Researchers link protein to prostate cancer cell death

August 3, 2006

If a protein known as BAD is inhibited, then prostate cancer cells survive, a finding that may lead to more effective drug treatments for the disease. Researchers from Wake Forest University Baptist Medical Center, Winston-Salem, NC, recently reported their findings about the BAD protein in the Journal of Biological Chemistry (2006; 281:20891-901).

If a protein known as BAD is inhibited, then prostate cancer cells survive, a finding that may lead to more effective drug treatments for the disease. Researchers from Wake Forest University Baptist Medical Center, Winston-Salem, NC, recently reported their findings about the BAD protein in the Journal of Biological Chemistry (2006; 281:20891-901).

The researchers sought to uncover how prostate cancer cells become resistant to androgen ablation therapy. They evaluated three different pathways (activation by vasoactive intestinal peptide, epidermal growth factor, or phosphoinositide 3-kinase) involved in cell signaling in order to find out how these pathways are involved in cancer cells resisting death. Researchers found that all three pathways work by inactivating the BAD protein, which causes cell death.

Senior researcher George Kulik, PhD, DVM said it appears that each of the three molecules is separately capable of inactivating BAD, which means that prostate cancer cells have three redundant survival mechanisms.

“Our findings suggest that BAD is an important switch in the development and growth of prostate cancer,” Dr. Kulik said.

He and colleagues hope to conduct animal studies to test their findings. Dr. Kulik said confirmed findings in animal and human tumors could lead to future therapy. For example, a drug could be developed to prevent inhibition of BAD, or findings could be used to test current drugs designed to block the effects of PI3K, one of the molecules.