메뉴 건너뛰기




Volumn 11, Issue 12, 2012, Pages 5763-5772

Protein profiling of active cysteine cathepsins in living cells using an activity-based probe containing a cell-penetrating peptide

Author keywords

activity based probe; cathepsin; cell penetrating peptide; living cell; proteomics

Indexed keywords

BIOTIN; CATHEPSIN; CATHEPSIN B; CATHEPSIN F; CATHEPSIN H; CATHEPSIN K; CATHEPSIN L; CATHEPSIN S; CATHEPSIN X; CELL PENETRATING PEPTIDE; CELL PERMEABLE ACTIVITY BASED PROBE; CYSTEINE; DIPEPTIDYL PEPTIDASE I; MESSENGER RNA; UNCLASSIFIED DRUG;

EID: 84870923936     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr300575u     Document Type: Article
Times cited : (10)

References (46)
  • 1
    • 50649112213 scopus 로고    scopus 로고
    • Activity-based protein profiling: From enzyme chemistry to proteomic chemistry
    • Cravatt, B. F.; Wright, A. T.; Kozarich, J. W. Activity-based protein profiling: from enzyme chemistry to proteomic chemistry Annu. Rev. Biochem. 2008, 77, 383-414
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 383-414
    • Cravatt, B.F.1    Wright, A.T.2    Kozarich, J.W.3
  • 2
    • 0033604499 scopus 로고    scopus 로고
    • Active site-directed protein regulation
    • Kobe, B.; Kemp, B. E. Active site-directed protein regulation Nature 1999, 402 (6760) 373-6
    • (1999) Nature , vol.402 , Issue.6760 , pp. 373-376
    • Kobe, B.1    Kemp, B.E.2
  • 3
    • 33748595526 scopus 로고    scopus 로고
    • Mechanism-based profiling of enzyme families
    • Evans, M. J.; Cravatt, B. F. Mechanism-based profiling of enzyme families Chem. Rev. 2006, 106 (8) 3279-301
    • (2006) Chem. Rev. , vol.106 , Issue.8 , pp. 3279-3301
    • Evans, M.J.1    Cravatt, B.F.2
  • 4
    • 0037307787 scopus 로고    scopus 로고
    • Chemical proteomics and its application to drug discovery
    • Jeffery, D. A.; Bogyo, M. Chemical proteomics and its application to drug discovery Curr. Opin. Biotechnol. 2003, 14 (1) 87-95
    • (2003) Curr. Opin. Biotechnol. , vol.14 , Issue.1 , pp. 87-95
    • Jeffery, D.A.1    Bogyo, M.2
  • 5
  • 6
    • 0037462106 scopus 로고    scopus 로고
    • Activity-based protein profiling in vivo using a copper(i)-catalyzed azide-alkyne [3 + 2] cycloaddition
    • Speers, A. E.; Adam, G. C.; Cravatt, B. F. Activity-based protein profiling in vivo using a copper(i)-catalyzed azide-alkyne [3 + 2] cycloaddition J. Am. Chem. Soc. 2003, 125 (16) 4686-7
    • (2003) J. Am. Chem. Soc. , vol.125 , Issue.16 , pp. 4686-4687
    • Speers, A.E.1    Adam, G.C.2    Cravatt, B.F.3
  • 7
    • 1942522084 scopus 로고    scopus 로고
    • Profiling enzyme activities in vivo using click chemistry methods
    • Speers, A. E.; Cravatt, B. F. Profiling enzyme activities in vivo using click chemistry methods Chem. Biol. 2004, 11, 535-46
    • (2004) Chem. Biol. , vol.11 , pp. 535-546
    • Speers, A.E.1    Cravatt, B.F.2
  • 8
    • 54349106665 scopus 로고    scopus 로고
    • Activity-based probes as a tool for functional proteomic analysis of proteases
    • Fonovic, M.; Bogyo, M. Activity-based probes as a tool for functional proteomic analysis of proteases Expert Rev. Proteomics 2008, 5, 721-30
    • (2008) Expert Rev. Proteomics , vol.5 , pp. 721-730
    • Fonovic, M.1    Bogyo, M.2
  • 12
    • 84155174682 scopus 로고    scopus 로고
    • Novel cell-penetrating peptides based on alpha-aminoxy acids
    • Ma, Y.; Yang, D.; Ma, Y.; Zhang, Y. H. Novel cell-penetrating peptides based on alpha-aminoxy acids ChemBioChem 2012, 13 (1) 73-9
    • (2012) ChemBioChem , vol.13 , Issue.1 , pp. 73-79
    • Ma, Y.1    Yang, D.2    Ma, Y.3    Zhang, Y.H.4
  • 13
    • 84862807323 scopus 로고    scopus 로고
    • Target delivery of a gene into the brain using the RVG29-oligoarginine peptide
    • Gong, C.; Li, X.; Xu, L.; Zhang, Y. H. Target delivery of a gene into the brain using the RVG29-oligoarginine peptide Biomaterials 2012, 33 (12) 3456-63
    • (2012) Biomaterials , vol.33 , Issue.12 , pp. 3456-3463
    • Gong, C.1    Li, X.2    Xu, L.3    Zhang, Y.H.4
  • 14
    • 84865343913 scopus 로고    scopus 로고
    • Direct cytosolic delivery of cargoes in vivo by a chimera consisting of d - And l -arginine residues
    • Ma, Y.; Gong, C.; Fan, F.; Luo, M.; Yang, F.; Zhang, Y. H. Direct cytosolic delivery of cargoes in vivo by a chimera consisting of d-and l -arginine residues J. Controlled Release 2012, 162 (2) 286-294
    • (2012) J. Controlled Release , vol.162 , Issue.2 , pp. 286-294
    • Ma, Y.1    Gong, C.2    Fan, F.3    Luo, M.4    Yang, F.5    Zhang, Y.H.6
  • 15
    • 84862650253 scopus 로고    scopus 로고
    • Labeling lysosomes and tracking lysosome-dependent apoptosis with a cell-permeable activity-based probe
    • Fan, F.; Nie, S.; Yang, D.; Luo, M.; Shi, H.; Zhang, Y. H. Labeling lysosomes and tracking lysosome-dependent apoptosis with a cell-permeable activity-based probe Bioconjugate Chem. 2012, 23, 1309-17
    • (2012) Bioconjugate Chem. , vol.23 , pp. 1309-1317
    • Fan, F.1    Nie, S.2    Yang, D.3    Luo, M.4    Shi, H.5    Zhang, Y.H.6
  • 17
    • 77449100648 scopus 로고    scopus 로고
    • Development of near-infrared fluorophore (NIRF)-labeled activity-based probes for in vivo imaging of legumain
    • Lee, J.; Bogyo, M. Development of near-infrared fluorophore (NIRF)-labeled activity-based probes for in vivo imaging of legumain ACS Chem. Biol. 2010, 5 (2) 233-43
    • (2010) ACS Chem. Biol. , vol.5 , Issue.2 , pp. 233-243
    • Lee, J.1    Bogyo, M.2
  • 18
    • 33947686680 scopus 로고    scopus 로고
    • Endocytosis targets exogenous material selectively to cathepsin S in live human dendritic cells, while cell-penetrating peptides mediate nonselective transport to cysteine cathepsins
    • Reich, M.; van Swieten, P. F.; Sommandas, V.; Kraus, M.; Fischer, R.; Weber, E.; Kalbacher, H.; Overkleeft, H. S.; Driessen, C. Endocytosis targets exogenous material selectively to cathepsin S in live human dendritic cells, while cell-penetrating peptides mediate nonselective transport to cysteine cathepsins J. Leukocyte Biol. 2007, 81, 990-1001
    • (2007) J. Leukocyte Biol. , vol.81 , pp. 990-1001
    • Reich, M.1    Van Swieten, P.F.2    Sommandas, V.3    Kraus, M.4    Fischer, R.5    Weber, E.6    Kalbacher, H.7    Overkleeft, H.S.8    Driessen, C.9
  • 19
  • 20
    • 79961138638 scopus 로고    scopus 로고
    • Multicolor, one- and two-photon imaging of enzymatic activities in live cells with fluorescently Quenched Activity-Based Probes (qABPs)
    • Hu, M.; Li, L.; Wu, H.; Su, Y.; Yang, P. Y.; Uttamchandani, M.; Xu, Q. H.; Yao, S. Q. Multicolor, one- and two-photon imaging of enzymatic activities in live cells with fluorescently Quenched Activity-Based Probes (qABPs) J. Am. Chem. Soc. 2011, 133 (31) 12009-20
    • (2011) J. Am. Chem. Soc. , vol.133 , Issue.31 , pp. 12009-12020
    • Hu, M.1    Li, L.2    Wu, H.3    Su, Y.4    Yang, P.Y.5    Uttamchandani, M.6    Xu, Q.H.7    Yao, S.Q.8
  • 21
    • 33749017931 scopus 로고    scopus 로고
    • Cysteine cathepsins: Multifunctional enzymes in cancer
    • Mohamed, M. M.; Sloane, B. F. Cysteine cathepsins: multifunctional enzymes in cancer Nat. Rev. Cancer 2006, 6 (10) 764-75
    • (2006) Nat. Rev. Cancer , vol.6 , Issue.10 , pp. 764-775
    • Mohamed, M.M.1    Sloane, B.F.2
  • 22
    • 0036882393 scopus 로고    scopus 로고
    • Human and parasitic papain-like cysteine proteases: Their role in physiology and pathology and recent developments in inhibitor design
    • Lecaille, F.; Kaleta, J.; Bromme, D. Human and parasitic papain-like cysteine proteases: their role in physiology and pathology and recent developments in inhibitor design Chem. Rev. 2002, 102 (12) 4459-88
    • (2002) Chem. Rev. , vol.102 , Issue.12 , pp. 4459-4488
    • Lecaille, F.1    Kaleta, J.2    Bromme, D.3
  • 23
    • 13844275008 scopus 로고    scopus 로고
    • An improved preparation of the activity-based probe JPM-OEt and in situ applications
    • Chehade, K. A. H.; Baruch, A.; Verhelst, S. H. L.; Bogyo, M. An improved preparation of the activity-based probe JPM-OEt and in situ applications Synthesis 2005, 2, 240-4
    • (2005) Synthesis , vol.2 , pp. 240-244
    • Chehade, K.A.H.1    Baruch, A.2    Verhelst, S.H.L.3    Bogyo, M.4
  • 24
    • 21044447609 scopus 로고    scopus 로고
    • Solid-phase synthesis of double-headed epoxysuccinyl activity-based probes for selective targeting of papain family cysteine proteases
    • Verhelst, S. H.; Bogyo, M. Solid-phase synthesis of double-headed epoxysuccinyl activity-based probes for selective targeting of papain family cysteine proteases ChemBioChem 2005, 6 (5) 824-7
    • (2005) ChemBioChem , vol.6 , Issue.5 , pp. 824-827
    • Verhelst, S.H.1    Bogyo, M.2
  • 26
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • Eng, J. K.; McCormack, A. L.; Yates Iii, J. R. An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database J. Am. Soc. Mass Spectrom. 1994, 5 (11) 976-89
    • (1994) J. Am. Soc. Mass Spectrom. , vol.5 , Issue.11 , pp. 976-989
    • Eng, J.K.1    McCormack, A.L.2    Yates III, J.R.3
  • 27
    • 33847630405 scopus 로고    scopus 로고
    • Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry
    • Elias, J. E.; Gygi, S. P. Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry Nat. Methods 2007, 4 (3) 207-14
    • (2007) Nat. Methods , vol.4 , Issue.3 , pp. 207-214
    • Elias, J.E.1    Gygi, S.P.2
  • 28
    • 0037277179 scopus 로고    scopus 로고
    • Evaluation of multidimensional chromatography coupled with tandem mass spectrometry (LC/LC-MS/MS) for large-scale protein analysis: The yeast proteome
    • Peng, J.; Elias, J. E.; Thoreen, C. C.; Licklider, L. J.; Gygi, S. P. Evaluation of multidimensional chromatography coupled with tandem mass spectrometry (LC/LC-MS/MS) for large-scale protein analysis: the yeast proteome J. Proteome Res. 2003, 2 (1) 43-50
    • (2003) J. Proteome Res. , vol.2 , Issue.1 , pp. 43-50
    • Peng, J.1    Elias, J.E.2    Thoreen, C.C.3    Licklider, L.J.4    Gygi, S.P.5
  • 29
    • 0033835372 scopus 로고    scopus 로고
    • Epoxide electrophiles as activity-dependent cysteine protease profiling and discovery tools
    • Greenbaum, D.; Medzihradszky, K. F.; Burlingame, A.; Bogyo, M. Epoxide electrophiles as activity-dependent cysteine protease profiling and discovery tools Chem. Biol. 2000, 7 (8) 569-81
    • (2000) Chem. Biol. , vol.7 , Issue.8 , pp. 569-581
    • Greenbaum, D.1    Medzihradszky, K.F.2    Burlingame, A.3    Bogyo, M.4
  • 30
    • 0028276836 scopus 로고
    • A convenient synthesis of optically pure (2R,3R)-2,3-epoxysuccinyl- dipeptides
    • Korn, A.; Rudolph-Böhner, S.; Moroder, L. A convenient synthesis of optically pure (2R,3R)-2,3-epoxysuccinyl-dipeptides Tetrahedron 1994, 50 (28) 8381-92
    • (1994) Tetrahedron , vol.50 , Issue.28 , pp. 8381-8392
    • Korn, A.1    Rudolph-Böhner, S.2    Moroder, L.3
  • 31
    • 0034054576 scopus 로고    scopus 로고
    • Selective targeting of lysosomal cysteine proteases with radiolabeled electrophilic substrate analogs
    • Bogyo, M.; Verhelst, S.; Bellingard-Dubouchaud, V.; Toba, S.; Greenbaum, D. Selective targeting of lysosomal cysteine proteases with radiolabeled electrophilic substrate analogs Chem. Biol. 2000, 7 (1) 27-38
    • (2000) Chem. Biol. , vol.7 , Issue.1 , pp. 27-38
    • Bogyo, M.1    Verhelst, S.2    Bellingard-Dubouchaud, V.3    Toba, S.4    Greenbaum, D.5
  • 32
    • 13844256697 scopus 로고    scopus 로고
    • Transmembrane delivery of protein and peptide drugs by TAT-mediated transduction in the treatment of cancer
    • Wadia, J. S.; Dowdy, S. F. Transmembrane delivery of protein and peptide drugs by TAT-mediated transduction in the treatment of cancer Adv. Drug Delivery Rev. 2005, 57 (4) 579-96
    • (2005) Adv. Drug Delivery Rev. , vol.57 , Issue.4 , pp. 579-596
    • Wadia, J.S.1    Dowdy, S.F.2
  • 33
    • 80052715103 scopus 로고    scopus 로고
    • Comparative protein expression in different strains of the bloom-forming cyanobacterium Microcystis aeruginosa
    • 003749
    • Alexova, R.; Haynes, P. A.; Ferrari, B. C.; Neilan, B. A. Comparative protein expression in different strains of the bloom-forming cyanobacterium Microcystis aeruginosa Mol. Cell. Proteomics 2011, 10 (9) M110 003749
    • (2011) Mol. Cell. Proteomics , vol.10 , Issue.9 , pp. 110
    • Alexova, R.1    Haynes, P.A.2    Ferrari, B.C.3    Neilan, B.A.4
  • 37
    • 13844272399 scopus 로고    scopus 로고
    • Membrane-permeable arginine-rich peptides and the translocation mechanisms
    • Futaki, S. Membrane-permeable arginine-rich peptides and the translocation mechanisms Adv. Drug Delivery Rev. 2005, 57 (4) 547-58
    • (2005) Adv. Drug Delivery Rev. , vol.57 , Issue.4 , pp. 547-558
    • Futaki, S.1
  • 38
    • 60649108749 scopus 로고    scopus 로고
    • The integral membrane of lysosomes: Its proteins and their roles in disease
    • Callahan, J. W.; Bagshaw, R. D.; Mahuran, D. J. The integral membrane of lysosomes: its proteins and their roles in disease J. Proteomics 2009, 72 (1) 23-33
    • (2009) J. Proteomics , vol.72 , Issue.1 , pp. 23-33
    • Callahan, J.W.1    Bagshaw, R.D.2    Mahuran, D.J.3
  • 40
    • 15444379089 scopus 로고    scopus 로고
    • Syntaxin 6 and Vti1b form a novel SNARE complex, which is up-regulated in activated macrophages to facilitate exocytosis of tumor necrosis factor-alpha
    • Murray, R. Z.; Wylie, F. G.; Khromykh, T.; Hume, D. A.; Stow, J. L. Syntaxin 6 and Vti1b form a novel SNARE complex, which is up-regulated in activated macrophages to facilitate exocytosis of tumor necrosis factor-alpha J. Biol. Chem. 2005, 280 (11) 10478-83
    • (2005) J. Biol. Chem. , vol.280 , Issue.11 , pp. 10478-10483
    • Murray, R.Z.1    Wylie, F.G.2    Khromykh, T.3    Hume, D.A.4    Stow, J.L.5
  • 41
    • 28844469794 scopus 로고    scopus 로고
    • Elevated levels of the 64-kDa cleavage stimulatory factor (CstF-64) in lipopolysaccharide-stimulated macrophages influence gene expression and induce alternative poly(A) site selection
    • Shell, S. A.; Hesse, C.; Morris, S. M., Jr.; Milcarek, C. Elevated levels of the 64-kDa cleavage stimulatory factor (CstF-64) in lipopolysaccharide- stimulated macrophages influence gene expression and induce alternative poly(A) site selection J. Biol. Chem. 2005, 280 (48) 39950-61
    • (2005) J. Biol. Chem. , vol.280 , Issue.48 , pp. 39950-39961
    • Shell, S.A.1    Hesse, C.2    Morris, Jr.S.M.3    Milcarek, C.4
  • 42
    • 67349214659 scopus 로고    scopus 로고
    • Dose-dependent transitions in Nrf2-mediated adaptive response and related stress responses to hypochlorous acid in mouse macrophages
    • Woods, C. G.; Fu, J.; Xue, P.; Hou, Y.; Pluta, L. J.; Yang, L.; Zhang, Q.; Thomas, R. S.; Andersen, M. E.; Pi, J. Dose-dependent transitions in Nrf2-mediated adaptive response and related stress responses to hypochlorous acid in mouse macrophages Toxicol. Appl. Pharmacol. 2009, 238 (1) 27-36
    • (2009) Toxicol. Appl. Pharmacol. , vol.238 , Issue.1 , pp. 27-36
    • Woods, C.G.1    Fu, J.2    Xue, P.3    Hou, Y.4    Pluta, L.J.5    Yang, L.6    Zhang, Q.7    Thomas, R.S.8    Andersen, M.E.9    Pi, J.10
  • 43
    • 33646594411 scopus 로고    scopus 로고
    • A selective activity-based probe for the papain family cysteine protease dipeptidyl peptidase I/cathepsin C
    • Yuan, F.; Verhelst, S. H.; Blum, G.; Coussens, L. M.; Bogyo, M. A selective activity-based probe for the papain family cysteine protease dipeptidyl peptidase I/cathepsin C J. Am. Chem. Soc. 2006, 128 (17) 5616-7
    • (2006) J. Am. Chem. Soc. , vol.128 , Issue.17 , pp. 5616-5617
    • Yuan, F.1    Verhelst, S.H.2    Blum, G.3    Coussens, L.M.4    Bogyo, M.5
  • 44
    • 17944366493 scopus 로고    scopus 로고
    • Structure of human dipeptidyl peptidase i (cathepsin C): Exclusion domain added to an endopeptidase framework creates the machine for activation of granular serine proteases
    • Turk, D.; Janjic, V.; Stern, I.; Podobnik, M.; Lamba, D.; Dahl, S. W.; Lauritzen, C.; Pedersen, J.; Turk, V.; Turk, B. Structure of human dipeptidyl peptidase I (cathepsin C): exclusion domain added to an endopeptidase framework creates the machine for activation of granular serine proteases EMBO J. 2001, 20 (23) 6570-82
    • (2001) EMBO J. , vol.20 , Issue.23 , pp. 6570-6582
    • Turk, D.1    Janjic, V.2    Stern, I.3    Podobnik, M.4    Lamba, D.5    Dahl, S.W.6    Lauritzen, C.7    Pedersen, J.8    Turk, V.9    Turk, B.10
  • 46
    • 34248175825 scopus 로고    scopus 로고
    • Catch-and-release reagents for broadscale quantitative proteomics analyses
    • Gartner, C. A.; Elias, J. E.; Bakalarski, C. E.; Gygi, S. P. Catch-and-release reagents for broadscale quantitative proteomics analyses J. Proteome Res. 2007, 6 (4) 1482-91
    • (2007) J. Proteome Res. , vol.6 , Issue.4 , pp. 1482-1491
    • Gartner, C.A.1    Elias, J.E.2    Bakalarski, C.E.3    Gygi, S.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.