Proteasome inhibitors: A novel class of potent and effective antitumor agents

Cancer Research

Volumn 59, Issue 11, 1999, Pages 2615-2622

  Adams, Julian ^a   Palombella, Vito J ^a   Sausville, Edward A ^c   Johnson, Jill ^c   Destree, Antonia ^a   Lazarus, Douglas D ^a   Maas, Jochen ^b   Pien, Christine S ^a   Prakash, Samuel ^b   Elliott, Peter J ^a  

^a ProScript Inc   (United States)

^b SANOFI   (France)

^c NATIONAL INSTITUTES OF HEALTH   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANTINEOPLASTIC AGENT; BORTEZOMIB; PROTEASOME INHIBITOR; UNCLASSIFIED DRUG;

ANIMAL EXPERIMENT; ANTINEOPLASTIC ACTIVITY; ARTICLE; CANCER CELL CULTURE; CANCER GROWTH; CANCER INHIBITION; CELL CYCLE G2 PHASE; CYTOPATHOGENIC EFFECT; GROWTH INHIBITION; HUMAN; HUMAN CELL; MALE; MOUSE; NONHUMAN; NUDE MOUSE; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEINASE INHIBITION;

ALGORITHMS; ANIMALS; ANTINEOPLASTIC AGENTS; BORONIC ACIDS; COMPUTER SIMULATION; DRUG SCREENING ASSAYS, ANTITUMOR; HUMANS; MALE; MICE; MICE, NUDE; MODELS, CHEMICAL; PROTEASE INHIBITORS; TUMOR CELLS, CULTURED;

EID: 0033152760     PISSN: 00085472     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (32)

1. Goldberg, A. L., Stein, R., and Adams, J. New insights into proteasome function: from Archaebacteria to drug development. Chem. Biol., 2: 503-508, 1995.
2. Coux, O., Tanaka, K., and Goldberg, A. L. Structure and function of the 20S and 26S proteasomes. Annu. Rev. Biochem., 65: 801-847, 1996.
3. King, R. W., Deshaies, R. J., Peters, J-M., and Kirschner, M. W. How proteolysis drives the cell cycle. Science (Washington DC), 274: 1652-1659, 1996.
4. Chau, V., Tobias, J. W., Bachmair, A., Marriott, D., Ecker, D. J., Gonda, D. K., and Varshavsky, A. A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein. Science (Washington DC), 243: 1576-1583, 1989.
5. Palombella, V. J., Rando, O. J., Goldberg, A. L., and Maniatis, T. The ubiquitin-proteasome pathway is required for processing the NF-κB1 precursor protein and the activation of NF-κB. Cell, 78: 773-785, 1994.
6. Beg, A. A., and Baltimore, D. An essential role for NF-κB in preventing TNF-α-induced cell death. Science (Washington DC), 274: 782-784, 1996.
7. Van Antwerp, D. J., Martin, S. J., Kafri, T., Green, D. R., and Verma, I. M. Suppression of TNF-α-induced apoptosis by NF-κB. Science (Washington DC), 274: 787-789, 1996.
8. Wang, C-Y., Mayo, M. W., and Baldwin, A. S. TNF-and cancer therapy-induced apoptosis: potentiation by inhibition of NF-κB. Science (Washington DC). 274: 784-787, 1996.
9. Chu, Z-L., McKinsey, T. A., Liu, L., Gentry, J. J., Malim, M. H., and Ballard, D. W. Suppression of tumor necrosis factor-induced cell death by inhibitor of apoptosis c-IAP2 is under NF-κB control. Proc. Natl. Acad. Sci. USA, 94: 10057-10062, 1997.
10. Zetter, B. R. Adhesion molecules in tumor metastasis. Semin. Cancer Biol., 4: 219-229, 1993.
11. Read, M. A., Neish, A. S., Luscinskas, F. W., Palombella, V. J., Maniatis, T., and Collins, T. The proteasome pathway is required for cytokine-induced endothelial-leukocyte adhesion molecule expression. Immunity, 2: 493-506, 1995.
12. Sherr, C. J. Cancer cell cycles. Science (Washington DC), 274: 1672-1677, 1996.
13. Adams, J., Behnke, M., Chen, S., Cruickshank, A. A., Dick, L. R., Grenier, L., Klunder, J. M., Ma, Y-T., Plamondon, L., and Stein, R. L. Potent and selective inhibitors of the proteasome: dipeptidyl boronic acids. Bioorg. Med. Chem. Lett., 8: 333-338, 1998.
14. Stein, R. L., Melandri, F., and Dick, L. Inhibition of the chymotryptic-like proteolytic activity of rabbit muscle 20S proteasome. Proteasome isolation, purification, and assays were performed as previously described. Biochemistry, 35: 3899-3908, 1996.
15. Boyd, M. R., and Paull, D. Some practical considerations and applications of the National Cancer Institute in vitro anticancer drug discovery screen. Drug Dev. Res., 34: 91-109, 1995.
16. Weinstein, J. N., Myers, T. G., O'Connor, P. M., Friend, S. H., Fornace, A. J., Kohn, K. W., Fojo, T., Bates, S. E. Rubinstein, L. V., Anderson, N. L., Buolamwini, J. K., van Osdol, W. W., Monks, A. P., Scudiero, D. A., Viswanadhan, V. N., Johnson, G. S., Wittes, R. E., and Paull, K. D. An information-intensive approach to the molecular pharmacology of cancer. Science (Washington DC), 275: 343-349, 1997.
17. Mosmann, T. Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. J. Immunol. Methods. 65: 55-63, 1983.
18. Noguchi, P. D. Use of flow cytomelry for DNA analysis. Curr. Protocol Immunol., 57: 1-8, 1996.
19. Tsubuki, S., Kawasaki, H., Saito, Y., Miyashita, N., Inomata, M., and Kawashima, S. Purification and characterization of a Z-Leu-Leu-MCA degrading protease expected to regulate neunte formation: a novel catalytic activity in proteasome. Biochem. Biophys. Res., 196: 1195-1201, 1993.
20. Adams, J., and Stein, R. Novel inhibitors of the proteasome and their therapeutic use in inflammation. Annu. Rep. Med. Chem., 11: 279-288, 1996.
21. Seemüller, E., Lupas, A., Stock, D., Löwe, J., Huber, R., and Baumeister, W. Proteasome from Thermoplasma acidophilum: a threonine protease. Science (Washington DC), 268: 579-582, 1995.
22. Kaighn, M. E., Narauam, K. S., Ohnuki, Y., Lechner, J. F., and Jones, L. W. Establishment and characterization of a human prostatic carcinoma cell line (PC-3). Invest. Urol., 17: 16-23, 1979.
23. Tang, D. G., Li, L., Chopra, D. P., and Porter, A. T. Extended survivability of prostate cancer cells in the absence of trophic factors: increased proliferation, evasion of apoptosis, and the role of apoptosis proteins. Cancer Res., 58: 3466-3479, 1998.
24. Machiels, B. M., Henfling, M. E. R., Gerards, W. L. H., Broers, J. L. V , Bloemendal, H., Ramaekers, F. C. S., and Schutte, B. Detailed analysis of cell cycle kinetics upon proteasome inhibition. Cytometry, 28: 243-252, 1997.
25. 2/M-phase transition. Mol. Cell. Biol., 18: 546-557, 1998.
26. Drexler, H. C. A. Activation of the cell death program by inhibition of proteasome function. Proc. Natl. Acad. Sci. USA, 94: 855-860, 1997.
27. Orlowski, R. Z., Eswara, J. R., Lafond-Walker, A., Grever, M. R., Orlowski, M., and Dang, C. V. Tumor growth inhibition induced in a murine model of human Burkitt's lymphoma by a proteasome inhibitor. Cancer Res., 58: 4342-4348, 1998.
28. Nicholson, D. W., Ali, A., Thornberry, N. A., Vaillancourt, J. P., Ding, C. K., Gallant, M., Gareau, Y., Griffin, P. R., Labelle, M., Lazebnik, Y. A., Munday, N. A., Raju, S. M., Smulson, M. E., Yamin, T. T., Yu, V. L., and Miller, D. K. Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis. Nature (Lond.), 37: 37-43, 1995.
29. Hollingshead, M. G., Alley, M. C., Camalier, R. F., Abbott, B. J., Mayo, J. G., Malspeis, L., and Grever, M. R. In vivo cultivation of tumor cells in hollow fibers. Life Sci., 57: 131-141, 1995.
30. Imajoh-Ohmi, S., Kawaguchi, T., Sugiyama, S., Tanaka, T., Omura, K., and Kikuchi, H. Lactacystin, a specific inhibitor of the proteasome, induces apoptosis in human monoblast U937 cells. Biochem. Biophys. Res. Commun., 217: 1070-1077, 1995.
31. Lopes, U. G., Erhardt, P., Yao, R., and Cooper, G. M. p53-dependent induction of apoptosis by proteasome inhibitors. J. Biol. Chem., 272: 12893-12896, 1997.
32. Wang, X., Luo, H., Chen, H., Duguid, W., and Wu, J. Role of proteasomes in T cell activation and proliferation. J. Immunol., 160: 788-801, 1998.