Although disease is often thought of as damage to healthy cells, the lack of death in unhealthy cells presents a host of complications of its own. The body relies on certain self-destructive processes to ensure that defective cells die off in a timely manner. These processes are kept in check under normal conditions, but cues from within or from outside a cell can trigger a sequence of signals and processes that carry out apoptosis, or programmed cell death, collectively known as the apoptotic cascade. A group of enzymes known as caspases play a vital role in this cascade with some participating as initiators and others acting as effectors of protein cleavage and intracellular breakdown. Very little information exists in the current primary literature in regards to protein structure changes of the executioner caspases (3 and 7) or the initiator caspases (8 and 12) in the presence and absence of calcium ions. This study will first amplify and isolate large amounts of the caspases of interest via molecular biology techniques and then investigate the effects of calcium ions on the protein folding of caspase-8, caspase-12, and caspase-7 in the presence and absence of associated apoptotic proteins such as Bax, Bcl-2, and cytochrome c. Structural changes and binding interactions will be monitored using circular dichroism spectroscopy. Data from this project will lead to a better understanding of apoptosis and could provide more targets for treatment of cancers and neurodegenerative diseases.

Investigations of protein conformational changes of caspases as a signal for apoptosis

2019 Spring National Meeting

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