Preparation of the caspase-3/7 substrate Ac-DEVD-pNA by solution-phase peptide synthesis

Nature Protocols

Volumn 5, Issue 2, 2010, Pages 294-302

  Peterson, Quinn P ^a   Goode, David R ^b   West, Diana C ^b   Botham, Rachel C ^b   Hergenrother, Paul J ^a,b  

^a UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

^b UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

4 NITROANILINE; ACETIC ACID ETHYL ESTER; ASPARAGINE; CASPASE 3; CASPASE 3 SUBSTRATE 1; CASPASE 7; TRIFLUOROACETIC ACID; UNCLASSIFIED DRUG; VALINE;

AMINO ACID SEQUENCE; APOPTOSIS; ARTICLE; COLORIMETRY; CROSS COUPLING REACTION; CRYSTALLIZATION; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME SUBSTRATE; HYDROLYSIS; NONHUMAN; PEPTIDE SYNTHESIS; PRIORITY JOURNAL; SOLID PHASE SYNTHESIS;

ANILIDES; ANILINE COMPOUNDS; APOPTOSIS; CASPASE 3; CASPASE 7; ENZYME ACTIVATION; HUMANS; HYDROLYSIS; INFLAMMATION; OLIGOPEPTIDES; PEPTIDES; SOLUTIONS; SOLVENTS; SUBSTRATE SPECIFICITY;

EID: 76649112052     PISSN: 17542189     EISSN: 17502799     Source Type: Journal    
DOI: 10.1038/nprot.2009.223     Document Type: Article

References (55)

1. Shi, Y. Mechanisms of caspase activation and inhibition during apoptosis. Mol. Cell 9, 459-470 (2002).
2. Bose, K., Pop, C., Feeney, B. & Clark, A.C. An uncleavable procaspase-3 mutant has a lower catalytic efficiency but an active site similar to that of mature caspase-3. Biochemistry 42, 12298-12310 (2003).
3. Hengartner, M.O. The biochemistry of apoptosis. Nature 407, 770-776 (2000).
4. Acehan, D. et al. Three-dimensional structure of the apoptosome: implications for assembly, procaspase-9 binding, and activation. Mol. Cell 9, 423-432 (2002).
5. Chao, Y. et al. Engineering a dimeric caspase-9: a re-evaluation of the induced proximity model for caspase activation. PLoS Biol. 3, e183 (2005).
6. Yin, Q. et al. Caspase-9 holoenzyme is a specific and optimal procaspase-3 processing machine. Mol. Cell 22, 259-268 (2006).
7. Walsh, J.G. et al. Executioner caspase-3 and caspase-7 are functionally distinct proteases. Proc. Natl. Acad. Sci. USA 105, 12815-12819 (2008).
8. Riedl, S.J. et al. Structural basis for the activation of human procaspase-7. Proc. Natl. Acad. Sci. USA 98, 14790-14795 (2001).
9. Luthi, A.U. & Martin, S.J. The CASBAH: a searchable database of caspase substrates. Cell Death Differ. 14, 641-650 (2007).
10. Timmer, J.C. & Salvesen, G.S. Caspase substrates. Cell Death Differ. 14, 66-72 (2007).
11. Engidawork, E., Gulesserian, T., Yoo, B.C., Cairns, N. & Lubec, G. Alteration of caspases and apoptosis-related proteins in brains of patients with Alzheimer's disease. Biochem. Biophys. Res. Commun. 281, 84-93 (2001). (Pubitemid 32924403)
12. Blandini, F. et al. Peripheral proteasome and caspase activity in Parkinson disease and Alzheimer disease. Neurology 66, 529-534 (2006).
13. Roth, K.A. Caspases, apoptosis, and Alzheimer disease: causation, correlation, and confusion. J. Neuropathol. Exp. Neurol. 60, 829-838 (2001).
14. Nagatsu, T. & Sawada, M. Biochemistry of postmortem brains in Parkinson's disease: historical overview and future prospects. J. Neural. Transm. Suppl. 113-120 (2007).
15. Rubinsztein, D.C. & Carmichael, J. Huntington's disease: molecular basis of neurodegeneration. Expert Rev. Mol. Med. 5, 1-21 (2003).
16. Martin, L.J. Neuronal death in amyotrophic lateral sclerosis is apoptosis: possible contribution of a programmed cell death mechanism. J. Neuropathol. Exp. Neurol. 58, 459-471 (1999).
17. Green, D.R. & Kroemer, G. Pharmacological manipulation of cell death: clinical applications in sight? J. Clin. Invest. 115, 2610-2617 (2005).
18. Hanahan, D. & Weinberg, R.A. The hallmarks of cancer. Cell 100, 57-70 (2000).
19. Soung, Y.H. et al. Caspase-8 gene is inactivated by somatic mutations in gastric carcinomas. Cancer Res. 65, 815-821 (2005).
20. Soung, Y.H. et al. Caspase-8 gene is frequently inactivated by the frameshift somatic mutation 1225-1226delTG in hepatocellular carcinomas. Oncogene 24, 141-147 (2005).
21. Kim, H.S. et al. Inactivating mutations of caspase-8 gene in colorectal carcinomas. Gastroenterology 125, 708-715 (2003).
22. Mandruzzato, S., Brasseur, F., Andry, G., Boon, T. & van der Bruggen, P. A CASP-8 mutation recognized by cytolytic T lymphocytes on a human head and neck carcinoma. J. Exp. Med. 186, 785-793 (1997).
23. Teitz, T. et al. Caspase 8 is deleted or silenced preferentially in childhood neuroblastomas with amplification of MYCN. Nat. Med. 6, 529-535 (2000).
24. Teitz, T., Lahti, J.M. & Kidd, V.J. Aggressive childhood neuroblastomas do not express caspase-8: an important component of programmed cell death. J. Mol. Med. 79, 428-436 (2001).
25. Shin, M.S. et al. Inactivating mutations of CASP10 gene in non-Hodgkin lymphomas. Blood 99, 4094-4099 (2002).
26. Park, W.S. et al. Inactivating mutations of the caspase-10 gene in gastric cancer. Oncogene 21, 2919-2925 (2002).
27. Kania, J., Konturek, S.J., Marlicz, K., Hahn, E.G. & Konturek, P.C. Expression of survivin and caspase-3 in gastric cancer. Dig. Dis. Sci. 48, 266-271 (2003).
28. Zou, H. et al. Regulation of the Apaf-1/caspase-9 apoptosome by caspase-3 and XIAP. J. Biol. Chem. 278, 8091-8098 (2003).
29. Shiozaki, E.N. et al. Mechanism of XIAP-mediated inhibition of caspase-9. Mol. Cell 11, 519-527 (2003).
30. Roy, S. et al. Maintenance of caspase-3 proenzyme dormancy by an intrinsic 'safety catch' regulatory tripeptide. Proc. Natl. Acad. Sci. USA 98, 6132-6137 (2001).
31. Grigoriev, M.Y., Pozharissky, K.M., Hanson, K.P., Imyanitov, E.N. & Zhivotovsky, B. Expression of caspase-3 and-7 does not correlate with the extent of apoptosis in primary breast carcinomas. Cell Cycle 1, 337-342 (2002).
32. Krepela, E., Prochazka, J., Liul, X., Fiala, P. & Kinkor, Z. Increased expression of Apaf-1 and procaspase-3 and the functionality of intrinsic apoptosis apparatus in non-small cell lung carcinoma. Biol. Chem. 385, 153-168 (2004).
33. Fink, D. et al. Elevated procaspase levels in human melanoma. Melanoma Res. 11, 385-393 (2001).
34. Estrov, Z. et al. Caspase 2 and caspase 3 protein levels as predictors of survival in acute myelogenous leukemia. Blood 92, 3090-3097 (1998).
35. Putt, K.S. et al. Small molecule activation of procaspase-3 to caspase-3 as a personalized anticancer strategy. Nat. Chem. Biol. 2, 543-550 (2006).
36. Peterson, Q.P. et al. PAC-1 activates procaspase-3 in vitro through relief of zinc-mediated inhibition. J. Mol. Biol. 388, 144-158 (2009).
37. Peterson, Q.P. et al. Procaspase-3 activation as an anti-cancer strategy: structure-activity relationship of PAC-1, and its cellular co-localization with procaspase-3. J. Med. Chem. 52, 5721-5731 (2009).
38. Thornberry, N. et al. A combinatorial approach defines specificities of members of the caspase family and granzyme B. Funtional relationships established for key mediators of apoptosis. J. Biol. Chem. 27, 17907-17911 (1997).
39. Nicholson, D.W. et al. Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis. Nature 376, 37-43 (1995).
40. Goode, D.R., Sharma, A.K. & Hergenrother, P.J. Using peptidic inhibitors to systematically probe the S1' site of caspase-3 and caspase-7. Org. Lett. 7, 3529-3532 (2005).
41. Smolewski, P., Grabarek, J., Phelps, D.J. & Darzynkiewicz, Z. Stathmo-apoptosis: arresting apoptosis by fluorochrome-labeled inhibitor of caspases. Int. J. Oncol. 19, 657-663 (2001).
42. Hardy, J.A. & Wells, J.A. Dissecting an allosteric switch in caspase-7 using chemical and mutational probes. J. Biol. Chem. 284, 26063-26069 (2009).
43. Chu, W., Rothfuss, J., Chu, Y., Zhou, D. & Mach, R.H. Synthesis and in vitro evaluation of sulfonamide isatin Michael acceptors as small molecule inhibitors of caspase-6. J. Med. Chem. 52, 2188-2191 (2009).
44. Chu, W. et al. Isatin sulfonamide analogs containing a Michael addition acceptor: a new class of caspase 3/7 inhibitors. J. Med. Chem. 50, 3751-3755 (2007).
45. Chu, W. et al. N-benzylisatin sulfonamide analogues as potent caspase-3 inhibitors: synthesis, in vitro activity, and molecular modeling studies. J. Med. Chem. 48, 7637-7647 (2005).
46. Guo, Z., Xian, M., Zhang, W., McGill, A. & Wang, P.G. N-nitrosoanilines: a new class of caspase-3 inhibitors. Bioorg. Med. Chem. 9, 99-106 (2001).
47. Chen, Y.-H. et al. Design, synthesis and biological evaluation of isoquinoline-1,3,4-trione derivatives as potent caspase-3 inhibitors. J. Med. Chem. 49, 1613-1623 (2006).
48. Lee, D. et al. Potent and selective non-peptide inhibitors of caspases 3 and 7. J. Med. Chem. 44, 2015-2026 (2001).
49. Wu, J.C. & Fritz, L.C. Irreversible caspase inhibitors: tools for studying apoptosis. Methods 17, 320-328 (1999).
50. Chapman, J.G. et al. A novel nonpeptidic caspase-3/7 inhibitor, (S)-(+)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin reduces myocardial ischemic injury. Eur. J. Pharmacol. 456, 59-68 (2002).
51. Hardy, J.A., Lam, J., Nguyen, J.T., O'Brien, T. & Wells, J.A. Discovery of an allosteric site in the caspases. Proc. Natl. Acad. Sci. USA 101, 12461-12466 (2004).
52. Hoeg-Jensen, T., Jakobsen, M.H. & Holm, A. A new method for rapid solution synthesis of shorter peptides by use of PyBOP. Tetrahedron Lett. 32, 6387-6390 (1991).
53. Carpino, L.A. et al. Rapid, continuous solution-phase peptide synthesis: application to peptides of pharmaceutical interest. Org. Process Res. Dev. 7, 28-37 (2002).
54. Thompson, C.M., Quinn, C.A. & Hergenrother, P.J. Total synthesis and cytoprotective properties of dykellic acid. J. Med. Chem. 52, 117-125 (2009).
55. Rijkers, D.T.S., Adams, H.P.H.M., Hemker, H.C. & Tesser, G.I. A convenient synthesis of amino acid p-nitroanilides; synthons in the synthesis of protease substrates. Tetrahedron 51, 11235-11250 (1995).