Effects of Protein Inhibitors on Melanoma Cancer Cells

Trevar Lytle


Melanoma, a popular cancer found in humans is a base for modern research. Strands of this cancer can be isolated and cultured for study using different inhibitors of proteins related to the production of proteins and cell defense systems. Targeted gene expression could be regulated from an external source by treatment of inhibitors on proteins associated with these functions. Cultures treaded with various combinations of Suicide inhibitors were examined to better understand the role that these proteins have in melanoma tumor growth and development.  Targeted proteins were: Heat Shock Protein (Hsp90) and it’s relationship with protein folding and function within the signal cascade of many cells. This relationship allows for the regulation of specific proteins that are weakened or over taken by cancer cells. Heme-Oxygenase (Hsp32) is an enzyme that in recent years has been found in abnormal concentrations in active tumor cells. It plays a vital role in Oxidative stress and Heme degradation in functioning cells, but it seems to be upregulated in cancer cells. This experiment coupled Hsp90 inhibitors and Hsp32 inhibitors on A375 melanoma cells. Hsp90 inhibitor used was NMS E973 and Hsp32 inhibitor used was SnMP. 

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