Redox signaling is how molecules, such as superoxide, communicate within cells to negatively impact normal cell function. Understanding redox signaling is important because of the role of redox signaling in the aging of a cell as a result of superoxide radicals. Superoxide Dismutase (SOD) is an antioxidant enzyme that functions to eliminate superoxide radicals and is likely to contribute to cell maintenance distribution. Uncoupling Protein 2 (UCP2) has been shown to have an antioxidant role and is known to be present in neuronal cells. Here, we investigated the presence of SOD2 in SH-SY5Y cells, a neuroblastoma cell line with the intent to conduct further experiments that analyze a relationship between SOD2 and UCP2. SOD2 activity experiments were conducted by obtaining cell lysates from the SH-SY5Y cells, followed by using a riboflavin SOD activity stain after gel electrophoresis. The studies revealed that SOD2 activity is present in SH-SY5Y cells. The determination of SOD2 activity in SH-SY5Y cells combined with previous studies that revealed that UCP2 is present in SH-SY5Y cells suggests that both proteins may communicate with each other to effectively function as antioxidant proteins.
