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Last Reviewed May 27, 2008
Chemistry Web Manager

Apoptosis is programmed cell death, a process that allows animals to eliminate unneeded or unhealthy cells. At a biochemical level, apoptosis requires protein enzymes called caspases. Caspases are present in most animal cells but are kept inhibited by IAP (inhibitor of apoptosis) proteins. This inhibition is relieved by apoptosis-stimulating proteins when apoptosis is needed.

KU Chemistry Undergraduate Research
Investigating Apoptosis -
Programmed Cell Death
Dr. Matt Junker

Caspase activity
Many of the research projects in this laboratory investigate how caspases, IAP's, and apoptosis stimulators work at a biochemical level. The goal is to relate protein structure to function. Recombinant DNA methods are used to generate genes for apoptosis proteins that can be expressed in bacteria. The apoptosis proteins are then expressed in and purified from bacteria, and assayed in biochemical assays.
IAP gel

The research projects in this laboratory address such questions as: How does the IAP inhibit the caspase? Does the IAP block the caspase catalytic site, or does it change the caspase's conformation ("shape")? And how does stimulator binding do to the IAP to alter its ability to inhibit the caspase?

Answers to such questions provide insight into how proteins work in living cells. They can also provide clues for developing new therapies to treat diseases where apoptosis dysfunction occurs, such as cancer and neurodegeneration.