Activity-Based Probes that Target Diverse Cysteine Protease Families

Nature Chemical Biology

Volumn 1, Issue 1, 2005, Pages 33-38

  Kato, Daisuke ^a   Boatright, Kelly M ^a   Berger, Alicia B ^a   Nazif, Tamim ^a   Blum, Galia ^a   Ryan, Ciara ^b   Chehade, Kareem A H ^c   Salvesen, Guy S ^b   Bogyo, Matthew ^a,c  

^a STANFORD UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b BURNHAM INSTITUTE   (United States)

^c UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE PROTEINASE; CYSTEINE PROTEINASE INHIBITOR; KETONE;

ANIMAL; ARTICLE; CELL LINE; CHEMISTRY; ENZYME SPECIFICITY; GENETIC PROCEDURES; HUMAN; METABOLISM; MOLECULAR PROBE; SYNTHESIS;

ANIMALS; CELL LINE; CYSTEINE ENDOPEPTIDASES; CYSTEINE PROTEINASE INHIBITORS; HUMANS; KETONES; MOLECULAR PROBE TECHNIQUES; MOLECULAR PROBES; SUBSTRATE SPECIFICITY;

EID: 29444460784     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio707     Document Type: Letter

References (28)

1. Speers, A.E. & Cravatt, B.F. Chemical strategies for activity-based proteomics. ChemBioChem 5, 41-47 (2004).
2. Berger, A.B., Vitorino, P.M. & Bogyo, M. Activity-based protein profiling: applications to biomarker discovery, in vivo imaging and drug discovery. Am. J. Pharmacogenomics 4, 371-381 (2004).
3. Jeffery, D.A. & Bogyo, M. Chemical proteomics and its application to drug discovery. Curr. Opin. Biotechnol. 14, 87-95 (2003).
4. Thornberry, N.A. et al. A combinatorial approach defines specificities of members of the caspase family and granzyme B. Functional relationships established for key mediators of apoptosis. J. Biol. Chem. 272, 17907-17911 (1997).
5. Stennicke, H.R., Renatus, M., Meldal, M. & Salvesen, G.S. Internally quenched fluorescent peptide substrates disclose the subsite preferences of human caspases 1, 3, 6, 7 and 8. Biochem. J. 350, 563-568 (2000).
6. Loak, K. et al. Novel cell-permeable acyloxymethylketone inhibitors of asparaginyl endopeptidase. Biol. Chem. 384, 1239-1246 (2003).
7. Niestroj, A.J. et al. Inhibition of mammalian legumain by Michael acceptors and AzaAsn-halomethylketones. Biol. Chem. 383, 1205-1214 (2002).
8. Asgian, J.L. et al. Aza-peptide epoxides: a new class of inhibitors selective for clan CD cysteine proteases. J. Med. Chem. 45, 4958-4960 (2002).
9. Powers, J.C., Asgian, J.L., Ekici, O.D. & James, K.E. Irreversible inhibitors of serine, cysteine, and threonine proteases. Chem. Rev. 102, 4639-4750 (2002).
10. Thornberry, N.A. et al. Inactivation of interleukin-1β converting enzyme by peptide (acyloxy)methyl ketones. Biochemistry 33, 3934-3940 (1994).
11. Uhlmann, F., Wernic, D., Poupart, M.A., Koonin, E.V. & Nasmyth, K. Cleavage of cohesin by the CD clan protease separin triggers anaphase in yeast. Cell 103, 375-386 (2000).
12. Lee, A., Huang, L. & Ellman, J.A. General solid-phase method for the preparation of mechanism-based cysteine protease inhibitors. J. Am. Chem. Soc. 121, 9907-9914 (1999).
13. Wood, W.J., Huang, L. & Ellman, J.A. Synthesis of a diverse library of mechanism-based cysteine protease inhibitors. J. Comb. Chem. 5, 869-880 (2003).
14. Chen, J.M., Rawlings, N.D., Stevens, R.A. & Barrett, A.J. Identification of the active site of legumain links it to caspases, clostripain and gingipains in a new clan of cysteine endopeptidases. FEBSLett. 441, 361-365 (1998).
15. Fox, T., Mason, P., Storer, A.C. & Mort, J.S. Modification of S1 subsite specificity in the cysteine protease cathepsin B. Protein Eng. 8, 53-57 (1995).
16. Manoury, B. et al. An asparaginyl endopeptidase processes a microbial antigen for class II MHC presentation. Nature 396, 695-699 (1998).
17. Chen, J.M., Fortunato, M. & Barrett, A.J. Activation of human prolegumain by cleavage at a C-terminal asparagine residue. Biochem. J. 352, 327-334 (2000).
18. Li, D.N., Matthews, S.P., Antoniou, A.N., Mazzeo, D. & Watts, C. Multistep autoactivation of asparaginyl endopeptidase in vitro and in vivo. J. Biol. Chem. 278, 38980-38990 (2003).
19. Halfon, S., Patel, S., Vega, F., Zurawski, S. & Zurawski, G. Autocatalytic activation of human legumain at aspartic acid residues. FEBS Lett. 438, 114-118 (1998).
20. Boatright, K.M. & Salvesen, G.S. Mechanisms of caspase activation. Curr. Opin. Cell Biol. 15, 725-731 (2003).
21. Li, P. et al. Cytochrome c and dATP-dependent formation ofApaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 91, 479-489 (1997).
22. Meergans, T., Hildebrandt, A.K., Horak, D., Haenisch, C. & Wendel, A. The short prodomain influences caspase-3 activation in HeLa cells. Biochem. J. 349, 135-140 (2000).
23. Denault, J.B. & Salvesen, G.S. Human caspase-7 activity and regulation by its N-terminal peptide. J. Biol. Chem. 278, 34042-34050 (2003).
24. Turk, B., Turk, V. & Turk, D. Structural and functional aspects of papain-like cysteine proteinases and their protein inhibitors. Biol. Chem. 378, 141-150 (1997).
25. Bogyo, M., Verhelst, S., Bellingard-Dubouchaud, V., Toba, S. & Greenbaum, D. Selective targeting of lysosomal cysteine proteases with radiolabeled electrophilic substrate analogs. Chem. Biol. 7, 27-38 (2000).
26. Yamamoto, A. et al. Crystallization and preliminary X-ray study of the cathepsin B complexed with CA074, a selective inhibitor. J. Mol. Biol. 227,942-944 (1992).
27. Stennicke, H.R. & Salvesen, G.S. Caspases: preparation and characterization. Methods 17, 313-319 (1999).
28. Stennicke, H.R. et al. Pro-caspase-3 isamajorphysiologictargetofcaspase-8. J. Biol. Chem. 273, 27084-27090 (1998).