Anti-myeloma activity of the novel 2-aminothienopyrimidine Hsp90 inhibitor NVP-BEP800

Br J Haematol. 2009 Nov;147(3):319-27. doi: 10.1111/j.1365-2141.2009.07852.x. Epub 2009 Aug 13.

Abstract

The 90 kD heat shock protein (Hsp90) molecular chaperone sustains multiple components of oncogenic pathways and has recently emerged as a therapeutic target that is now being clinically tested in a number of malignancies. In order to address formulation issues and to deal with possible resistance mechanisms against small molecule Hsp90 inhibitors, a range of compounds based on different molecular scaffolds are now being developed. The present study preclinically tested the effects of the novel 2-aminothienopyrimidine class Hsp90 inhibitor NVP-BEP800, which is suitable for oral formulations, on multiple myeloma cells from established cell lines and on a larger cohort (n = 40) of primary myeloma samples. The drug effectively and specifically killed the majority of primary myeloma cells in coculture with bone marrow stromal cells and reliably entailed molecular consequences of Hsp90 blockade - such as survival pathway breakdown and client protein depletion - in multiple myeloma cells from cell lines as well as from patients. Collectively, the properties of this novel drug support clinical testing in multiple myeloma.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antineoplastic Combined Chemotherapy Protocols / pharmacology
  • Bone Marrow Cells / pathology
  • Cell Death / drug effects
  • Coculture Techniques
  • Dose-Response Relationship, Drug
  • Drug Evaluation, Preclinical / methods
  • HSP90 Heat-Shock Proteins / antagonists & inhibitors*
  • HSP90 Heat-Shock Proteins / metabolism
  • Humans
  • Multiple Myeloma / metabolism
  • Multiple Myeloma / pathology*
  • Neoplasm Proteins / antagonists & inhibitors
  • Neoplasm Proteins / metabolism
  • Pyrimidines / pharmacology*
  • Stromal Cells / pathology
  • Tumor Cells, Cultured

Substances

  • HSP90 Heat-Shock Proteins
  • NVP-BEP800
  • Neoplasm Proteins
  • Pyrimidines