Neglected heat shock protein shown to have anti-tumour properties

Research Lead

Researchers funded by the charity Cancer Research UK, based at the Institute of Cancer Research, London, have found that heat shock protein 70 (HSP70) inhibitors could be used as adjuvant treatments to existing  HSP90 inhibitor therapies, and can also destroy tumour cells when used on their own.

Paul Workman, of the Institute of Cancer Research said, “HSP70 proteins haven’t received as much attention, and were the neglected members of the HSP family of proteins. When we silenced these proteins our results were really surprising.”
 
The team studied the effects of silencing HSP proteins in bowel and ovarian cancer cells and found that knocking out two particular proteins, HSC70 and HSP72 caused apoptosis (cell death) in cancer cells only.

Herbie Newell, Cancer Research UK’s executive director of clinical and translational research, said, “HSP90 inhibitors are currently being tested in clinical trials on patients with breast and other cancers. We hope this new research on HSP70 will be translated into  drug discoveries in the future.”

The heat shock family of proteins are molecular chaperones which play an important role in normal cells, helping other proteins to fold correctly, become activated or degraded. They are also important in helping the cell deal with stresses, including heat. As cancer is in effect a stressed state tumour cells are more dependent on molecular chaperones than are normal cells.