- Apoptosis: 1 | 2 | 3 | 4 | Related article: How to kill a cancer cell
Research in high gear
Such an encouraging outcome has shifted Walensky and his colleagues into high gear in pursuit of this new drug approach. Many variations of the "death domain" coils exist, and, since some might perform better than others in different cancers, the researchers are hard at work to make and then test large panels of them. "The application of this chemical technology to Bcl-2 domains may lead to an arsenal of new compounds to use against different cancers," he says.
Walensky is gratified that the years spent studying apoptosis and the Bcl-2 family are beginning to bring potential cancer treatments into view. "The beauty of this approach is that you use what nature has already perfected — the pro-apoptotic signals and cell death machinery — to develop new treatments for cancer."
But apoptosis has a flip side. Too much programmed cell death can kill normal cells before their time, resulting in degenerative conditions like Alzheimer's disease and amyotrophic lateral sclerosis (ALS), infertility, and the destruction of pancreatic islet cells in diabetes. Nika Danial, PhD, also in the Korsmeyer lab, has found that the pro-death molecule BAD is involved in apoptosis of insulin-producing islet cells.
In a 2004 publication that gained wide attention, Danial reported that BAD unexpectedly bridges apoptosis and the conversion of glucose (sugar) to energy in the body. She says her work suggests that "controlling cellular metabolism may provide an effective therapeutic tool to manipulate the cell's death machinery to make cancer cells die a good death."
Research on apoptosis has exploded over the last 15 years, with the Korsmeyer lab contributing on many fronts. It's now perfectly reasonable to ask, as he did in the fall of 2004, "Can we exploit the inherent structure of these pro-and anti-death Bcl-2 family members to regulate human diseases?" The answers to that question should begin arriving soon.
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