Expression of heat shock protein 70 and NKG2D ligands in acute myeloid leukemia cell lines

References

• Calderwood SK, Theriault JR, Gong J. Message in a bottle: role of the 70-kDa heat shock protein family in anti-tumor immunity. Eur J Immunol 2005, 35, 2518–2527.
   PubMed Web of Science ®Google Scholar
• Aghdassi A, Phillips P, Dudeja V, Dhaulakhandi D, Sharif R, Dawra R, Lerch MM, Saluja A. Heat shock protein 70 increases tumorigenicity and inhibits apoptosis in pancreatic adenocarcinoma. Cancer Res 2007, 67, 616–625.
   PubMed Web of Science ®Google Scholar
• Duval A, Olaru D, Campos L, Flandrin P, Nadal N, Guyotat D. Expression and prognostic significance of heat-shock proteins in myelodysplastic syndromes. Haematologica 2006, 91, 713–714.
   PubMed Web of Science ®Google Scholar
• Rohde M, Daugaard M, Jensen MH, Helin K, Nylandsted J, Jäättelä M. Members of the heat-shock protein 70 family promote cancer cell growth by distinct mechanisms. Genes Dev 2005, 19, 570–582.
   PubMed Web of Science ®Google Scholar
• Ciocca DR, Vargas-Roig LM. Heat shock proteins and drug resistance in breast cancer. In: Bernal SD ed. Drug Resistance in Oncology (pp 167–190 ). New York: Marcel Dekker Inc., 1997.
   Google Scholar
• Nanbu K, Konishi I, Mandai M, Kuroda H, Hamid AA, Komatsu T, Mori T. Prognostic significance of heat shock proteins HSP70 and HSP90 in endometrial carcinomas. Cancer Detect Prev 1998, 22, 549–555.
   PubMedGoogle Scholar
• Thomas X, Campos L, Mounier C, Cornillon J, Flandrin P, Le QH, Piselli S, Guyotat D. Expression of heat-shock proteins is associated with major adverse prognostic factors in acute myeloid leukemia. Leuk Res 2005, 29, 1049–1058.
   PubMed Web of Science ®Google Scholar
• Yeh CH, Tseng R, Zhang Z, Cortes J, O′Brien S, Giles F, Hannah A, Estrov Z, Keating M, Kantarjian H, Albitar M. Circulating heat shock protein 70 and progression in patients with chronic myeloid leukemia. Leuk Res 2009, 33, 212–217.
   PubMed Web of Science ®Google Scholar
• Nimmanapalli R, O′Bryan E, Bhalla K. Geldanamycin and its analogue 17-allylamino-17-demethoxygeldanamycin lowers Bcr–Abl levels and induces apoptosis and differentiation of Bcr–Abl-positive human leukemic blasts. Cancer Res 2001, 61, 1799–1804.
   PubMed Web of Science ®Google Scholar
• Guo F, Sigua C, Bali P, George P, Fiskus W, Scuto A, Annavarapu S, Mouttaki A, Sondarva G, Wei S, Wu J, Djeu J, Bhalla K. Mechanistic role of heat shock protein 70 in Bcr-Abl-mediated resistance to apoptosis in human acute leukemia cells. Blood 2005, 105, 1246–1255.
   PubMed Web of Science ®Google Scholar
• Ciocca DR, Calderwood SK. Heat shock proteins in cancer: diagnostic, prognostic, predictive, and treatment implications. Cell Stress Chaperones 2005, 10, 86–103.
   PubMed Web of Science ®Google Scholar
• Gurbuxani S, Bruey JM, Fromentin A, Larmonier N, Parcellier A, Jäättelä M, Martin F, Solary E, Garrido C. Selective depletion of inducible HSP70 enhances immunogenicity of rat colon cancer cells. Oncogene 2001, 20, 7478–7485.
   PubMed Web of Science ®Google Scholar
• Vega VL, Rodríguez-Silva M, Frey T, Gehrmann M, Diaz JC, Steinem C, Multhoff G, Arispe N, De Maio A. Hsp70 translocates into the plasma membrane after stress and is released into the extracellular environment in a membrane-associated form that activates macrophages. J Immunol 2008, 180, 4299–4307.
   PubMed Web of Science ®Google Scholar
• Multhoff G, Botzler C, Wiesnet M, Müller E, Meier T, Wilmanns W, Issels RD. A stress-inducible 72-kDa heat-shock protein (HSP72) is expressed on the surface of human tumor cells, but not on normal cells. Int J Cancer 1995, 61, 272–279.
   PubMed Web of Science ®Google Scholar
• Multhoff G. Heat shock protein 70 (Hsp70): membrane location, export and immunological relevance. Methods 2007, 43, 229–237.
   PubMed Web of Science ®Google Scholar
• Srivastava P. Roles of heat-shock proteins in innate and adaptive immunity. Nat Rev Immunol 2002, 2, 185–194.
   PubMed Web of Science ®Google Scholar
• Delneste Y, Magistrelli G, Gauchat J, Haeuw J, Aubry J, Nakamura K, Kawakami-Honda N, Goetsch L, Sawamura T, Bonnefoy J, Jeannin P. Involvement of LOX-1 in dendritic cell-mediated antigen cross-presentation. Immunity 2002, 17, 353–362.
   PubMed Web of Science ®Google Scholar
• Figueiredo C, Wittmann M, Wang D, Dressel R, Seltsam A, Blasczyk R, Eiz-Vesper B. Heat shock protein 70 (HSP70) induces cytotoxicity of T-helper cells. Blood 2009, 113, 3008–3016.
   PubMedGoogle Scholar
• Gastpar R, Gross C, Rossbacher L, Ellwart J, Riegger J, Multhoff G. The cell surface-localized heat shock protein 70 epitope TKD induces migration and cytolytic activity selectively in human NK cells. J Immunol 2004, 172, 972–980.
   PubMed Web of Science ®Google Scholar
• Asea A, Rehli M, Kabingu E, Boch JA, Bare O, Auron PE, Stevenson MA, Calderwood SK. Novel signal transduction pathway utilized by extracellular HSP70: role of toll-like receptor (TLR) 2 and TLR4. J Biol Chem 2002, 277, 15028–15034.
   PubMed Web of Science ®Google Scholar
• Becker T, Hartl FU, Wieland F. CD40, an extracellular receptor for binding and uptake of Hsp70-peptide complexes. J Cell Biol 2002, 158, 1277–1285.
   PubMed Web of Science ®Google Scholar
• Multhoff G, Mizzen L, Winchester CC, Milner CM, Wenk S, Eissner G, Kampinga HH, Laumbacher B, Johnson J. Heat shock protein 70 (Hsp70) stimulates proliferation and cytolytic activity of natural killer cells. Exp Hematol 1999, 27, 1627–1636.
   PubMed Web of Science ®Google Scholar
• Stangl S, Gross C, Pockley AG, Asea AA, Multhoff G. Influence of Hsp70 and HLA-E on the killing of leukemic blasts by cytokine/Hsp70 peptide-activated human natural killer (NK) cells. Cell Stress Chaperones 2008, 13, 221–230.
   PubMed Web of Science ®Google Scholar
• Elsner L, Flügge PF, Lozano J, Muppala V, Eiz-Vesper B, Demiroglu SY, Malzahn D, Herrmann T, Brunner E, Bickeböller H, Multhoff G, Walter L, Dressel R. The endogenous danger signals HSP70 and MICA cooperate in the activation of cytotoxic effector functions of NK cells. J Cell Mol Med 2009.
   Web of Science ®Google Scholar
• Drexler HG, Dirks W, MacLeod RAF, Quentimeier H, Steube KG, Uphoff CC. DSMZ catalogue of cell lines 2009: www.cell-lines.de.
   Google Scholar
• Farkas B, Hantschel M, Magyarlaki M, Becker B, Scherer K, Landthaler M, Pfister K, Gehrmann M, Gross C, Mackensen A, Multhoff G. Heat shock protein 70 membrane expression and melanoma-associated marker phenotype in primary and metastatic melanoma. Melanoma Res 2003, 13, 147–152.
   PubMed Web of Science ®Google Scholar
• Casasnovas RO, Slimane FK, Garand R, Faure GC, Campos L, Deneys V, Bernier M, Falkenrodt A, Lecalvez G, Maynadié M, Béné MC. Immunological classification of acute myeloblastic leukemias: relevance to patient outcome. Leukemia 2003, 17, 515–527.
   PubMed Web of Science ®Google Scholar
• Hromadnikova I, Sedlackova L. Analysis of cell surface and relative gene expression of heat shock protein 70 in human leukemia cell lines. Leuk Lymphoma 2008, 49, 570–576.
   PubMed Web of Science ®Google Scholar
• Nowbakht P, Ionescu MC, Rohner A, Kalberer CP, Rossy E, Mori L, Cosman D, De Libero G, Wodnar-Filipowicz A. Ligands for natural killer cell-activating receptors are expressed upon the maturation of normal myelomonocytic cells but at low levels in acute myeloid leukemias. Blood 2005, 105, 3615–3622.
   PubMed Web of Science ®Google Scholar
• Pende D, Rivera P, Marcenaro S, Chang CC, Biassoni R, Conte R, Kubin M, Cosman D, Ferrone S, Moretta L, Moretta A. Major histocompatibility complex class I-related chain A and UL16-binding protein expression on tumor cell lines of different histotypes: analysis of tumor susceptibility to NKG2D-dependent natural killer cell cytotoxicity. Cancer Res 2002, 62, 6178–6186.
   PubMed Web of Science ®Google Scholar
• Rohner A, Langenkamp U, Siegler U, Kalberer CP, Wodnar-Filipowicz A. Differentiation-promoting drugs up-regulate NKG2D ligand expression and enhance the susceptibility of acute myeloid leukemia cells to natural killer cell-mediated lysis. Leuk Res 2007, 31, 1393–1402.
   PubMed Web of Science ®Google Scholar
• Salih HR, Antropius H, Gieseke F, Lutz SZ, Kanz L, Rammensee HG, Steinle A. Functional expression and release of ligands for the activating immunoreceptor NKG2D in leukemia. Blood 2003, 102, 1389–1396.
   PubMed Web of Science ®Google Scholar
• Feder JH, Rossi JM, Solomon J, Solomon N, Lindquist S. The consequences of expressing hsp70 in Drosophila cells at normal temperatures. Genes Dev 1992, 6, 1402–1413.
   PubMed Web of Science ®Google Scholar
• Abravaya K, Myers MP, Murphy SP, Morimoto RI. The human heat shock protein hsp70 interacts with HSF, the transcription factor that regulates heat shock gene expression. Genes Dev 1992, 6, 1153–1164.
   PubMed Web of Science ®Google Scholar
• Ding XZ, Tsokos GC, Kiang JG. Overexpression of HSP-70 inhibits the phosphorylation of HSF1 by activating protein phosphatase and inhibiting protein kinase C activity. FASEB J 1998, 12, 451–459.
   PubMed Web of Science ®Google Scholar
• Mosser DD, Duchaine J, Massie B. The DNA-binding activity of the human heat shock transcription factor is regulated in vivo by hsp70. Mol Cell Biol 1993, 13, 5427–5438.
   PubMed Web of Science ®Google Scholar
• Kim D, Ouyang H, Li GC. Heat shock protein hsp70 accelerates the recovery of heat-shocked mammalian cells through its modulation of heat shock transcription factor HSF1. Proc Natl Acad Sci USA 1995, 92, 2126–2130.
   PubMed Web of Science ®Google Scholar
• Balakrishnan K, De Maio A. Heat shock protein 70 binds its own messenger ribonucleic acid as part of a gene expression self-limiting mechanism. Cell Stress Chaperones 2006, 11, 44–50.
   PubMed Web of Science ®Google Scholar
• Theodorakis NG, Drujan D, De Maio A. Thermotolerant cells show an attenuated expression of Hsp70 after heat shock. J Biol Chem 1999, 274, 12081–12086.
   PubMedGoogle Scholar
• Zimmer J, Michel T, Andrès E, Hentges F. Up-regulation of NKG2D ligands by AML cells to increase sensitivity to NK cells: the tumour might strike back. Comment on “differentiation-promoting drugs up-regulate NKG2D ligand expression and enhance the susceptibility of acute myeloid leukemia cells to natural killer cell-mediated lysis” by Rohner et al. [Leuk Res 2007;31:1393-402]. Leuk Res 2008, 32, 676–677.
   PubMedGoogle Scholar
• McCann FE, Eissmann P, Onfelt B, Leung R, Davis DM. The activating NKG2D ligand class I-related chain A transfers from target cells to NK cells in a manner that allows functional consequences. J Immunol 2007, 178, 3418–3426.
   PubMed Web of Science ®Google Scholar