all Stanley Korsmeyer stories

Enzyme responsible for protein's 'Jekyll-and-Hyde' personality

70652986 — Mon, 26 Mar 2007 05:32:52 -0400

Normally, a protein regulates when and how body parts develop, but when mutated, it triggers a rare, often-lethal infant leukemia called mixed lineage leukemia. The newly identified protease enzyme, Taspase1, plays a key role in the MLL protein's dual-personality. (A protease enzyme cuts protein molecules into smaller pieces). Blocking Taspase1, Dana-Farber Cancer Institute researchers say, might provide a novel way to shut down runaway production of cancer cells. The findings were reported in the Oct. 31, 2003 issue of Cell. "These findings demonstrate that a simple protease enzyme is required for the effects of this gene (MLL) and suggests that protease inhibitors, which have been effective with relatively few side effects in other diseases, could be a reasonable way to treat cancer," says Stanley Korsmeyer, senior author of the paper. Korsmeyer is the Sidney Farber Professor of Pathology at Harvard Medical School and a Howard Hughes Medical Institute investigator. Mixed lineage leukemia strikes fewer than 100 babies every year in the United States, but it is typically fatal in 60 percent. The research was supported in part by grants from the National Institutes of Health.

Death and survival proteins work together

70652986 — Mon, 26 Mar 2007 05:31:48 -0400

At a cellular level, life-sustaining activities such as glucose metabolism were thought to be carried out by entirely different proteins from those involved in apoptosis, or cell death. "People in the field always thought glucose metabolism and apoptosis were two independent pathways for the cell," said Nika Danial, Harvard Medical School research fellow in pathology at the Dana-Farber Cancer Institute. But the line between survival and extinction may be growing more tenuous. Danial, Emily Cheng, Stanley Korsmeyer, and colleagues have discovered that two of the cell's most notorious death proteins, BAK and BAD, have intimate partnerships with life-sustaining molecules and may help them carry out their survival activities. The findings, reported in two separate papers, could hold clues to new approaches for treating diseases as disparate as hepatitis, diabetes, and certain cancers. In some cases, the goal would be to prolong the lives of cells; in another -- that of cancer -- to get them to die more quickly.

Researchers isolate key part of cells' 'death' signals

70652986 — Mon, 26 Mar 2007 05:24:58 -0400

In the cover article of the September 2002 issue of the journal Cancer Cell, researchers from Dana-Farber Cancer Institute reported that peptide subunits of cell-signaling "BH3" proteins could out-maneuver opposing "anti-death" proteins and trigger the suicide process. Cell suicide or "apoptosis" prevents wayward cells from growing out of control and becoming cancerous. "Many cancer cells may stay alive due to the overexpression of anti-death proteins," said Dana-Farber's Anthony Letai, lead author of the paper and an instructor in medicine at Harvard Medical School.

Scientists using gene chips identify unique form of leukemia

70652986 — Mon, 26 Mar 2007 05:18:24 -0400

Currently, physicians diagnose and treat a rare form of cancer that strikes infants as a particularly aggressive form of the more common acute lymphoblastic leukemia. The cancer may respond to chemotherapy at first, but it tends to recur fatally. That's why the prognosis is so much worse than for most types of childhood leukemia, which today can usually be treated effectively. Using the relatively new technology of gene chips, scientists working at Dana-Farber Cancer Institute have discovered that this rare leukemia is genetically distinct from other types of leukemia.