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Novel therapeutic strategies in multiple myeloma: role of the heat shock protein inhibitors Allegra A; Sant'antonio E; Penna G; Alonci A; D'Angelo A; Russo S; Cannavo A; Gerace D; Musolino CEur J Haematol 2011[Feb]; 86 (2): 93-110Despite advances in understanding the molecular pathogenesis of multiple myeloma and promising new therapies, almost all patients eventually relapse with resistant disease. There is therefore a strong rationale for combining novel therapies that target intrinsic molecular pathways mediating multiple myeloma cell resistance. One such protein family is the heat shock proteins (HSP), especially the HSP90 family. Heat shock protein inhibitors have been identified as promising cancer treatments as, while they only inhibit a single biologic function, the chaperone-protein association, their effect is widespread as it results in the destruction of numerous client proteins. This article reviews the preclinical and clinical data, which support the testing of HSP90 inhibitors as cancer drugs and update the reader on the current status of the ongoing clinical trials of HSP90 inhibitors in multiple myeloma.|Animals[MESH]|Antineoplastic Agents/therapeutic use[MESH]|Autophagy[MESH]|Clinical Trials as Topic[MESH]|Epigenesis, Genetic[MESH]|HSP90 Heat-Shock Proteins/metabolism[MESH]|Heat-Shock Proteins/*antagonists & inhibitors[MESH]|Humans[MESH]|Medical Oncology/methods[MESH]|Mice[MESH]|Multiple Myeloma/*drug therapy[MESH]|Neovascularization, Pathologic[MESH] |
