Hsp90 Inhibitors

Dear Colleagues,

Cancer is a disease that has been demonstrated to involve the dysregulation of a minority of different key proteins or signaling pathways within cells which manifests itself in the aberrant expression and/or function of these proteins/pathways. Heat shock protein 90 (Hsp90) has been shown to play an integral role in regulating the stability of a number of these key cancer-causing proteins through its role as a protein chaperone. Proteins chaperoned by Hsp90, known as client proteins, include cancer-causing forms of ALK, BCR-ABL, EGFR, FLT3, and HER2. This role in controlling the activity of multiple client proteins makes Hsp90 an attractive target for therapeutic intervention. Indeed, Infinity Pharmaceuticals, as well as others, have shown the potential clinical utility of inhibiting Hsp90 function in the management of different malignancies including non-small cell lung cancer, gastro-intestinal stromal tumors and breast cancer. The purpose of this special issue is to evaluate the current status of Hsp90 inhibitors in preclinical and clinical development, review historical findings and examine where this exciting area of research and therapeutic development will lead in the future.

Dr. Kip A. West
Guest Editor