메뉴 건너뛰기




Volumn 116, Issue 1, 2011, Pages 1-19

Imaging of protease functions- Current guide to spotting cysteine cathepsins in classical and novel scenes of action in mammalian epithelial cells and tissues

Author keywords

Activity based probes; Endo lysosomal proteases; Enzyme cytochemistry; Green fluorescent protein; Immunofluorescence; Protein trafficking

Indexed keywords

CATHEPSIN; CYSTEINE PROTEINASE;

EID: 84860389887     PISSN: 11226714     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (15)

References (91)
  • 2
    • 0023189459 scopus 로고
    • Identification of the probable inhibitory reactive sites of the cysteine proteinase inhibitors human cystatin C and chicken cystatin
    • Abrahamson M., Ritonja A., Brown M. A., Grubb A., Machleidt W., Barrett A.J. (1987) Identification of the probable inhibitory reactive sites of the cysteine proteinase inhibitors human cystatin C and chicken cystatin. J. Biol. Chem. 262: 9688-9694. (Pubitemid 17102616)
    • (1987) Journal of Biological Chemistry , vol.262 , Issue.20 , pp. 9688-9694
    • Abrahamson, M.1    Ritonja, A.2    Brown, M.A.3
  • 3
    • 0034256042 scopus 로고    scopus 로고
    • Regulated secretion of conventional lysosomes
    • DOI 10.1016/S0962-8924(00)01794-3, PII S0962892400017943
    • Andrews N.W. (2000) Regulated secretion of conventional lysosomes. Trends Cell Biol. 10: 316-321. (Pubitemid 30445238)
    • (2000) Trends in Cell Biology , vol.10 , Issue.8 , pp. 316-321
    • Andrews, N.W.1
  • 4
    • 0022896891 scopus 로고
    • The cystatins: A diverse superfamily of cysteine peptidase inhibitors
    • Barrett A.J. (1986) The cystatins: a diverse superfamily of cysteine peptidase inhibitors. Biomed. Biochim. Acta 45: 1363-1374. (Pubitemid 17018565)
    • (1986) Biomedica Biochimica Acta , vol.45 , Issue.11-12 , pp. 1363-1374
    • Barrett, A.J.1
  • 5
    • 0019948262 scopus 로고
    • L-trans-Epoxysuccinyl-leucylamido(4-guanidino)butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins, B, H and L
    • Barrett A.J., Kembhavi A.A., Brown M.A., Kirschke H., Knight C.G., Tamai M., Hanada K. (1982) L-trans-Epoxysuccinyl-leucylamido(4-guanidino)butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins B, H and L. Biochem. J. 201: 189-198. (Pubitemid 12038477)
    • (1982) Biochemical Journal , vol.201 , Issue.1 , pp. 189-198
    • Barrett, A.J.1    Kembhavi, A.A.2    Brown, M.A.3
  • 6
    • 0019720180 scopus 로고
    • E-64 [L-trans-epoxysuccinyl-leucyl-amido(4-guanidino)butane] and related epoxides as inhibitors of cysteine proteinases
    • Barrett A.J., Kembhavi A.A., Hanada K. (1981) E-64 [L-trans- epoxysuccinyl-leucylamido( 4-guanidino)butane] and related epoxides as inhibitors of cysteine proteinases. Acta Biol. Med. Ger. 40: 1513-1517. (Pubitemid 12022366)
    • (1981) Acta Biologica et Medica Germanica , vol.40 , Issue.10-11 , pp. 1513-1517
    • Barrett, A.J.1    Kembhavi, A.A.2    Hanada, K.3
  • 7
    • 0034930561 scopus 로고    scopus 로고
    • Evolutionary lines of cysteine peptidases
    • DOI 10.1515/BC.2001.088
    • Barrett A.J., Rawlings N.D. (2001) Evolutionary lines of cysteine peptidases. Biol. Chem. 382: 727-733. (Pubitemid 32631709)
    • (2001) Biological Chemistry , vol.382 , Issue.5 , pp. 727-733
    • Barrett, A.J.1    Rawlings, N.D.2
  • 9
    • 12444288446 scopus 로고    scopus 로고
    • Cathepsin S controls MHC class II-mediated antigen presentation by epithelial cells in vivo
    • Beers C., Burich A., Kleijmeer M.J., Griffith J.M., Wong P., Rudensky A.Y. (2005) Cathepsin S controls MHC class II-mediated antigen presentation by epithelial cells in vivo. J. Immunol. 174: 1205-1212.
    • (2005) J. Immunol. , vol.174 , pp. 1205-1212
    • Beers, C.1    Burich, A.2    Kleijmeer, M.J.3    Griffith, J.M.4    Wong, P.5    Rudensky, A.Y.6
  • 10
    • 11144245547 scopus 로고    scopus 로고
    • Activity-based protein profiling: Applications to biomarker discovery, in vivo imaging and drug discovery
    • DOI 10.2165/00129785-200404060-00004
    • Berger A.B., Vitorino P.M., Bogyo M. (2004) Activity-based protein profiling: applications to biomarker discovery, in vivo imaging and drug discovery. Am. J. Pharmacogenomics 4: 371-381. (Pubitemid 40052846)
    • (2004) American Journal of PharmacoGenomics , vol.4 , Issue.6 , pp. 371-381
    • Berger, A.B.1    Vitorino, P.M.2    Bogyo, M.3
  • 11
    • 50249145214 scopus 로고    scopus 로고
    • Use of fluorescent imaging to investigate pathological protease activity
    • Blum G. (2008) Use of fluorescent imaging to investigate pathological protease activity. Curr. Opin. Drug Discov. Devel. 11: 708-716.
    • (2008) Curr. Opin. Drug Discov. Devel. , vol.11 , pp. 708-716
    • Blum, G.1
  • 13
    • 34548666006 scopus 로고    scopus 로고
    • Noninvasive optical imaging of cysteine protease activity using fluorescently quenched activity-based probes
    • DOI 10.1038/nchembio.2007.26, PII NCHEMBIO200726
    • Blum G., von Degenfeld G., Merchant M.J., Blau H.M., Bogyo M. (2007) Noninvasive optical imaging of cysteine protease activity using fluorescently quenched activitybased probes. Nat. Chem. Biol. 3: 668-677. (Pubitemid 47417706)
    • (2007) Nature Chemical Biology , vol.3 , Issue.10 , pp. 668-677
    • Blum, G.1    Von Degenfeld, G.2    Merchant, M.J.3    Blau, H.M.4    Bogyo, M.5
  • 14
    • 68149166462 scopus 로고    scopus 로고
    • Comparative assessment of substrates and activity based probes as tools for non-invasive optical imaging of cysteine protease activity
    • Blum G., Weimer R.M., Edgington L.E., Adams W., Bogyo M. (2009) Comparative assessment of substrates and activity based probes as tools for non-invasive optical imaging of cysteine protease activity. PLoS One 4: e6374.
    • (2009) PLoS One , vol.4
    • Blum, G.1    Weimer, R.M.2    Edgington, L.E.3    Adams, W.4    Bogyo, M.5
  • 15
    • 0024066065 scopus 로고
    • The 2.0 A X-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases
    • Bode W., Engh R., Musil D., Thiele U., Huber R., Karshikov A., Brzin J., Kos J., Turk V. (1988) The 2.0 A X-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases. Embo J. 7: 2593-2599.
    • (1988) Embo J. , vol.7 , pp. 2593-2599
    • Bode, W.1    Engh, R.2    Musil, D.3    Thiele, U.4    Huber, R.5    Karshikov, A.6    Brzin, J.7    Kos, J.8    Turk, V.9
  • 16
    • 0032542348 scopus 로고    scopus 로고
    • Antigen presentation. A protease draws first blood
    • Bogyo M., Ploegh H.L. (1998) Antigen presentation. A protease draws first blood. Nature 396: 625, 627.
    • (1998) Nature , vol.396 , Issue.625 , pp. 627
    • Bogyo, M.1    Ploegh, H.L.2
  • 17
    • 38649111363 scopus 로고    scopus 로고
    • Cysteine cathepsins: Cellular roadmap to different functions
    • DOI 10.1016/j.biochi.2007.07.024, PII S0300908407002003
    • Brix K., Dunkhorst A., Mayer K., Jordans S. (2008) Cysteine cathepsins: cellular roadmap to different functions. Biochimie 90: 194-207. (Pubitemid 351172569)
    • (2008) Biochimie , vol.90 , Issue.2 , pp. 194-207
    • Brix, K.1    Dunkhorst, A.2    Mayer, K.3    Jordans, S.4
  • 18
    • 0028280493 scopus 로고
    • Extrathyroidal release of thyroid hormones from thyroglobulin by J774 mouse macrophages
    • Brix K., Herzog V. (1994) Extrathyroidal release of thyroid hormones from thyroglobulin by J774 mouse macrophages. J. Clin. Invest. 93: 1388-1396. (Pubitemid 24116373)
    • (1994) Journal of Clinical Investigation , vol.93 , Issue.4 , pp. 1388-1396
    • Brix, K.1    Herzog, V.2
  • 19
    • 33644831206 scopus 로고    scopus 로고
    • Watching proteases in action
    • Brix K., Jordans S. (2005) Watching proteases in action. Nat Chem Biol. 1: 186-187.
    • (2005) Nat Chem Biol. , vol.1 , pp. 186-187
    • Brix, K.1    Jordans, S.2
  • 20
    • 0029996240 scopus 로고    scopus 로고
    • Evidence for extracellularly acting cathepsins mediating thyroid hormone liberation in thyroid epithelial cells
    • DOI 10.1210/en.137.5.1963
    • Brix K., Lemansky P., Herzog V. (1996) Evidence for extracellularly acting cathepsins mediating thyroid hormone liberation in thyroid epithelial cells. Endocrinology 137: 1963-1974. (Pubitemid 26139692)
    • (1996) Endocrinology , vol.137 , Issue.5 , pp. 1963-1974
    • Brix, K.1    Lemansky, P.2    Herzog, V.3
  • 21
    • 0034945881 scopus 로고    scopus 로고
    • Cysteine proteinases mediate extracellular prohormone processing in the thyroid
    • DOI 10.1515/BC.2001.087
    • Brix K., Linke M., Tepel C., Herzog V. (2001) Cysteine proteinases mediate extracellular prohormone processing in the thyroid. Biol. Chem. 382: 717-725. (Pubitemid 32631708)
    • (2001) Biological Chemistry , vol.382 , Issue.5 , pp. 717-725
    • Brix, K.1    Linke, M.2    Tepel, C.3    Herzog, V.4
  • 22
    • 67649628133 scopus 로고    scopus 로고
    • Cathepsin K inhibitors for osteoporosis and potential off-target effects
    • Bromme D., Lecaille F. (2009) Cathepsin K inhibitors for osteoporosis and potential off-target effects. Expert Opin. Investig. Drugs 18: 585-600.
    • (2009) Expert Opin. Investig. Drugs , vol.18 , pp. 585-600
    • Bromme, D.1    Lecaille, F.2
  • 25
    • 63049095880 scopus 로고    scopus 로고
    • Livecell imaging demonstrates extracellular matrix degradation in association with active cathepsin B in caveolae of endothelial cells during tube formation
    • Cavallo-Medved D., Rudy D., Blum G., Bogyo M., Caglic D., Sloane B.F. (2009) Livecell imaging demonstrates extracellular matrix degradation in association with active cathepsin B in caveolae of endothelial cells during tube formation. Exp. Cell Res. 315: 1234-1246.
    • (2009) Exp. Cell Res. , vol.315 , pp. 1234-1246
    • Cavallo-Medved, D.1    Rudy, D.2    Blum, G.3    Bogyo, M.4    Caglic, D.5    Sloane, B.F.6
  • 26
    • 0030970119 scopus 로고    scopus 로고
    • Emerging roles for cysteine proteases in human biology
    • DOI 10.1146/annurev.physiol.59.1.63
    • Chapman H.A., Riese R.J., Shi G.P. (1997) Emerging roles for cysteine proteases in human biology. Annu. Rev. Physiol. 59: 63-88. (Pubitemid 27142435)
    • (1997) Annual Review of Physiology , vol.59 , pp. 63-88
    • Chapman, H.A.1    Riese, R.J.2    Shi, G.-P.3
  • 27
    • 33744961634 scopus 로고    scopus 로고
    • Substrate profiling of cysteine proteases using a combinatorial peptide library identifies functionally unique specificities
    • DOI 10.1074/jbc.M513331200
    • Choe Y., Leonetti F., Greenbaum D.C., Lecaille F., Bogyo M., Bromme D., Ellman J.A., Craik C.S. (2006) Substrate profiling of cysteine proteases using a combinatorial peptide library identifies functionally unique specificities. J. Biol. Chem. 281: 12824-12832. (Pubitemid 43855375)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.18 , pp. 12824-12832
    • Choe, Y.1    Leonetti, F.2    Greenbaum, D.C.3    Lecaille, F.4    Bogyo, M.5    Bromme, D.6    Ellman, J.A.7    Craik, C.S.8
  • 28
    • 77955640606 scopus 로고    scopus 로고
    • Fluorescent proteins and their applications in imaging living cells and tissues
    • Chudakov D.M., Matz M.V., Lukyanov S., Lukyanov K.A. (2010) Fluorescent proteins and their applications in imaging living cells and tissues. Physiol. Rev. 90: 1103-1163.
    • (2010) Physiol. Rev. , vol.90 , pp. 1103-1163
    • Chudakov, D.M.1    Matz, M.V.2    Lukyanov, S.3    Lukyanov, K.A.4
  • 30
    • 0024393623 scopus 로고
    • Novel structures CTLA-2α and CTLA-2β expressed in mouse activated T cells and mast cells and homologous to cysteine proteinase proregions
    • DOI 10.1002/eji.1830190409
    • Denizot F., Brunet J.F., Roustan P., Harper K., Suzan M., Luciani M.F., Mattei M.G., Golstein P. (1989) Novel structures CTLA-2 alpha and CTLA-2 beta expressed in mouse activated T cells and mast cells and homologous to cysteine proteinase proregions. Eur. J. Immunol. 19: 631-635. (Pubitemid 19152928)
    • (1989) European Journal of Immunology , vol.19 , Issue.4 , pp. 631-635
    • Denizot, F.1    Brunet, J.-F.2    Roustan, P.3    Harper, K.4    Suzan, M.5    Luciani, M.-F.6    Mattei, M.-G.7    Golstein, P.8
  • 31
    • 55049133250 scopus 로고    scopus 로고
    • Metadegradomics: Toward in vivo quantitative degradomics of proteolytic post-translational modifications of the cancer proteome
    • Doucet A., Butler G.S., Rodriguez D., Prudova A., Overall C.M. (2008) Metadegradomics: toward in vivo quantitative degradomics of proteolytic post-translational modifications of the cancer proteome. Mol. Cell. Proteomics 7: 1925-1951.
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 1925-1951
    • Doucet, A.1    Butler, G.S.2    Rodriguez, D.3    Prudova, A.4    Overall, C.M.5
  • 33
    • 33846167705 scopus 로고    scopus 로고
    • Activity based probes for proteases: Applications to biomarker discovery, molecular imaging and drug screening
    • DOI 10.2174/138161207779313623
    • Fonovic M., Bogyo M. (2007) Activity based probes for proteases: applications to biomarker discovery, molecular imaging and drug screening. Curr. Pharm. Des. 13: 253-261. (Pubitemid 46085277)
    • (2007) Current Pharmaceutical Design , vol.13 , Issue.3 , pp. 253-261
    • Fonovic, M.1    Bogyo, M.2
  • 34
    • 0033952145 scopus 로고    scopus 로고
    • The biology of cell locomotion within three-dimensional extracellular matrix
    • DOI 10.1007/s000180050498
    • Friedl P., Brocker E.B. (2000) The biology of cell locomotion within three-dimensional extracellular matrix. Cell. Mol. Life Sci. 57: 41-64. (Pubitemid 30105329)
    • (2000) Cellular and Molecular Life Sciences , vol.57 , Issue.1 , pp. 41-64
    • Friedl, P.1    Brocker, E.-B.2
  • 36
    • 1942470581 scopus 로고    scopus 로고
    • A cathepsin L isoform that is devoid of a signal peptide localizes to the nucleus in S phase and processes the CDP/Cux transcription factor
    • DOI 10.1016/S1097-2765(04)00209-6, PII S1097276504002096
    • Goulet B., Baruch A., Moon N.S., Poirier M., Sansregret L.L., Erickson A., Bogyo M., Nepveu A. (2004) A cathepsin L isoform that is devoid of a signal peptide localizes to the nucleus in S phase and processes the CDP/Cux transcription factor. Mol. Cell 14: 207-219. (Pubitemid 38515648)
    • (2004) Molecular Cell , vol.14 , Issue.2 , pp. 207-219
    • Goulet, B.1    Baruch, A.2    Moon, N.-S.3    Poirier, M.4    Sansregret, L.L.5    Erickson, A.6    Bogyo, M.7    Nepveu, A.8
  • 37
    • 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. (2000) Epoxide electrophiles as activity-dependent cysteine protease profiling and discovery tools. Chem. Biol. 7: 569-581.
    • (2000) Chem. Biol. , vol.7 , pp. 569-581
    • Greenbaum, D.1    Medzihradszky, K.F.2    Burlingame, A.3    Bogyo, M.4
  • 39
    • 0033776087 scopus 로고    scopus 로고
    • Potency and selectivity of inhibition of cathepsin K, L and S by their respective propeptides
    • Guay J., Falgueyret J.P., Ducret A., Percival M.D., Mancini J.A. (2000) Potency and selectivity of inhibition of cathepsin K, L and S by their respective propeptides. Eur. J. Biochem. 267: 6311-6318.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6311-6318
    • Guay, J.1    Falgueyret, J.P.2    Ducret, A.3    Percival, M.D.4    Mancini, J.A.5
  • 40
    • 0037805704 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases regulate antigen presentation
    • DOI 10.1038/nri1110
    • Honey K., Rudensky A.Y. (2003) Lysosomal cysteine proteases regulate antigen presentation. Nat. Rev. Immunol. 3: 472-482. (Pubitemid 37339187)
    • (2003) Nature Reviews Immunology , vol.3 , Issue.6 , pp. 472-482
    • Honey, K.1    Rudensky, A.Y.2
  • 41
    • 0348038755 scopus 로고    scopus 로고
    • Apoptosis caused by cathepsins does not require Bid signaling in an in vivo model of progressive myoclonus epilepsy (EPM1)
    • DOI 10.1038/sj.cdd.4401309
    • Houseweart M.K., Vilaythong A., Yin X.M., Turk B., Noebels J.L., Myers R.M. (2003) Apoptosis caused by cathepsins does not require Bid signaling in an in vivo model of progressive myoclonus epilepsy (EPM1). Cell Death Differ. 10: 1329-1335. (Pubitemid 37536737)
    • (2003) Cell Death and Differentiation , vol.10 , Issue.12 , pp. 1329-1335
    • Houseweart, M.K.1    Vilaythong, A.2    Yin, X.-M.3    Turk, B.4    Noebels, J.L.5    Myers, R.M.6
  • 42
    • 26244445000 scopus 로고    scopus 로고
    • The lysosomal cysteine proteases in MHC class II antigen presentation
    • DOI 10.1111/j.0105-2896.2005.00310.x
    • Hsing L.C., Rudensky A.Y. (2005) The lysosomal cysteine proteases in MHC class II antigen presentation. Immunol. Rev. 207: 229-241. (Pubitemid 41415021)
    • (2005) Immunological Reviews , vol.207 , pp. 229-241
    • Hsing, L.C.1    Rudensky, A.Y.2
  • 43
    • 57549090060 scopus 로고    scopus 로고
    • Visualizing protease activity in living cells: From two dimensions to four dimensions
    • Chapter 4: Unit 4 20
    • Jedeszko C., Sameni M., Olive M.B., Moin K., Sloane B.F. (2008) Visualizing protease activity in living cells: from two dimensions to four dimensions. Curr. Protoc. Cell Biol. Chapter 4: Unit 4 20.
    • (2008) Curr. Protoc. Cell Biol
    • Jedeszko, C.1    Sameni, M.2    Olive, M.B.3    Moin, K.4    Sloane, B.F.5
  • 44
    • 0037307787 scopus 로고    scopus 로고
    • Chemical proteomics and its application to drug discovery
    • DOI 10.1016/S0958-1669(02)00010-1
    • Jeffery D.A., Bogyo M. (2003) Chemical proteomics and its application to drug discovery. Curr. Opin. Biotechnol. 14: 87-95. (Pubitemid 36151848)
    • (2003) Current Opinion in Biotechnology , vol.14 , Issue.1 , pp. 87-95
    • Jeffery, D.A.1    Bogyo, M.2
  • 45
    • 0037459045 scopus 로고    scopus 로고
    • Crystal structure of stefin A in complex with cathepsin H: N-terminal residues of inhibitors can adapt to the active sites of endo- and exopeptidases
    • DOI 10.1016/S0022-2836(02)01432-8
    • Jenko S., Dolenc I., Guncar G., Dobersek A., Podobnik M., Turk D. (2003) Crystal structure of Stefin A in complex with cathepsin H: N-terminal residues of inhibitors can adapt to the active sites of endo- and exopeptidases. J. Mol. Biol. 326: 875-885. (Pubitemid 36279326)
    • (2003) Journal of Molecular Biology , vol.326 , Issue.3 , pp. 875-885
    • Jenko, S.1    Dolenc, I.2    Guncar, G.3    Dobersek, A.4    Podobnik, M.5    Turk, D.6
  • 46
    • 71049188177 scopus 로고    scopus 로고
    • Monitoring compartment-specific substrate cleavage by cathepsins B, K, L, and S at physiological pH and redox conditions
    • Jordans S., Jenko-Kokalj S., Kuhl N.M., Tedelind S., Sendt W., Bromme D., Turk D., Brix K. (2009) Monitoring compartment-specific substrate cleavage by cathepsins B, K, L, and S at physiological pH and redox conditions. BMC Biochem. 10: 23.
    • (2009) BMC Biochem. , vol.10 , pp. 23
    • Jordans, S.1    Jenko-Kokalj, S.2    Kuhl, N.M.3    Tedelind, S.4    Sendt, W.5    Bromme, D.6    Turk, D.7    Brix, K.8
  • 49
    • 0035799319 scopus 로고    scopus 로고
    • Profiling serine hydrolase activities in complex proteomes
    • DOI 10.1021/bi002579j
    • Kidd D., Liu Y., Cravatt B.F. (2001) Profiling serine hydrolase activities in complex proteomes. Biochemistry 40: 4005-4015. (Pubitemid 32280438)
    • (2001) Biochemistry , vol.40 , Issue.13 , pp. 4005-4015
    • Kidd, D.1    Liu, Y.2    Cravatt, B.F.3
  • 50
    • 28544435485 scopus 로고    scopus 로고
    • Lysosomes and autophagy in cell death control
    • DOI 10.1038/nrc1738
    • Kroemer G., Jaattela M. (2005) Lysosomes and autophagy in cell death control. Nat. Rev. Cancer 5: 886-897. (Pubitemid 41746033)
    • (2005) Nature Reviews Cancer , vol.5 , Issue.11 , pp. 886-897
    • Kroemer, G.1    Jaattela, M.2
  • 51
    • 0037115483 scopus 로고    scopus 로고
    • Trafficking of lysosomal cathepsin B-green fuorescent protein to the surface of thyroid epithelial cells involves the endosomal/lysosomal compartment
    • DOI 10.1242/jcs.00184
    • Linke M., Herzog V., Brix K. (2002a) Trafficking of lysosomal cathepsin B-green fluorescent protein to the surface of thyroid epithelial cells involves the endosomal/ lysosomal compartment. J. Cell Sci. 115: 4877-4889. (Pubitemid 36054640)
    • (2002) Journal of Cell Science , vol.115 , Issue.24 , pp. 4877-4889
    • Linke, M.1    Herzog, V.2    Brix, K.3
  • 52
    • 0035985060 scopus 로고    scopus 로고
    • Thyroid stimulating hormone upregulates secretion of cathepsin B from thyroid epithelial cells
    • DOI 10.1515/BC.2002.081
    • Linke M., Jordans S., Mach L., Herzog V., Brix K. (2002b) Thyroid stimulating hormone upregulates secretion of cathepsin B from thyroid epithelial cells. Biol. Chem. 383: 773-784. (Pubitemid 34649896)
    • (2002) Biological Chemistry , vol.383 , Issue.5 , pp. 773-784
    • Linke, M.1    Jordans, S.2    Mach, L.3    Herzog, V.4    Brix, K.5
  • 54
    • 57649155302 scopus 로고    scopus 로고
    • Proteases: Multifunctional enzymes in life and disease
    • Lopez-Otin C., Bond J.S. (2008) Proteases: multifunctional enzymes in life and disease. J. Biol. Chem. 283: 30433-30437.
    • (2008) J. Biol. Chem. , vol.283 , pp. 30433-30437
    • Lopez-Otin, C.1    Bond, J.S.2
  • 55
    • 0036302814 scopus 로고    scopus 로고
    • Protease degradomics: A new challenge for proteomics
    • DOI 10.1038/nrm858
    • Lopez-Otin C., Overall C.M. (2002) Protease degradomics: a new challenge for proteomics. Nat. Rev. Mol. Cell Biol. 3: 509-519. (Pubitemid 34733432)
    • (2002) Nature Reviews Molecular Cell Biology , vol.3 , Issue.7 , pp. 509-519
    • Lopez-Otin, C.1    Overall, C.M.2
  • 56
    • 0028237920 scopus 로고
    • Maturation of human procathepsin B. Proenzyme activation and proteolytic processing of the precursor to the mature proteinase, in vitro, are primarily unimolecular processes
    • Mach L., Mort J.S., Glossl J. (1994) Maturation of human procathepsin B. Proenzyme activation and proteolytic processing of the precursor to the mature proteinase, in vitro, are primarily unimolecular processes. J. Biol. Chem. 269: 13030-13035.
    • (1994) J. Biol. Chem. , vol.269 , pp. 13030-13035
    • Mach, L.1    Mort, J.S.2    Glossl, J.3
  • 57
    • 57349176440 scopus 로고    scopus 로고
    • Nuclear cathepsin F regulates activation markers in rat hepatic stellate cells
    • Maubach G., Lim M.C., Zhuo L. (2008) Nuclear cathepsin F regulates activation markers in rat hepatic stellate cells. Mol. Biol. Cell 19: 4238-4248.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 4238-4248
    • Maubach, G.1    Lim, M.C.2    Zhuo, L.3
  • 58
    • 50849092878 scopus 로고    scopus 로고
    • Intestine-specific expression of green fluorescent protein-tagged cathepsin B: Proof-of-principle experiments
    • Mayer K., Iolyeva M.E., Meyer-Grahle U., Brix K. (2008) Intestine-specific expression of green fluorescent protein-tagged cathepsin B: proof-of-principle experiments. Biol. Chem. 389, 1085-1096.
    • (2008) Biol. Chem. , vol.389 , pp. 1085-1096
    • Mayer, K.1    Iolyeva, M.E.2    Meyer-Grahle, U.3    Brix, K.4
  • 59
    • 67649620040 scopus 로고    scopus 로고
    • Release of endo-lysosomal cathepsins B, D, and L from IEC6 cells in a cell culture model mimicking intestinal manipulation
    • Mayer K., Vreemann A., Qu H., Brix K. (2009) Release of endo-lysosomal cathepsins B, D, and L from IEC6 cells in a cell culture model mimicking intestinal manipulation. Biol. Chem. 390: 471-480.
    • (2009) Biol. Chem. , vol.390 , pp. 471-480
    • Mayer, K.1    Vreemann, A.2    Qu, H.3    Brix, K.4
  • 60
    • 33749017931 scopus 로고    scopus 로고
    • Cysteine cathepsins: Multifunctional enzymes in cancer
    • DOI 10.1038/nrc1949, PII NRC1949
    • Mohamed M.M., Sloane B.F. (2006) Cysteine cathepsins: multifunctional enzymes in cancer. Nat. Rev. Cancer 6: 764-775. (Pubitemid 44450465)
    • (2006) Nature Reviews Cancer , vol.6 , Issue.10 , pp. 764-775
    • Mohamed, M.M.1    Sloane, B.F.2
  • 63
    • 4644267867 scopus 로고    scopus 로고
    • Exon skipping of cathepsin B: Mitochondrial targeting of a lysosomal peptidase provokes cell death
    • DOI 10.1074/jbc.M405333200
    • Muntener K., Zwicky R., Csucs G., Rohrer J., Baici A. (2004) Exon skipping of cathepsin B: mitochondrial targeting of a lysosomal peptidase provokes cell death. J. Biol. Chem. 279: 41012-41017. (Pubitemid 39287702)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.39 , pp. 41012-41017
    • Muntener, K.1    Zwicky, R.2    Csucs, G.3    Rohrer, J.4    Baici, A.5
  • 64
    • 0037810410 scopus 로고    scopus 로고
    • Family C1 cysteine proteases: Biological diversity or redundancy?
    • DOI 10.1515/BC.2003.094
    • Nagler D.K., Menard R. (2003) Family C1 cysteine proteases: biological diversity or redundancy? Biol. Chem. 384: 837-843. (Pubitemid 36874497)
    • (2003) Biological Chemistry , vol.384 , Issue.6 , pp. 837-843
    • Nagler, D.K.1    Menard, R.2
  • 66
    • 33646576168 scopus 로고    scopus 로고
    • Degradomics: Systems biology of the protease web. Pleiotropic roles of MMPs in cancer
    • DOI 10.1007/s10555-006-7890-0, Metalloproteinases and Cancer
    • Overall C.M., Dean R.A. (2006) Degradomics: systems biology of the protease web. Pleiotropic roles of MMPs in cancer. Cancer Metastasis Rev. 25: 69-75. (Pubitemid 43723983)
    • (2006) Cancer and Metastasis Reviews , vol.25 , Issue.1 , pp. 69-75
    • Overall, C.M.1    Dean, R.A.2
  • 67
    • 43749107913 scopus 로고    scopus 로고
    • Application of activity-based probes to the study of enzymes involved in cancer progression
    • DOI 10.1016/j.gde.2007.12.001, PII S0959437X07002134
    • Paulick M.G., Bogyo M. (2008) Application of activity-based probes to the study of enzymes involved in cancer progression. Curr. Opin. Genet. Dev. 18: 97-106. (Pubitemid 351694441)
    • (2008) Current Opinion in Genetics and Development , vol.18 , Issue.1 , pp. 97-106
    • Paulick, M.G.1    Bogyo, M.2
  • 68
    • 0037803570 scopus 로고    scopus 로고
    • Human and mouse proteases: A comparative genomic approach
    • DOI 10.1038/nrg1111
    • Puente X.S., Sanchez L.M., Overall C.M., Lopez-Otin C. (2003) Human and mouse proteases: a comparative genomic approach. Nat. Rev. Genet. 4: 544-558. (Pubitemid 36781345)
    • (2003) Nature Reviews Genetics , vol.4 , Issue.7 , pp. 544-558
    • Puente, X.S.1    Sanchez, L.M.2    Overall, C.M.3    Lopez-Otin, C.4
  • 70
    • 78149357485 scopus 로고    scopus 로고
    • Peptidase inhibitors in the MEROPS database
    • Rawlings N.D. (2010) Peptidase inhibitors in the MEROPS database. Biochimie 92: 1463-1483.
    • (2010) Biochimie , vol.92 , pp. 1463-1483
    • Rawlings, N.D.1
  • 71
  • 72
    • 0034930528 scopus 로고    scopus 로고
    • Towards specific functions of lysosomal cysteine peptidases: Phenotypes of mice deficient for cathepsin B or cathepsin L
    • DOI 10.1515/BC.2001.089
    • Reinheckel T., Deussing J., Roth W., Peters C. (2001) Towards specific functions of lysosomal cysteine peptidases: phenotypes of mice deficient for cathepsin B or cathepsin L. Biol. Chem. 382: 735-741. (Pubitemid 32631710)
    • (2001) Biological Chemistry , vol.382 , Issue.5 , pp. 735-741
    • Reinheckel, T.1    Deussing, J.2    Roth, W.3    Peters, C.4
  • 73
    • 0034930565 scopus 로고    scopus 로고
    • Imaging proteolysis by living human glioma cells
    • DOI 10.1515/BC.2001.094
    • Sameni M., Dosescu J., Sloane B.F. (2001) Imaging proteolysis by living human glioma cells. Biol. Chem. 382: 785-788. (Pubitemid 32631715)
    • (2001) Biological Chemistry , vol.382 , Issue.5 , pp. 785-788
    • Sameni, M.1    Dosescu, J.2    Sloane, B.F.3
  • 75
    • 0035985072 scopus 로고    scopus 로고
    • Epoxysuccinyl peptide-derived cathepsin B inhibitors: Modulating membrane permeability by conjugation with the C-terminal heptapeptide segment of penetratin
    • DOI 10.1515/BC.2002.090
    • Schaschke N., Deluca D., Assfalg-Machleidt I., Hohneke C., Sommerhoff C.P., Machleidt W. (2002) Epoxysuccinyl peptide-derived cathepsin B inhibitors: modulating membrane permeability by conjugation with the C-terminal heptapeptide segment of penetratin. Biol. Chem. 383: 849-852. (Pubitemid 34649905)
    • (2002) Biological Chemistry , vol.383 , Issue.5 , pp. 849-852
    • Schaschke, N.1    Deluca, D.2    Assfalg-Machleidt, I.3    Hohneke, C.4    Sommerhoff, C.P.5    Machleidt, W.6
  • 77
    • 33646462162 scopus 로고    scopus 로고
    • Proteomic profiling of metalloprotease activities with cocktails of active-site probes
    • Sieber S.A., Niessen S., Hoover H.S., Cravatt B.F. (2006) Proteomic profiling of metalloprotease activities with cocktails of active-site probes. Nat. Chem. Biol. 2: 274-281.
    • (2006) Nat. Chem. Biol. , vol.2 , pp. 274-281
    • Sieber, S.A.1    Niessen, S.2    Hoover, H.S.3    Cravatt, B.F.4
  • 78
    • 0028341492 scopus 로고
    • Cathepsin B activity in human lung tumor cell lines: Ultrastructural localization, pH sensitivity, and inhibitor status at the cellular level
    • Spiess E., Bruning A., Gack S., Ulbricht B., Spring H., Trefz G., Ebert W. (1994) Cathepsin B activity in human lung tumor cell lines: ultrastructural localization, pH sensitivity, and inhibitor status at the cellular level. J. Histochem. Cytochem. 42: 917-929. (Pubitemid 24198450)
    • (1994) Journal of Histochemistry and Cytochemistry , vol.42 , Issue.7 , pp. 917-929
    • Spiess, E.1    Bruning, A.2    Gack, S.3    Ulbricht, B.4    Spring, H.5    Trefz, G.6    Ebert, W.7
  • 79
    • 0025301658 scopus 로고
    • The refined 2.4 A X-ray crystal structure of recombinant human stefin B in complex with the cysteine proteinase papain: A novel type of proteinase inhibitor interaction
    • Stubbs M.T., Laber B., Bode W., Huber R., Jerala R., Lenarcic B., Turk V. (1990) The refined 2.4 A X-ray crystal structure of recombinant human stefin B in complex with the cysteine proteinase papain: a novel type of proteinase inhibitor interaction. Embo J. 9: 1939-1947.
    • (1990) Embo J. , vol.9 , pp. 1939-1947
    • Stubbs, M.T.1    Laber, B.2    Bode, W.3    Huber, R.4    Jerala, R.5    Lenarcic, B.6    Turk, V.7
  • 82
    • 0034502852 scopus 로고    scopus 로고
    • Cathepsin K in thyroid epithelial cells: Sequence, localization and possible function in extracellular proteolysis of thyroglobulin
    • Tepel C., Bromme D., Herzog V., Brix K. (2000) Cathepsin K in thyroid epithelial cells: sequence, localization and possible function in extracellular proteolysis of thyroglobulin. J. Cell Sci. 113: 4487-4498. (Pubitemid 32117909)
    • (2000) Journal of Cell Science , vol.113 , Issue.24 , pp. 4487-4498
    • Tepel, C.1    Bromme, D.2    Herzog, V.3    Brix, K.4
  • 83
    • 33748308883 scopus 로고    scopus 로고
    • Targeting proteases: Successes, failures and future prospects
    • DOI 10.1038/nrd2092, PII NRD2092
    • Turk B. (2006) Targeting proteases: successes, failures and future prospects. Nat. Rev. Drug Discov. 5: 785-799. (Pubitemid 44323703)
    • (2006) Nature Reviews Drug Discovery , vol.5 , Issue.9 , pp. 785-799
    • Turk, B.1
  • 84
    • 69249140641 scopus 로고    scopus 로고
    • Lysosomes as "suicide bags" in cell death: Myth or reality?
    • Turk B., Turk V. (2009) Lysosomes as "suicide bags" in cell death: myth or reality? J. Biol. Chem. 284: 21783-21787.
    • (2009) J. Biol. Chem. , vol.284 , pp. 21783-21787
    • Turk, B.1    Turk, V.2
  • 85
    • 0035801514 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases: Facts and opportunities
    • DOI 10.1093/emboj/20.17.4629
    • Turk V., Turk B., Turk D. (2001) Lysosomal cysteine proteases: facts and opportunities. Embo J. 20: 4629-4633. (Pubitemid 32848615)
    • (2001) EMBO Journal , vol.20 , Issue.17 , pp. 4629-4633
    • Turk, V.1    Turk, B.2    Turk, D.3
  • 86
    • 33846164404 scopus 로고    scopus 로고
    • Emerging roles of cysteine cathepsins in disease and their potential as drug targets
    • DOI 10.2174/138161207780162962
    • Vasiljeva O., Reinheckel T., Peters C., Turk D., Turk V., Turk B. (2007) Emerging roles of cysteine cathepsins in disease and their potential as drug targets. Curr. Pharm. Des. 13: 387-403. (Pubitemid 46477760)
    • (2007) Current Pharmaceutical Design , vol.13 , Issue.4 , pp. 387-403
    • Vasiljeva, O.1    Reinheckel, T.2    Peters, C.3    Turk, D.4    Turk, V.5    Turk, B.6
  • 90
    • 68049107457 scopus 로고    scopus 로고
    • A suite of activity-based probes for human cytochrome P450 enzymes
    • Wright A.T., Song J.D., Cravatt B.F. (2009) A suite of activity-based probes for human cytochrome P450 enzymes. J. Am. Chem. Soc. 131: 10692-10700.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 10692-10700
    • Wright, A.T.1    Song, J.D.2    Cravatt, B.F.3
  • 91
    • 58949099705 scopus 로고    scopus 로고
    • Evaluation of alpha,beta-unsaturated ketone-based probes for papain-family cysteine proteases
    • Yang Z., Fonovic M., Verhelst S.H., Blum G., Bogyo M. (2009) Evaluation of alpha,beta-unsaturated ketone-based probes for papain-family cysteine proteases. Bioorg Med. Chem. 17: 1071-1078.
    • (2009) Bioorg Med. Chem. , vol.17 , pp. 1071-1078
    • Yang, Z.1    Fonovic, M.2    Verhelst, S.H.3    Blum, G.4    Bogyo, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.