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Cancer is the second leading cause of death in the United States. Thus, understanding the mechanisms that drive cancer progression is urgent and vital. Two common characteristics of many cancers are the abnormal expression of the BCL-2 pathway (involved in regulating apoptosis) and elevated levels of oxidative stress. Despite new insights into the role of BCL-2 proteins within and beyond the intrinsic apoptosis pathway, much remains to be elucidated about the function of specific BCL-2 proteins, such as Bak and Bax. Bak and Bax are two proteins within the BCL-2 family of proteins that play a role in mitochondrial outer membrane permeabilization (MOMP), leading to the release of cytochrome c from the mitochondria. The cytochrome c then activates a cascade of caspases 3 and 9 that lead to the activation of proteases. These proteases break down cellular structures leading to cell death. One thing that is unknown about Bak and Bax is their contribution to oxidative stress within cancer cells treated with chemotherapy. One such agent is the anti-cancer drug Trichostatin A (TSA). TSA is a histone deacetylase inhibitor (HDACi). TSA arrests cancer cells in the G2/M phase in a mitochondrial derived reactive oxygen species (ROS) dependent matter leading to apoptosis. Testing the effect of Bak and Bax on oxidative stress in the presence of TSA can shed new light on the functions of Bak and Bax. This can lead to a new understanding of how Bak and Bax interact with different parts of the cell and could lead to a new mechanistic model for Bak and Bax, which can be tested in future projects, including therapeutic design.



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Effect of Bak and Bax on Oxidative Stress in A549 Cells