Pharmacological proteasome inhibitors and their therapeutic potential

Bibliography

• HOCHSTRASSER M: Ubiquitin, proteasomes and the regulation of intracellular protein degradation. Curr. Opin. Cell. Biol. (1995) 7:215–223.
   PubMed Web of Science ®Google Scholar
• CIECHANOVER A: The ubiquitin-proteasome proteolytic pathway. Cell (1994) 79:13–21.
   PubMed Web of Science ®Google Scholar
• DOU QP, LI B: Proteasome inhibitors as potential novel anticancer agents. DrugResist. Updates (1999) 2:215–223.
   PubMed Web of Science ®Google Scholar
• ORLOWSKI RZ: The role of the ubiquitin-proteasome pathway in apoptosis. Cell Death Differ. (1999) 6:303–313.
   PubMed Web of Science ®Google Scholar
• SPATARO V, NORBURY C, HARRIS AL: The ubiquitin-proteasome pathway in cancer. Br. J Cancer (1998) 77:448–455.
   PubMed Web of Science ®Google Scholar
• SCHWARTZ AL, CIECHANOVER A: The ubiquitin-proteasome pathway and pathogenesis of human diseases. Ann. Rev. Med. (1999) 50:57–74.
   PubMed Web of Science ®Google Scholar
• CIECHANOVER A, ORIAN A, SCHWARTZ AL: Theubiquitin-mediated proteolytic pathway: mode of action and clinical implications. J Cell. Biochem. (2000) 77:40–51.
   Google Scholar
• KATOGJ: Human genetic diseases of proteolysis. Hum. MutaL (1999) 13:87–98.
   PubMedGoogle Scholar
• MULLER S, SCHWARTZ LM: Ubiquitin in homeostasis, development and disease. Bioessays (1995) 17:677–684.
   PubMedGoogle Scholar
• IMAJOH-OHMI S, KAWAGUCHI T, SUGIYAMA S, TANAKA K, OMURA S, KIKUCHI H: I2.tacystin, a specific inhibitor of the protesome, induces apotosis in human monoblast U937 cells. Biochem. Biophys. Res. Commun. (1995) 217:1070–1077.
   Google Scholar
• OMURA S, MATSUZAKI K, FUJIMOTO T et al.: Structure of, a new microbial metabolite which induces differentiation of neuroblastoma cells. J AntibioL (Tokyo) (1991) 44:117–118.
   PubMed Web of Science ®Google Scholar
• FENTEANY G, STANDAERT RF, REICHARD GA, COREY EJ, SL: A beta-lactone related to lactacystin induces neurite outgrowth in a neuroblastoma cell line and inhibits cell cycle progression in an osteosar-coma cell line. Proc. Natf Acad. Sci. USA (1994) 91:3358–3362.
   PubMed Web of Science ®Google Scholar
• FUJITA E, MUKASA T, TSUKAHARA T, ARAHATA K, OMURA S, MOMOI T: Enhancement of cpp32-like activity in the tnf-treated u937 cells by the proteasome inhibitors. Biochem. Biophys. Res. Commun. (1996) 224:74–79.
   PubMedGoogle Scholar
• SHINOHARA K, TOMIOKA M, NAKANO H, TONES, ITO H, KAWASHIMA S: Apoptosis induction resulting from proteasome inhibition. Biochem. J (1996) 317:385–388.
   PubMedGoogle Scholar
• LOPES UG, ERHARDT P, YAO R, COOPER GM: p53-Dependent induction of apoptosis by proteasome inhibitors. J Biol. Chem. (1997) 272:12893–12896.
   PubMed Web of Science ®Google Scholar
• •This paper describes a proteasome inhibitor able to induce p53-dependent apoptosis in rat-1 and pc12 cells.
   Google Scholar
• AN B, GOLDFARB RH, SIMAN R, DOU QP: Novel dipeptidyl proteasome inhibitors overcome bc1-2 protective function and selectively accumulate the cyclin-dependent kinase inhibitor p27 and induce apoptosis in transformed, but not normal, human fibroblasts. Cell Death Differ. (1998) 5:1062–1075.
   PubMed Web of Science ®Google Scholar
• •This publication reports that a proteasome inhibitor selectively induces p53-independent apoptosis in tumour and transformed, but not normal, cells and that proteasome inhibition is sufficient to induce apoptosis in human leukaemia Jurkat T-cells overexpressing Bc1–2.
   Google Scholar
• SUGAWARA K, HATORI M, NISHIYAMA Y et al.: Eponemycin, a new antibiotic active against B16 melanoma. I. Production, isolation, structure and biological activity. J Antibiot. (Tokyo) (1990) 43:8–18.
   PubMed Web of Science ®Google Scholar
• MENG L, KWOK BH, SIN N, CREWS CM: Eponemycin exerts its antitumor effect through the inhibition of proteasome function. Cancer Res. (1999) 59:2798–2801.
   PubMed Web of Science ®Google Scholar
• •This paper demonstrates that proteasome subunits LMP2 and LMP7 are specific targets of the antitumour compound eponemycin.
   Google Scholar
• ORLOWSKI RZ, ESWARA JR, LAFOND-WALKER A, GREVER, ORLOWSKI M, DANG CV: Tumor growth inhibition induced in a murine model of human Burkitt's lymphoma by a proteasome inhibitor. Cancer Res. (1998) 58:4342–4348.
   PubMed Web of Science ®Google Scholar
• •This paper reports that transformed fibroblasts are more sensitive to apoptosis induced by proteasome inhibitors than non-transformed cells and that tumour inhibition by proteasome inhibitors in vivo is associated with enhanced apoptotic cell death.
   Google Scholar
• DELIC J, MASDEHORS P, OMURA S et al.: The proteasome inhibitor lactacystin induces apoptosis and sensitizes chemo- and radioresistant human chronic lympho-cy tic leukaemia lymphocytes to TNF-alp h a-in itiated apoptosis. Br. J Cancer (1998) 77:1103–1107.
   PubMed Web of Science ®Google Scholar
• MASDEHORS P, OMURA S, MERLE-BERAL H et al.: Increased sensitivity of CLL-derived lymphocytes to apoptotic death activation by the proteasome-specific inhibitor lactacystin. Br.J Haematol (1999) 105:752–757.
   PubMed Web of Science ®Google Scholar
• SPATARO V, TODA T, CRAIG R et al: Resistance to drugs and ultraviolet light conferred by overexpression of a novel human 26 S proteasome subunit. J. Biol. Chem. (1997) 272:30470–30475.
   PubMed Web of Science ®Google Scholar
• •This paper suggests involvement of the proteasome in development of drug resistance of human cancers.
   Google Scholar
• HERRMANN JL, BRIONES F, JR., BRISBAY S, LOGOTHETISCJ, MCDONNELL TJ: Prostate carcinoma cell death resulting from inhibition of proteasome activity is independent of functional Bc1-2 and p 53 . Oncogene (1998) 17:2889–2899.
   Google Scholar
• LI B, DOU QP: Bax degradation by the ubiquitin/proteasome-dependent pathway: involve-ment in tumor survival and progression. Proc. Natl. Acad. ScL USA (2000) 97:3850–3855.
   PubMed Web of Science ®Google Scholar
• •This report suggests a correlation between the inhibition of Box degradation by a proteasome inhibitor and the drug ability to induce tumour cell death.
   Google Scholar
• DOU QP, MCGUIRE TF, PENG Y, AN B: Proteasome inhibition leads to significant reduction of Bcr-Abl expression and subsequent induction of apoptosis in K562 human chronic myelogenous leukemia cells. J. Pharmacol. Exp. Ther. (1999) 289:781–790.
   PubMed Web of Science ®Google Scholar
• FANELLI M, MINUCCI S, GELMETTI V, NERVI C,GAMBACORTI-PASSERINI C: Constitutive degradation of PML/RARalpha through the proteasome pathway mediates retinoic acid resistance. Blood (1999) 93:1477–1481.
   PubMed Web of Science ®Google Scholar
• CHANDRA J, NIEMER I, GILBREATH J et al.: Proteasomeinhibitors induce apoptosis in glucocorticoid-resistant chronic lymphocytic leukemic lymphocytes. Blood (1998) 92:4220–4229.
   PubMed Web of Science ®Google Scholar
• OGISO Y, TOMIDA A, LEI S, OMURA S, TSURUO T: Protea-some inhibition circumvents solid tumor resistance to topoisomerase II-directed drugs. Cancer Res. (2000) 60:2429–2434.
   PubMed Web of Science ®Google Scholar
• •This publication reports that proteasome inhibitors were able to increase the toxicity of topoisomerase II-directed drugs in resistant solid tumour cells, but had no effect against the non-topoisomerase II-targeted drugs. The ability of proteasome inhibitors to sensitise these drug-resistant tumour cells correlated with their ability to inhibit depletion of topoisomerase II.
   Google Scholar
• ADAMS J, PALOMBELLA VJ, SAUSVILLE EA et al.: Protea- inhibitors: a novel class of potent and effective anti-tumor agents. Cancer Res. (1999) 59:2615–2622.
   PubMed Web of Science ®Google Scholar
• •This paper reports inhibition of tumour growth in mice by injected proteasome inhibitor and a rapid and widespread distribution of the proteasome inhibitor in vivo.
   Google Scholar
• AGHAJANIAN C, ELLIOT P, ADAMS J, SOIGNET S, SPRIGGS: Phase I Trial of the Proteasome Inhibitor PS-341 in Advanced Malignancy. 36th ASCO Meeting, New Orleans, USA (2000):736.
   Google Scholar
• PAPANDREOU CN, PAGLIARO L, MILLIKAN R et al: Phase Study of PS-341, a Novel Proteasome Inhibitor, in Patients with Advanced Malignancies. 36th ASCO Meeting, New Orleans, USA (2000738.
   Google Scholar
• OIKAWA T, SASAKI T, NAKAMURA M et al: The protea-some is involved in angiogenesis. Biochem. Biophys. Res. Commun. (1998) 246:243–248.
   PubMed Web of Science ®Google Scholar
• LI J, POST M, VOLK R SM et al.: PR39, a peptide regulator of an gio gen esis. Nature Med. (2000) 6:49–55.
   Google Scholar
• GOURLEY M, WILLIAMSON JS: Angiogenesis: new targets for the development of anticancer chemotherapies. Curr. Pharm. Des. (2000) 6:417–439.
   PubMed Web of Science ®Google Scholar
• BERNSEN HJ, VAN DER KOGEL AJ: Antiangiogenic therapy in brain tumor models. J. Neurooncol (1999) 45:247–255.
   PubMed Web of Science ®Google Scholar
• FENTEANY G, STANDAERT RF, LANE WS, CHOI S, SCHREIBER SL: Inhibition of proteasome activities and subunit-specific amino-terminal threonine modifica-tion by lactacystin. Science (1995) 268:726–731.
   PubMed Web of Science ®Google Scholar
• DICK LR, CRUIKSHANK AA, GRENIER L, MELANDRI FD,NUNES SL, STEIN RL: Mechanistic studies on the inacti-vation of the proteasome by lactacystin: a central role for clasto-lactacystin beta-lactone. J. Biol. Chem. (1996) 271:7273–7276.
   PubMed Web of Science ®Google Scholar
• DICK LR, SRUIKSHANK AA, DESTREE AT et al.: Mechanistic studies on the inactivation of the protea-some by lactacystin in cultured cells. J. Biol. Chem. (1997) 272:182–188.
   PubMed Web of Science ®Google Scholar
• GROLL M, DITZEL L, LOWE J et al.: Structure of 20S proteasome from yeast at 2.4 Ã resolution. Nature (1997) 386:463–471.
   Google Scholar
• GROETTRUP M, SCHMIDTKE G: Selective proteasome inhibitors: modulators of antigen presentation? Drug Discov. Today (1999) 4:63–71.
   Google Scholar
• LEE DH, GOLDBERG AL: Proteasome inhibitors: valuable new tools for cell biologists. Trends. Cell Biol. (1998) 8:397–403.
   PubMed Web of Science ®Google Scholar
• LOWE J, STOCK D, JAP B, ZWICKI P, BAUMEISTER W, HUBBER R.: Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution. Science (1995) 268:533–539.
   Google Scholar
• SIN N, KIM KB, ELOFSSON M et al.: Total synthesis of the potent proteasome inhibitor epoxomicin: a useful tool for understanding proteasome biology. Bioorg. Med. Chem. Lett. (1999) 9:2283–2288.
   PubMed Web of Science ®Google Scholar
• GROLL M, KIM KB, KAIRIES N, HUBER R, CREWS CM: Crystal structure of epoxomicin:205 proteasome reveals a molecular basis for selectivity of acbt-epoxyketon proteasome inhibitors. j Am. Chem. Soc. (2000) 122:1237–1238.
   Web of Science ®Google Scholar
• ADAMS J, PALOMBELLA VJ, SAUVILLE EA et al: Potent and selective inhibitors of the proteasome: dipeptidyl boronic acids. Bioorg. Med. Chem. Lett. (1998) 8:333–338.
   PubMed Web of Science ®Google Scholar
• KETTNER CA, SHENVI AB: Inhibition of the serine proteases leukocyte elastase, pancreatic elastase, cathepsin G and chymotrypsin by peptide boronic acids. J. Biol. Chem. (1984) 259:15106–15114.
   PubMedGoogle Scholar
• LUM RT, NELSON MG, JOLY A et al: Selective inhibition of the chymotrypsin-like activity of the 20S protea-some by 5-methoxy-1-indanone dipeptide benzamides. Bioorg. Med. Chem. Lett. (1998) 8:209–214.
   PubMedGoogle Scholar
• LUM RT, KERWAR SS, MEYER SM et al.: Anew structural class of proteasome inhibitors that prevent NF-kappa B activation. Biochem. Pharmacol (1998) 55:1391–1397.
   PubMed Web of Science ®Google Scholar
• LYNAS JF, HARRIOTT P, HEALY A et al.: Inhibitors of the chymotrypsin-like activity of proteasome based on di-and tri-peptidyl alpha-keto aldehydes (glyoxals). Bioorg. Med. Chem. Lett. (1998) 8:373–378.
   PubMed Web of Science ®Google Scholar
• ISOE T, NAITO M, HIRAI R et al.: Inhibition of ubiquitin-ATP-dependent pro teolysis and ubiquitination by cisplatin. AntiCancer Res. (1991) 11:1905–1909.
   PubMed Web of Science ®Google Scholar
• ISOE T, NAITO M, SHIRAI A et al.: Inhibition of different steps of the ubiquitin system by cisplatin and aclaru-bicin. Biochim Biophys Acta (1992) 1117:131–135.
   PubMed Web of Science ®Google Scholar
• FIGUEIREDO-PEREIRA ME, CHEN WE, LI J et al: The antitumor drug aclacinomycin A, which inhibits the degradation of ubiquitinated proteins, shows selectivity for the chymotrypsin-like activity of the bovine pituitary 20 S proteasome. J. Biol. Chem. (1996) 271:16455–16459.
   PubMed Web of Science ®Google Scholar