Targeting the proteasome in mantle cell lymphoma: A promising therapeutic approach

References

• Harris N L, Jaffe E S, Stein H, Banks P M, Chan J KC, Cleary M L, et al. A revised European – American classification of lymphoid neoplasms: a proposal from the International Lymphoma Study Group. Blood 1994; 84: 1361–1392
   PubMed Web of Science ®Google Scholar
• Harris N L, Jaffe E S, Diebold J, Flandrin G, Müller-Hermelink H K, Vardiman J, et al. World Health Organization classification of neoplastic diseases of the hematopoetic and lymphoid tissues: report of the clinical advisory committee meeting. Journal of Clinical Oncology 1999; 17: 3835–3849
   PubMed Web of Science ®Google Scholar
• Bosch F, Jares P, Campos E, Lopez- Guilermo A, Piris M A, Villamor N, et al. Prad-1/Cyclin D1 gene overexpression in chronic lymphoproliferative disorders: a highly specific marker of mantle cell lymphoma. Blood 1994; 84: 2726–2732
   PubMed Web of Science ®Google Scholar
• Ott M, Bartkova J, Bartek J, Dürr A, Fischer L, Ott G, et al. Cyclin D1 expression in mantle cell lymphoma is accompanied by downregulation of cyclin D3 and is not related to the proliferative activity. Blood 1997; 90: 3154–3159
   PubMed Web of Science ®Google Scholar
• Zukerberg L R, Benedict W F, Arnold A, Dyson N, Harlow E, Harris N L. Expression of the retinoblastoma protein in low-grade B-cell lymphoma: relationship to cyclin D1. Blood 1996; 88: 268–276
   PubMed Web of Science ®Google Scholar
• Campo E, Raffelnd M, Jaffe E S. Mantle-cell lymphoma. Seminars in Haematology 1999; 36: 115–127
   PubMed Web of Science ®Google Scholar
• Quintanilla-Martinez L, Davies-Hill T, Fend F, Calzada-Wack J, Sorbara L, Campo E, et al. Sequestration of p27kip1 protein by cyclin D1 in typical and blastic variants of mantle cell lymphomas (MCL): implications for pathogenesis. Blood 2002; 101: 3181–3187
   PubMed Web of Science ®Google Scholar
• Bernard M, Gressin R, Drenou B, Branger B, Caulet-Maugendre S, Tass P, et al. Blastic variant of mantle cell lymphoma: a rare but highly aggressive subtype. Leukemia 2001; 15: 1785–1791
   PubMed Web of Science ®Google Scholar
• Greiner T C, Moynihan M J, Chan W C, Lytle D M, Pedersen A, Anderson J R, Weisenburger D D. P53 mutations in mantle cell lymphoma are associated with variant cytology and predict a poor prognosis. Blood 1996; 87: 4302–4310
   PubMed Web of Science ®Google Scholar
• Pinyol M, Hernandez L, Cazorla M, Balbin M, Jares P, Fernandez P L, et al. Deletions and loss of expression of p16 and p21 genes are associated with aggressive variants of mantle cell lymphoma. Blood 1997; 89: 272–280
   PubMed Web of Science ®Google Scholar
• Gronbaek K, Nedergaard T, Andresen M K, Straten P T, Guldberg P, Moller P, et al. Concurrent disruption of cell cycle associated genes in mantle cell lymphoma: a genotypic and phenotypic study of cyclin D1, 16, 15, 53 and pRB. Leukemia 1998; 12: 1266–1271
   PubMed Web of Science ®Google Scholar
• Leonard J P, Schattner E J, Coleman M. Biology and management of mantle cell lymphoma. Current Opinion in Oncology 2001; 13: 342–347
   PubMed Web of Science ®Google Scholar
• Freedman A, Neuberg D, Gribben J G, Mauch P, Soiffer R J, Fisher D C, et al. High-dose chemoradiotherapy and anti-B-cell monoclonal antibody-purged autologous bone marrow transplantation in mantle-cell lymphoma: no evidence for long term remission. Journal of Clinical Oncology 1998; 16: 13–18
   PubMed Web of Science ®Google Scholar
• Howard O M, Gribben J G, Neuberg D S, Grossbard M, Poor C, Janicek M J, Shipp M A. Rituximab and CHOP induction therapy for newly diagnosed mantle-cell lymphoma. Molecular complete responses are not predictive of progression free survival. Journal of Clinical Oncology 2002; 20: 1288–1294
   PubMed Web of Science ®Google Scholar
• Ciechanover A. The ubiquitin-proteasome proteolytic pathway. Cell 1994; 79: 13–21
   PubMed Web of Science ®Google Scholar
• Hershko A, Ciechanover A. The ubiquitin system. Annual Reviews in Biochemistry 1998; 67: 425–479
   PubMed Web of Science ®Google Scholar
• Groll M, Ditzel L, Lowe J, Stock D, Bochtler M, Bartunik H D, et al. Structure of 20S proteasome from yeast at 2.4 Å resolution. Nature 1997; 386: 463–471
   PubMed Web of Science ®Google Scholar
• Orlowski M, Cardozo C, Michaud C. Evidence for the presence of five distinct proteolytic components in the pituitary multicatalytic proteasome complex. Properties of two components cleaving bonds on the carboxyl side of branched chain and small neutral amino acids. Biochemistry 1993; 32: 1563–1572
   PubMed Web of Science ®Google Scholar
• Lowe J, Stock D, Jap B, Zwickl P, Baumeister W, Huber R. Crystal structure of the 20S proteasome from the archaeon T. scidophilum at 3.4 Å resolution. Science 1995; 268: 533–539
   PubMed Web of Science ®Google Scholar
• Stock D, Ditzel L, Baumeister W, Huber R, Lowe J. Catalytic mechanism of the 20S proteasome of Thermoplasma acidophilum revealed by X-ray crystallography. Cold Spring Harbour Symposium on Quantum Biology 1995; 60: 525–532
   PubMedGoogle Scholar
• Nussbaum A K, Dick T P, Keilholz W, Schirle M, Stevanovic S, Dietz K, et al. Cleavage motifs of the yeast 20S proteasome beta subunits deduced from digest of enolase 1. Proceedings of the National Academy of Sciences (USA) 1998; 95: 12504–12509
   PubMed Web of Science ®Google Scholar
• Cayrol C, Ducommun B. Interaction with cyclin-dependent kinases and PCNA modulates proteasome-dependent degradation of p21. Oncogene 1998; 17: 2437–2444
   PubMed Web of Science ®Google Scholar
• Pagano M, Tam S W, Theodoras A M, Beer-Romero P, Del Sal G, Chau V, et al. Role of the ubiquitin-proteasome pathway in regulating abundance of the cyclin dependent kinase inhibitor p27. Science 1995; 269: 682–685
   PubMed Web of Science ®Google Scholar
• King R W, Deshaies R J, Peters J M, Kirschner M W. How proteolysis drives the cell cycle. Science 1996; 274: 1652–1659
   PubMed Web of Science ®Google Scholar
• Clurman B E, Sheaff R J, Thress K, Groudine M, Roberts J M. Turnover of cyclin E by the ubiquitin – proteasome pathway is regulated by cdk2 binding and cyclin phosphorylation. Genes Development 1996; 10: 1979–1990
   PubMed Web of Science ®Google Scholar
• Diehl J A, Zindy F, Sherr C J. Inhibition of cyclin D1 phosphorylation on threonine-286 prevents its rapid degradation via the ubiquitin – proteasome pathway. Genes Development 1997; 11: 957–972
   PubMed Web of Science ®Google Scholar
• Sudakin V, Ganoth D, Dahan A, Heller H, Hershko J, Luca F C, et al. The cyclosome, a large complex containing cyclin-selective ubiquitin ligase activity, targets cyclins for destruction at the end of mitosis. Molecular Biology of the Cell 1995; 6: 185–197
   PubMed Web of Science ®Google Scholar
• Donzelli M, Squatrito M, Ganoth D, Hershko A, Pagano M, Draetta G F. Dual mode of degradation of Cdc25A phosphatase. EMBO Journal 2002; 21: 4875–4884
   PubMed Web of Science ®Google Scholar
• Chen F, Zhang Z, Bower J, Lu Y, Leonard S S, Ding M, et al. Arsenite-induced Cdc25C degradation is through the KEN-box and ubiquitin – proteasome pathway. Proceedings of the National Academy of Sciences (USA) 2002; 99: 1990–1995
   PubMed Web of Science ®Google Scholar
• Maki C G, Huibregtse J M, Howley P M. In vivo ubiquitination and proteasome-mediated degradation of p53(1). Cancer Research 1996; 56: 2649–2654
   PubMed Web of Science ®Google Scholar
• Serrano M, Hannon G J, Beach D. A new regulatory motif in cell-cycle control causing specific inhibition of cyclin D/CDK4. Nature 1993; 366: 704–707
   PubMed Web of Science ®Google Scholar
• Fuchs S Y, Xie B, Adler V, Fried V A, Davis R J, Ronai Z. c-Jun NH2-terminal kinases target the ubiquitination of their associated transcription factors. Journal of Biological Chemistry 1997; 272: 32163–32168
   PubMed Web of Science ®Google Scholar
• Salvat C, Jariel-Encontre I, Acquaviva C, Omura S, Piechaczyk M. Differential directing of c-Fos and c-Jun proteins to the proteasome in serum-stimulated mouse embryo fibroblasts. Oncogene 1998; 17: 327–337
   PubMed Web of Science ®Google Scholar
• Latres E, Chiaur D S, Pagano M. The human F box protein beta-Trcp associates with the Cul1/Skp1 complex and regulates the stability of beta-catenin. Oncogene 1999; 18: 849–854
   PubMed Web of Science ®Google Scholar
• Hateboer G, Kerkhoven R M, Shvarts A, Bernards R, Beijersbergen R L. Degradation of E2F by the ubiquitin-proteasome pathway: regulation by retinoblastoma family proteins and adenovirus transforming proteins. Genes Development 1996; 10: 2960–2970
   PubMed Web of Science ®Google Scholar
• Smith E J, Leone G, Nevins J R. Distinct mechanisms control the accumulation of the Rb-related p107 and p130 proteins during cell growth. Cell Growth Difference 1998; 9: 297–303
   PubMedGoogle Scholar
• Gross-Mesilaty S, Hargrove J L, Ciechanover A. Degradation of tyrosine aminotransferase (TAT) via the ubiquitin-proteasome pathway. FEBS Letters 1997; 405: 175–180
   PubMed Web of Science ®Google Scholar
• Ferris D K, Maloid S C, Li C C. Ubiquitination and proteasome mediated degradation of polo-like kinase. Biochemistry & Biophysics Research Communications 1998; 252: 340–344
   PubMed Web of Science ®Google Scholar
• Desai S D, Liu L F, Vazquez-Abad D, D'Arpa P. Ubiquitin-dependent destruction of topoisomerase I is stimulated by the antitumor drug camptothecin. Journal of Biological Chemistry 1997; 272: 24159–24164
   PubMed Web of Science ®Google Scholar
• Marshansky V, Wang X, Bertrand R, Luo H, Duguid W, Chinnadurai G. Proteasomes modulate balance among proapoptotic and antiapoptotic Bcl-2 family members and compromise functioning of the electron transport chain in leukemic cells. Journal of Immunology 2001; 166: 3130–3142
   PubMed Web of Science ®Google Scholar
• Alkalay I, Yaron A, Hatzubai A, Orian A, Ciechanover A, Ben-Neriah Y. Stimulation-dependent I-κ-B-α phosphorylation marks the NF-κ-B inhibitor for degradation via the ubiquitin-proteasome pathway. Proceedings of the National Academy of Sciences (USA) 1995; 92: 10599–10603
   PubMed Web of Science ®Google Scholar
• Baldi L, Brown K, Franzoso G, Siebenlist U. Critical role for lysines 21 and 22 in signal-induced, ubiquitin-mediated proteolysis of I-κ-B-α. Journal of Biological Chemistry 1996; 271: 376–379
   PubMed Web of Science ®Google Scholar
• Chen Z, Hagler J, Palombella V J, Melandri F, Scherer D, Ballard D, et al. Signal-induced site-specific phosphorylation targets I-κ-B-α to the ubiquitin-proteasome pathway. Genes Development 1995; 9: 1586–1597
   PubMed Web of Science ®Google Scholar
• Lin Y C, Brown K, Siebenlist U. Activation of NF-κ-B requires proteolysis of the inhibitor I-κ-B-α: signal-induced phosphorylation of I-κ-B-α alone does not release active NF-κ-B. Proceedings of the National Academy of Sciences (USA) 1995; 92: 552–556
   PubMed Web of Science ®Google Scholar
• Roff M, Thompson J, Rodriguez M S, Jacque J M, Baleux F, Arenzana-Seisdedos F, et al. Role of I-κ-B-α ubiquitination in signal-induced activation of NF-κ-B in vivo. Journal of Biological Chemistry 1996; 271: 7844–7850
   PubMed Web of Science ®Google Scholar
• An W G, Hwang S G, Trepel J B, Blagosklonny M V. Protease inhibitor-induced apoptosis: accumulation of wt p53, p21 WAF1/CIP1, and induction of apoptosis are independent markers of proteasome inhibition. Leukemia 2000; 14: 1276–1283
   PubMed Web of Science ®Google Scholar
• Dietrich C, Bartsch T, Schanz F, Oesch F, Wieser R J. P53-dependent cell cycle arrest induced by N-acetyl-L-leucinyl-L-norleucinal in platlet-derived growth factor-stimulated human fibroblasts. Proceedings of the National Academy of Sciences (USA) 1996; 93: 10815–10819
   PubMed Web of Science ®Google Scholar
• Adams J, Palombella V J, Sausville E A, Johnson J, Destree A, Lazarus D D, et al. Proteasome inhibitors: a novel class of potent and effective antitumor agents. Cancer Research 1999; 59: 2615–2622
   PubMed Web of Science ®Google Scholar
• Beg A A, Baltimore D. NF-kappa B in preventing TNF-alpha induced cell death. Science 1996; 274: 782–784
   PubMed Web of Science ®Google Scholar
• Van Antwerp D J, Martin S J, Kafri T, Green D R, Verma I M. Suppression of TNF-alpha-induced apoptosis by NF-kappa B. Science 1996; 274: 787–789
   PubMed Web of Science ®Google Scholar
• de Moissac D, Musapha S, Greenberg A H, Kirshenbaum L A. Bcl-2 activates the transcription factor NF-kappa-B through the degradation of the cytoplasmatic inhibitor I-kappa-B-alpha. Journal of Biological Chemistry 1998; 273: 23946–23951
   PubMed Web of Science ®Google Scholar
• Almond J B, Cohen G M. The proteasome: a novel target for cancer chemotherapy. Leukemia 2002; 16: 433–443
   PubMed Web of Science ®Google Scholar
• Ling Y, Liebes L, Jiang J, Holland J F, Elliott P J, Adams J, et al. Mechanisms of proteasome inhibitor PS-341-induced G2-M-phase arrest and apoptosis in human non-small cell lung cancer cell lines. Clinical Cancer Research 2003; 9: 1145–1154
   PubMed Web of Science ®Google Scholar
• Ling Y, Liebes L, Ng B, Buckley M, Elliott P J, Adams J, et al. PS-341, a novel proteasome inhibitor, induces Bcl-2 phosphorylation and cleavage in association with G2-M-phase arrest and apoptosis. Molecular Cancer Therapy 2002; 1: 841–849
   PubMed Web of Science ®Google Scholar
• Perez-Soler R, Ling Y H, Ellitott P J. Effect of the proteasome inhibitor PS-341 on cell cycle progression and bcl-2: a potentially unique mechanism of action. Clinical Cancer Research 2000; 6: 4549s
   Google Scholar
• Hirama T, Koeffler P. Role of the cyclin-dependent kinase inhibitors in the development of cancer. Blood 1995; 86: 841–854
   PubMed Web of Science ®Google Scholar
• Wagner E F, Hleb M, Hanna N, Sharma S. A pivotal role of cyclin D3 and cyclin-dependent kinase inhibitor p27 in the regulation of IL-2, IL-4- or IL-10-mediated human B cell proliferation. Journal of Immunology 1998; 161: 1123–1131
   PubMed Web of Science ®Google Scholar
• Bargonetti J, Manfredi J J. Multiple roles of the tumor suppressor p53. Current Opinion in Oncology 2002; 14: 86–91
   PubMed Web of Science ®Google Scholar
• Chen C, Edelstein L C, Gelinas C. The Rel/NF-κB family directly activates expression of the apoptosis inhibitor Bcl-xL. Molecular Cell Biology 2000; 20: 2687–2695
   PubMed Web of Science ®Google Scholar
• Wang C Y, Mayo M W, Korneluk R G, Goeddel D V, jun Baldwin A S. NF-κ-B antiapoptosis. Induction of TRAF1 and TRAF2 and c-IAP1 and c-IAP2 to suppress caspase-8 activation. Science 1998; 281: 1680–1683
   PubMed Web of Science ®Google Scholar
• Wang C Y, Guttridge D C, Mayo M W, Baldwin A S jun. NF-κ-B induces expression of the Bcl-2 homologue A1/Bfl-1 to preferentially suppress chemotherapy-induced apoptosis. Molecular Cell Biology 1999; 19: 5923–5929
   PubMed Web of Science ®Google Scholar
• Zong W X, Edelstein L C, Chen C, Bash J, Gelinas C. The pro survival Bcl-2 homologBfl-1/A1 is a direct transcriptional target of NF-κ-B that blocks TNF α-induced apoptosis. Genes Development 1999; 13: 382–387
   PubMed Web of Science ®Google Scholar
• Brown K, Park S, Kanno T, Franzoso G, Siebenlist U. Mutual regulation of the transcriptional activator NF-κ-B and its inhibitor, Iκ B α. Proceedings of the National Academy of Sciences (USA) 1993; 90: 2532–2536
   PubMed Web of Science ®Google Scholar
• Adams J, Palombella V J, Elliott P J. Proteasome inhibition: a new strategy in cancer treatment. Investigations in New Drugs 2000; 18: 109–121
   PubMed Web of Science ®Google Scholar
• Chiarle R, Budel L M, Skolnik J, Frizzera G, Chilosi M, Corato A, et al. Increased proteasome degradation of cyclin-dependent kinase inhibitor p27 is associated with a decreased overall survival in mantle cell lymphoma. Blood 2000; 95: 619–626
   PubMed Web of Science ®Google Scholar
• Orlowski R Z, Stinchcombe T E, Mitchell B S, Shea T C, Baldwin A S, Stahl S, et al. Phase I trial of the proteasome inhibitor PS-341 in patients with refractory hematologic malignancies. Journal of Clinical Oncology 2002; 22: 4420–4427
   Web of Science ®Google Scholar
• Orlowski R Z, Voorhees P M, Garcia R A, Hall M D, Kudrik F J, Johri A R, et al. Phase I trial of the proteasome inhibitor Bortezomib and pegylated liposomal doxorubicin in patients with advanced hematologic malignancies. Blood 2005; 105: 3058–3065
   PubMed Web of Science ®Google Scholar
• O'Connor O A, Wright J, Moskowitz C, Muzzy J, MacGregor-Cortelli, Stubblefield M, et al. Phase II clinical experience with the novel proteasome inhibitor Bortezomib in patients with indolent Non-Hodgkin's lymphoma and mantle cell lymphoma. Journal of Clinical Oncology 2005; 23: 676–684
   PubMed Web of Science ®Google Scholar
• Goy A, Younes A, McLaughlin P, Pro B, Romaguera J E, Hagemeister F, et al. Phase II study of proteasome inhibitor bortezomib in relapsed or refractory B-cell Non-Hodgkin lymphoma. Journal of Clinical Oncology 2005; 23: 667–675
   PubMed Web of Science ®Google Scholar
• Assouline S, Belch A, Sehn L, Kouroukis C T, Gascoyne R, Meyer R, Powers J. A phase II study of bortezomib in patients with mantle cell lymphoma. Poster session, 3358, 578-III, Ash meeting.
   Google Scholar
• Kisselev A F, Goldberg A L. Proteasome inhibitors. From research tools to drug candidates. Chemical Biology 2001; 8: 739–758
   PubMed Web of Science ®Google Scholar
• Masdehors P, Omura S, Merle-Beral H, Mentz F, Cosset J M, Dumont J, et al. Increased sensitivity of CLL-derived lymphocytes to apoptotic death activation by the proteasome-specific inhibitor lactacystin. British Journal of Haematology 1999; 105: 752–757
   PubMed Web of Science ®Google Scholar
• Adams J. Development of the proteasome inhibitor PS-341. Oncologist 2002; 7: 9–16
   PubMed Web of Science ®Google Scholar
• Drexler H C. Activation of the cell death program by inhibition of proteasome function. Proceedings of the National Academy of Sciences (USA) 1997; 94: 855–860
   PubMed Web of Science ®Google Scholar
• Fenteany G, Standaert R F, Lane W S, Choi S, Corey E J, Schreiber S L. Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin. Science 1995; 268: 726–731
   PubMed Web of Science ®Google Scholar
• Dick L R, Cruickshank A A, Grenier L, Melandri F D, Nunes S L, Stein R L. Mechanistic studies on the inactivation of the proteasome by lactacystin in cultured cells. Journal of Biological Chemistry 1996; 271: 7273–7276
   PubMed Web of Science ®Google Scholar
• Pham L V, Tamayo A T, Yoshimura L C, Lo P, Ford R J. Inhibition of constitutive NF-κ-B activation in mantle cell lymphoma B cells leads to induction of cell cycle arrest and apoptosis. The Journal of Immunology 2003; 171: 88–95
   PubMed Web of Science ®Google Scholar
• Cusack J C. Rationale for the treatment of solid tumors with the proteasome inhibitor bortezomib. Cancer Treatment Reviews 2003; 29: 21–31
   PubMed Web of Science ®Google Scholar
• Hideshima T, Richardson P, Chauhan D, Palombella V J, Elliott P J, Adams J, et al. The proteasome inhibitor PS-341 inhibits growth, induces apoptosis, and overcomes drug resistance in human multiple myeloma cells. Cancer Research 2001; 61: 3071–3076
   PubMed Web of Science ®Google Scholar
• Castillo R, Mascarenhas J, Telford W, Chadburn A, Friedman S M, Schattner E J. Proliferative response of mantle cell lymphoma cells stimulated by CD40 ligation and IL-4. Leukemia 2000; 14: 292–298
   PubMed Web of Science ®Google Scholar
• Bogner C, Ringshausen I, Schneller F, Fend F, Quintanilla-Martinez L, Häcker G, et al. Inhibition of the proteasome induces cell cycle arrest and apoptosis in mantle cell lymphoma cells. British Journal of Hematology 2003; 122: 260–268
   PubMed Web of Science ®Google Scholar
• O'Connor O A. The emerging role of bortezomib in the treatment of indolent non-Hodgkin's and mantle cell lymphomas. Current Treatment Options in Oncology 2004; 5: 269–281, Review
   PubMedGoogle Scholar
• Quintanilla-Martinez L, Thieblemont C, Fend F, Kumar S, Pinyol M, Campo E, et al. Mantle cell lymphomas lack expression of p27Kip1, a cyclin-dependent kinase inhibitor. American Journal of Pathology 1998; 153: 175–182
   PubMed Web of Science ®Google Scholar
• Baeuerle P A, Baltimore D. NF-κ-B: then years after. Cell 1996; 87: 13
   PubMed Web of Science ®Google Scholar
• Kordes U, Krappmann D, Heissmeyer V, Ludwig W D, Scheidereit C. Transcription factor NF-κ-B is constitutively activated in acute lymphoblastic leukemia cells. Leukemia 2000; 14: 399–402
   PubMed Web of Science ®Google Scholar
• Mitsiades N, Mitsiades C S, Richardson P G, Poulaki V, Tai Y T, Chauhan D, et al. The proteasome inhibitor PS-341 patentiates sensitivity of multiple myeloma to conventionally chemotherapeutic agents: therapeutic applications. Blood 2003; 101: 2377–2380
   PubMed Web of Science ®Google Scholar
• Cheng E H, Kirsch D G, Clem R J, Ravi R, Kastan M B, Bedi A, et al. Conversion of Bcl-2 to a Bax-like death effector caspases. Science 1997; 278: 1966
   PubMed Web of Science ®Google Scholar
• Zhang X, Lin H, Chen C, Chen B D. Inhibition of ubiquitin proteasome pathway activates a caspase-3-like protease and induces Bcl-2 cleavage in human M-07e leukaemic cells. Biochemistry Journal 1999; 1340: 127
   Web of Science ®Google Scholar
• Martinou J C, Desagher S, Antonsson B. Cytochrome c release from mitochondria: all or nothing. Natural Cell Biology 2002; 2: 601
   Google Scholar
• Ling Y, Liebes L, Ng B, Buckley M, Elliott P J, Adams J, et al. PS-341, a novel proteasome inhibitor, induces Bcl-2 phosphorylation and cleavage in association with G2-M-phase arrest and apoptosis. Molecular Cancer Therapy 2002; 1: 841–849
   PubMed Web of Science ®Google Scholar
• Perez-Soler R, Ling Y H, Elliott P J. Effect of the proteasome inhibitor PS-341 on cell cycle progression and bcl-2: a potentially unique mechanism of action. Clinical Cancer Research 2000; 6: 4549s
   Google Scholar
• Herr I, Debatin K M. Cellular stress response and apoptosis in cancer therapy. Blood 2001; 98: 2603–2614
   PubMed Web of Science ®Google Scholar
• Almond J B, Snowden R T, Hunter A, Dinsdale D, Cain K, Cohen G M. Proteasome inhibitor-induced apoptosis of B-chronic lymphocytic leukemia cells involves cytochrome c release and caspase activation, accompanied by formation of an approximately 700 kDa Apaf-1containing apoptosome complex. Leukemia 2001; 15: 1388–1397
   PubMed Web of Science ®Google Scholar
• Richardson P G, Barlogie B, Berenson J, Singhal S, Jagannath S, Irwin D, et al. A phase 2 study of bortezomib in relapsed, refractory myeloma. New England Journal of Medicine 2003; 348: 2609–2617
   PubMed Web of Science ®Google Scholar
• Berenson J R, Jagannath S, Barlogie B, Siegel D, Alexanian R, Irwin D, et al. Experience with long-term therapy using the proteasome inhibitor, bortezomib, in advanced multiple myeloma (MM). Proceedings of the American Society of Clinical Oncology 2003; 22: 581
   Google Scholar
• Jagannath S, Durie B GM, Wolf J, Berenson J R, Singhal S, Irwin D, et al. Bortezomib (VELCADE, formerly PS-341) as firstline therapy in patients with multiple myeloma (MM). Blood 2003; 102: 452a
   Google Scholar
• Drucker B J, Schwartz L, Bacik J, Mazumdar M, Marion S, Motzer R J. Phase II trial of PS-341 shows response in patients with advanced renal cell carcinoma. Proceedings of the American Society of Clinical Oncology 2003; 22: 386
   Web of Science ®Google Scholar
• Maki R G, Kraft A, Demetri G D, Siegel C, Hirst S, Connors E, et al. A phase II multicenter study of proteasome inhibitor PS-341 (LDP-341, bortezomib) for untreated recurrent or metastatic soft tissue sarcoma (STS); CTEP study 1757. Proceedings of the American Society of Clinical Oncology 2003; 22: 819
   Google Scholar
• Stevenson J, Nho C W, Schick J. Phase II clinical/pharmacodynamic trial of the proteasome inhibitor PS-341 in advanced nonsmall cell lung cancer. Proceedings of the American Society of Clinical Oncology 2003; 22: 202
   Web of Science ®Google Scholar
• Cheson B D. New drug development in non-Hodgkin lymphomas. Current Oncology Reports 2001; 3: 250–259
   PubMedGoogle Scholar
• CTEP, NCI. Common toxicity criteria manual, Version 2.0. National Cancer Institute, Bethesda, MD 1999; 1–35
   Google Scholar
• Cheson B D, Horning S J, Coiffier B, Shipp M A, Fisher R I, Connors J M, et al. Report of an International Workshop to standardize response criteria for non-Hodgkin's lymphoma. Journal of Clinical Oncology 1999; 17: 1244–1253
   PubMed Web of Science ®Google Scholar
• Cheson B D, Bennett J M, Grever M, Kay N, Keating M J, O'Brien S, et al. National Cancer Institute-sponsored Working Group guidelines for chronic lymphocytic leukemia. Revised guidelines for diagnosis and treatment. Blood 1996; 87: 4990–4997
   PubMed Web of Science ®Google Scholar