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Original Articles: Research

AUY922 effectively targets against activated B cell subtype of diffuse large B-cell lymphoma and low-grade lymphoma cells harboring genetic alteration-associated nuclear factor-κB activation

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Pages 2674-2682 | Received 22 Jun 2014, Accepted 30 Nov 2014, Published online: 21 Jan 2015

References

  • Surveillance, Epidemiology and End Results. Available from: http://seer.cancer.gov/
  • Morton LM, Wang SS, Devesa SS, et al. Lymphoma incidence patterns by WHO subtype in the United States. Blood 2006;107: 265–276.
  • Carreon JD, Morton LM, Devesa SS, et al. Incidence of lymphoid neoplasms by subtype among six Asia ethnic groups in the United States, 1996-2004. Cancer Causes Control 2008;19:1171–1181.
  • Feugier P, Van Hoof A, Sebban C, et al. Long term results of the R-CHOP study in the treatment of elderly patients with diffuse large B cell lymphoma: a study by the groupe d’Etude des Lymphomes del’Adulte. J Clin Oncol 2005;23:4117–4126.
  • Alizadeh AA, Eisen MB, Davis RE, et al. Distinct types of diffuse large B-cell lymphoma identified by gene expression profiling. Nature 2000;403:503–511.
  • Lenz G, Wright GW, Emre NC, et al. Molecular subtypes of diffuse large B-cell lymphoma arise by distinct genetic pathways. Proc Natl Acad Sci USA 2008;105:13520–13525.
  • Rosenwald A, Wright G, Chan WC, et al.; Lymphoma/Leukemia Molecular Profiling Project. The use of molecular profiling to predict survival after chemotherapy for diffuse large B-cell lymphoma. N Engl J Med 2002;346:1937–1947.
  • Wright G, Tan B, Rosenwald A, et al. A gene expression-based method to diagnose clinically distinct subgroups of diffuse large B cell lymphoma. Proc Natl Acad Sci USA 2003;100:9991–9996.
  • Rosenwald A, Wright G, Leroy K, et al. Molecular diagnosis of primary mediastinal B cell lymphoma identifies a clinically favorable subgroups of diffuse large B cell lymphoma related to Hodgkin lymphoma. J Exp Med 2003;198:851–862.
  • Davis RE, Ngo VN, Lenz G, et al. Chronic active B-cell-receptor signaling in diffuse large B-cell lymphoma. Nature 2010;463:88–92.
  • Ngo VN, Young RM, Schmitz R, et al. Oncogenically active MYD88 mutations in human lymphoma. Nature 2011;470:115–119.
  • Ngo VN, Davis RE, Lamy L, et al. A loss-of-function RNA interference screen for molecular targets in cancer. Nature 2006;441:106–110.
  • Sagaert X, De Wolf-Peeters C, Noels H, et al. The pathogenesis of MALT lymphomas: where do we stand? Leukemia 2007;21:389–396.
  • Du MQ. MALT lymphoma: many roads lead to nuclear factor-κb activation. Histopathology 2011;58:26–38.
  • Hamoudi RA, Appert A, Ye H, et al. Differential expression of NF-κB target genes in MALT lymphoma with and without chromosome translocation: insights into molecular mechanism. Leukemia 2010;24:1487–1497.
  • Yeh KH, Kuo SH, Chen LT, et al. Nuclear expression of BCL10 or nuclear factor kappa B helps predict Helicobacter pylori-independent status of low-grade gastric mucosa-associated lymphoid tissue lymphomas with or without t(11;18)(q21;q21). Blood 2005;106: 1037–1041.
  • Kuo SH, Chen LT, Yeh KH, et al. Nuclear expression of BCL10 or nuclear factor kappa B predicts Helicobacter pylori-independent status of early stage, high-grade gastric mucosa-associated lymphoid tissue lymphomas. J Clin Oncol 2004;22:3491–3497.
  • Ciocca DR, Clark GM, Tandon AK, et al. Heat shock protein hsp70 in patients with axillary lymph node-negative breast cancer: prognostic implications. J Natl Cancer Inst 1993;85:570–574.
  • Jameel A, Skilton RA, Campbell TA, et al. Clinical and biological significance of HSP89 alpha in human breast cancer. Int J Cancer 1992;50:409–415.
  • Wu X, Wanders A, Wardega P, et al. Hsp90 is expressed and represents a therapeutic target in human oesophageal cancer using the inhibitor 17-allylamino-17-demethoxygeldanamycin. Br J Cancer 2009;100:334–343.
  • Ito T, Kawabe R, Kurasono Y, et al. Expression of heat shock proteins in squamous cell carcinoma of the tongue: an immunohistochemical study. J Oral Pathol Med 1998;27:18–22.
  • Kang GH, Lee EJ, Jang KT, et al. Expression of HSP90 in gastrointestinal stromal tumours and mesenchymal tumours. Histopathology 2010;56:694–701.
  • Ogata M, Naito Z, Tanaka S, et al. Overexpression and localization of heat shock proteins mRNA in pancreatic carcinoma. J Nippon Med Sch 2000;67:177–185.
  • Ghobrial IM, McCormick DJ, Kaufmann SH, et al. Proteomic analysis of mantle-cell lymphoma by protein microarray. Blood 2005;105:3722–3730.
  • Valbuena JR, Rassidakis GZ, Lin P, et al. Expression of heat-shock protein-90 in non-Hodgkin's lymphomas. Modern Pathol 2005;18:1343–1349.
  • Eccles SA, Massey A, Raynaud FI, et al. NVP-AUY922: a novel heat shock protein 90 inhibitor active against xenograft tumor growth, angiogenesis, and metastasis. Cancer Res 2008;68:2850–2860.
  • Ramanathan RK, Trump DL, Eiseman JL, et al. Phase I pharmacokinetic-pharmacodynamic study of 17-(allylamino)-17-demethoxygeldanamycin (17AAG, NSC 330507), a novel inhibitor of heat shock protein 90, in patients with refractory advanced cancers. Clin Cancer Res 2005;11:3385–3391.
  • Ronnen EA, Kondagunta GV, Ishill N, et al. A phase II trial of 17-(allylamino)- 17-demethoxygeldanamycin in patients with papillary and clear cell renal cell carcinoma. Invest New Drugs 2006;24:543–546.
  • Weigel BJ, Blaney SM, Reid JM, et al. A phase I study of 17-allylaminogeldanamycin in relapsed/refractory pediatric patients with solid tumors: a Children's Oncology Group study. Clin Cancer Res 2007;13:1789–1793.
  • Modi S, Stopeck AT, Gordon MS, et al. Combination of trastuzumab and tanespimycin (17-AAG, KOS-953) is safe and active in trastuzumab-refractory HER-2 overexpressing breast cancer: a phase I dose-escalation study. J Clin Oncol 2007;25:5410–5417.
  • de Bono JS, Kristeleit R, Tolcher A, et al. Phase I pharmacokinetic and pharmacodynamic study of LAQ824, a hydroxamate histone deacetylase inhibitor with a heat shock protein-90 inhibitory profile, in patients with advanced solid tumors. Clin Cancer Res 2008;14: 6663–6673.
  • Lancet JE, Gojo I, Burton M, et al. Phase I study of the heat shock protein 90 inhibitor alvespimycin (KOS-1022, 17-DMAG) administered intravenously twice weekly to patients with acute myeloid leukemia. Leukemia 2010;24:699–705.
  • Pacey S, Gore M, Chao D, et al. A phase II trial of 17-allylamino, 17-demethoxygeldanamycin (17-AAG, tanespimycin) in patients with metastatic melanoma. Invest New Drugs 2012;30:341–349.
  • Sequist LV, Gettinger S, Senzer NN, et al. Activity of IPI-504, a novel heat-shock protein 90 inhibitor, in patients with molecularly defined non-small-cell lung cancer. J Clin Oncol 2010;28:4953–4960.
  • Walker AR, Klisovic R, Johnston JS, et al. Pharmacokinetics and dose escalation of the heat shock protein inhibitor 17-AAG in combination with bortezomib in relapsed or refractory acute myeloid leukemia. Leuk Lymphoma 2013;54:1996–2002.
  • Grbovic OM, Basso AD, Sawai A, et al. V600E B-Raf requires the Hsp90 chaperone for stability and is degraded in response to Hsp90 inhibitors. Proc Natl Acad Sci USA 2006;103:57–62.
  • Zhang J, Grubor V, Love CL, et al. Genetic heterogeneity of diffuse large B-cell lymphoma. Proc Natl Acad Sci USA 2013;110:1398–1403.
  • Kuo SH, Weng WH, Chen ZH, et al. Establishment of a novel MALT lymphoma cell line, Ma-1, from a patient with t(14;18)(q32;q21)-positive Helicobactor pylori-independent gastric MALT lymphoma. Genes Chromosomes Cancer 2011;50:908–921.
  • Karin M. NF-κB as a critical link between inflammation and cancer. Cold Spring Harb Perspect Biol 2009;1:a000141.
  • Hertlein E, Wagner AJ, Jones J, et al. 17-DMAG targets the nuclear factor-κB family of proteins to induce apoptosis in chronic lymphocytic leukemia: clinical implications of HSP90 inhibition. Blood 2010;116: 45–53.
  • Nayar U, Lu P, Goldstein RL, et al. Targeting the Hsp90-associated viral oncoptoteome in gammaherpesvirus-associated malignancies. Blood 2013;122:2837–2847.
  • Walsby E, Pearce L, Burnett AK, et al. The Hsp90 inhibitor NVP-AUY922-AG inhibits NF-κB signaling, overcomes microenvironmental cytoprotection and is highly synergistic with fludarabine in primary CLL cells. Oncotarget 2012;3:525–534.
  • Böll B, Eltaib F, Reiners KS, et al. Heat shock protein 90 inhibitor BIIB021 (CNF2024) depletes NF-κB and sensitizes Hodgkin's lymphoma cells for natural killer cell-mediated cytotoxicity. Clin Cancer Res 2009;15:5108–5116.
  • Qing G, Yan P, Qu Z, et al. Hsp90 regulates processing of NF-kappa B2 p100 involving protection of NF-kappa B-inducing kinase (NIK) from autophagy-mediated degradation. Cell Res 2007;17: 520–530.
  • Gupta M, Ansell SM, Novak AJ, et al. Inhibition of histone deacetylase overcomes rapamycin-mediated resistance in diffuse large B-cell lymphoma by inhibiting Akt signaling through mTORC2. Blood 2009;114:2926–2935.
  • Vajpayee N, Thakral C, Gopaluni S, et al. Activation of mammalian target of rapamycin in diffuse large B-cell lymphoma: a clinicopathological study. Leuk Res 2012;36:1403–1409.
  • Petrich AM, Leshchenko V, Kuo PY, et al. Akt inhibitors MK-2206 and Nelfinavir overcome mTOR inhibitor resistance in diffuse large B cell lymphoma. Clin Cancer Res 2012;18:2534–2544.
  • Whitesell L, Lindquist SL. HSP90 and the chaperoning of cancer. Nat Rev Cancer 2005;5:761–772.
  • Okui T, Shimo T, Hassan NM, et al. Antitumor effect of novel HSP90 inhibitor NVP-AUY922 against oral squamous cell carcinoma. Anticancer Res 2011;31:1197–1204.
  • Lee JH, Gao J, Kosinski PA, et al. Heat shock protein 90 (HSP90) inhibitors activate the heat shock factor 1 (HSF1) stress response pathway and improve glucose regulation in diabetic mice. Biochem Biophys Res Commun 2013;430:1109–1113.

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