT serine/threonine kinase fluorescence polarization assay using a product-specific anti-phospho-serine antibody
    • DOI 10.1006/abio.2001.5412
    • T.C. Turek, E.C. Small, R.W. Bryant, and W.A.G. Hill Development and validation of a competitive AKT serine/threonine kinase fluorescence polarization assay using a product-specific anti-phospho-serine antibody Anal. Biochem. 299 2001 45 53 (Pubitemid 33124126)
    • (2001) Analytical Biochemistry , vol.299 , Issue.1 , pp. 45-53
    • Turek, T.C.1    Small, E.C.2    Bryant, R.W.3    Adam, W.4    Hill, G.5
  • 15
    • 77953318642 scopus 로고    scopus 로고
    • Probing protein kinase (CK2) and alkaline phosphatase with CdSe/ZnS quantum dots
    • R. Freeman, T. Finder, R. Gill, and I. Willner Probing protein kinase (CK2) and alkaline phosphatase with CdSe/ZnS quantum dots Nano Lett. 10 2010 2192 2196
    • (2010) Nano Lett. , vol.10 , pp. 2192-2196
    • Freeman, R.1    Finder, T.2    Gill, R.3    Willner, I.4
  • 16
    • 78650161677 scopus 로고    scopus 로고
    • Protein kinase-actuated resonance energy transfer in quantum dot-peptide conjugates
    • J.E. Ghadiali, B.E. Cohen, and M.M. Stevens Protein kinase-actuated resonance energy transfer in quantum dot-peptide conjugates ACS Nano 4 2010 4915 4919
    • (2010) ACS Nano , vol.4 , pp. 4915-4919
    • Ghadiali, J.E.1    Cohen, B.E.2    Stevens, M.M.3
  • 17
    • 33947266913 scopus 로고    scopus 로고
    • Deep quench: An expanded dynamic range for protein kinase sensors
    • DOI 10.1021/ja068280r
    • V.R. Sharma, S. Agnes, and D.S. Lawrence Deep quench: an expanded dynamic range for protein kinase sensors J. Am. Chem. Soc. 129 2007 2742 2743 (Pubitemid 46417936)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.10 , pp. 2742-2743
    • Sharma, V.1    Agnes, R.S.2    Lawrence, D.S.3
  • 19
    • 0344443386 scopus 로고    scopus 로고
    • Versatile Fluorescence Probes of Protein Kinase Activity
    • DOI 10.1021/ja0380502
    • M.D. Shults, and B. Imperiali Versatile fluorescence probes of protein kinase activity J. Am. Chem. Soc. 125 2003 14248 14249 (Pubitemid 37452343)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.47 , pp. 14248-14249
    • Shults, M.D.1    Imperiali, B.2
  • 20
    • 18744408814 scopus 로고    scopus 로고
    • A multiplexed homogeneous fluorescence-based assay for protein kinase activity in cell lysates
    • M.D. Shults, K.A. Janes, D.A. Lauffenburg, and B. Imperiali A multiplexed homogeneous fluorescence-based assay for protein kinase activity in cell lysates Nat. Methods 2 2005 277 284
    • (2005) Nat. Methods , vol.2 , pp. 277-284
    • Shults, M.D.1    Janes, K.A.2    Lauffenburg, D.A.3    Imperiali, B.4
  • 21
    • 33646164175 scopus 로고    scopus 로고
    • Optimal sox-based fluorescent chemosensor design for serine/threonine protein kinases
    • M.D. Shults, D.C. Moniz, and B. Imperiali Optimal sox-based fluorescent chemosensor design for serine/threonine protein kinases Anal. Biochem. 352 2006 198 207
    • (2006) Anal. Biochem. , vol.352 , pp. 198-207
    • Shults, M.D.1    Moniz, D.C.2    Imperiali, B.3
  • 22
    • 52449096942 scopus 로고    scopus 로고
    • Recognition-domain focused chemosensors: Versatile and efficient reporters of protein kinase activity
    • E. Luković, J.A. González-Vera, and B. Imperiali Recognition-domain focused chemosensors: versatile and efficient reporters of protein kinase activity J. Am. Chem. Soc. 130 2008 12821 12827
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 12821-12827
    • Luković, E.1    González-Vera, J.A.2    Imperiali, B.3
  • 27
    • 34447125846 scopus 로고    scopus 로고
    • Phosphate-mediated molecular memory driven by two different protein kinases as information input elements
    • DOI 10.1021/ja0703067
    • K. Tomozaki, and H. Mihara Phosphate-mediated molecular memory driven by two different protein kinases as information input elements J. Am. Chem. Soc. 129 2007 8345 8352 (Pubitemid 47035145)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.26 , pp. 8345-8352
    • Tomizaki, K.-Y.1    Mihara, H.2
  • 28
    • 34249053810 scopus 로고    scopus 로고
    • Design of a hybrid biosensor for enhanced phosphopeptide recognition based on a phosphoprotein binding domain coupled with a fluorescent biosensor
    • T. Anai, E. Nakata, Y. Koshi, A. Ojida, and I. Hamachi Design of a hybrid biosensor for enhanced phosphopeptide recognition based on a phosphoprotein binding domain coupled with a fluorescent biosensor J. Am. Chem. Soc. 129 2007 6232 6239
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 6232-6239
    • Anai, T.1    Nakata, E.2    Koshi, Y.3    Ojida, A.4    Hamachi, I.5
  • 29
    • 80051741287 scopus 로고    scopus 로고
    • Fluorescent nanoparticles consisting of lipopeptides and fluorescein-modified polyanions for monitoring of protein kinase activity
    • H. Koga, R. Toita, T. Mori, T. Tomiyama, J.H. Kang, T. Niidome, and Y. Katayama Fluorescent nanoparticles consisting of lipopeptides and fluorescein-modified polyanions for monitoring of protein kinase activity Bioconjug. Chem. 22 2011 1526 1534
    • (2011) Bioconjug. Chem. , vol.22 , pp. 1526-1534
    • Koga, H.1    Toita, R.2    Mori, T.3    Tomiyama, T.4    Kang, J.H.5    Niidome, T.6    Katayama, Y.7
  • 30
    • 0030762437 scopus 로고    scopus 로고
    • The potential for isoenzyme-selective modulation of protein kinase C
    • J. Hofmann The potential for isoenzyme-selective modulation of protein kinase C FASEB J. 11 1997 649 667
    • (1997) FASEB J. , vol.11 , pp. 649-667
    • Hofmann, J.1
  • 31
    • 1542619344 scopus 로고    scopus 로고
    • Protein Kinase C Isozymes as Potential Targets for Anticancer Therapy
    • DOI 10.2174/1568009043481579
    • J. Hofmann Protein kinase C isozymes as potential targets for anti-cancer therapy Curr. Cancer Drug Targets 4 2004 125 146 (Pubitemid 38332552)
    • (2004) Current Cancer Drug Targets , vol.4 , Issue.2 , pp. 125-146
    • Hofmann, J.1
  • 32
    • 34250902930 scopus 로고    scopus 로고
    • Targeting the protein kinase C family: Are we there yet?
    • DOI 10.1038/nrc2168, PII NRC2168
    • H.J. Mackay, and C.J. Twelves Targeting the protein kinase C family: are we there yet? Nat. Rev. Cancer 7 2007 554 562 (Pubitemid 46985395)
    • (2007) Nature Reviews Cancer , vol.7 , Issue.7 , pp. 554-562
    • Mackay, H.J.1    Twelves, C.J.2
  • 34
    • 44649102706 scopus 로고    scopus 로고
    • A short peptide is a protein kinase C (PKC) α-specific substrate
    • DOI 10.1002/pmic.200701045
    • J.H. Kang, D. Asai, S. Yamada, R. Toita, J. Oishi, T. Mori, T. Niidome, and Y. Katayama A short peptide is a protein kinase C (PKC) α - specific substrate Proteomics 8 2008 2006 2011 (Pubitemid 351775780)
    • (2008) Proteomics , vol.8 , Issue.10 , pp. 2006-2011
    • Kang, J.-H.1    Asai, D.2    Yamada, S.3    Toita, R.4    Oishi, J.5    Mori, T.6    Niidome, T.7    Katayama, Y.8
  • 35
    • 0017235993 scopus 로고
    • On the determination of available lysine in casein and rapeseed protein concentrates using 2,4,6-trinitrobenzenesulphonic acid (TNBS) as a reagent for free epsilon amino group of lysine
    • A. Eklund On the determination of available lysine in casein and rapeseed protein concentrates using 2,4,6-trinitrobenzenesulphonic acid (TNBS) as a reagent for free epsilon amino group of lysine Anal. Biochem. 70 1976 434 439
    • (1976) Anal. Biochem. , vol.70 , pp. 434-439
    • Eklund, A.1
  • 36
    • 0028295796 scopus 로고
    • Resonance energy transfer: Methods and applications
    • DOI 10.1006/abio.1994.1134
    • P. Wu, and L. Brand Resonance energy transfer: methods and applications Anal. Biochem. 218 1994 1 13 (Pubitemid 24124740)
    • (1994) Analytical Biochemistry , vol.218 , Issue.1 , pp. 1-13
    • Wu, P.1    Brand, L.2
  • 37
    • 33847398652 scopus 로고    scopus 로고
    • Immobilized molecular beacons: A new strategy using UV-activated poly(methyl methacrylate) surfaces to provide large fluorescence sensitivities for reporting on molecular association events
    • DOI 10.1016/j.ab.2006.12.029, PII S0003269706009237
    • C. Situma, A.J. Moehring, M.A.F. Noor, and S.A. Soper Immobilized molecular beacons: a new strategy using UV-activated poly(methyl methacrylate) surfaces to provide large fluorescence sensitivities for reporting on molecular association events Anal. Biochem. 363 2007 35 45 (Pubitemid 46348970)
    • (2007) Analytical Biochemistry , vol.363 , Issue.1 , pp. 35-45
    • Situma, C.1    Moehring, A.J.2    Noor, M.A.F.3    Soper, S.A.4
  • 38
    • 0037099395 scopus 로고    scopus 로고
    • A stepwise huisgen cycloaddition process: Copper(I)-catalyzed regioselective 'ligation' of azides and terminal alkynes
    • DOI 10.1002/1521-3773(20020715)41:14<2596::AID-ANIE2596>3.0.CO;2-4
    • V.V. Rostovtsev, L.G. Green, V.V. Fokin, and K.B. Sharpless A stepwise cycloaddition process: copper(I)-catalyzed regioselective "ligation" of azides and terminal alkynes Angew. Chem. Int. Ed. 41 2002 2596 2599 (Pubitemid 34803480)
    • (2002) Angewandte Chemie - International Edition , vol.41 , Issue.14 , pp. 2596-2599
    • Rostovtsev, V.V.1    Green, L.G.2    Fokin, V.V.3    Sharpless, K.B.4
  • 39
    • 51049094897 scopus 로고    scopus 로고
    • Cu-catalyzed azide-alkyne cycloaddition
    • M. Meldal, and C.W. Tornøe Cu-catalyzed azide-alkyne cycloaddition Chem. Rev. 108 2008 2952 3015
    • (2008) Chem. Rev. , vol.108 , pp. 2952-3015
    • Meldal, M.1    Tornøe, C.W.2
  • 40
    • 0027248964 scopus 로고
    • Isoenzyme specificity of bisindolylmaleimides, selective inhibitors of protein kinase C
    • S.E. Wilkinson, P.J. Parker, and J.S. Nixon Isozyme specificity of bisindolylmaleimides, selective inhibitors of protein kinase C Biochem. J. 294 1993 335 337 (Pubitemid 23268828)
    • (1993) Biochemical Journal , vol.294 , Issue.2 , pp. 335-337
    • Wilkinson, S.E.1    Parker, P.J.2    Nixon, J.S.3
  • 41
    • 0029833019 scopus 로고    scopus 로고
    • Treatment of glioblastoma U-87 by systemic administration of an antisense protein kinase C-α phosphorothioate oligodeoxynucleotide
    • T. Yazaki, S. Ahmad, A. Chahlavi, E.Z. Katz, N.M. Dean, S.D. Rabkin, R.L. Martuza, and R.I. Glazer Treatment of glioblastoma U87 by systemic administration of an antisense protein kinase Cα phosphorothioate oligonucleotides Mol. Pharmcol. 50 1996 236 242 (Pubitemid 26265126)
    • (1996) Molecular Pharmacology , vol.50 , Issue.2 , pp. 236-242
    • Yazaki, T.1    Ahmad, S.2    Chahlavi, A.3    Zylber-Katz, E.4    Dean, N.M.5    Rabkin, S.D.6    Martuza, R.L.7    Glazer, R.I.8
  • 43
    • 0034306450 scopus 로고    scopus 로고
    • Specificity and mechanism of action of some commonly used protein kinase inhibitors
    • S.P. Davies, H. Reddy, M. Caivano, and P. Cohen Specificity and mechanism of action of some commonly used protein kinase inhibitors Biochem. J. 351 2000 95 105
    • (2000) Biochem. J. , vol.351 , pp. 95-105
    • Davies, S.P.1    Reddy, H.2    Caivano, M.3    Cohen, P.4


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