Superoxide dismutase (SOD) proteins are a class of metalloenzymes that play a crucial role in the antioxidant defense system of the body. They catalyze the conversion of superoxide radicals into oxygen and hydrogen peroxide, thereby neutralizing one of the most common reactive oxygen species (ROS) and protecting cells from oxidative damage. SODs are essential for maintaining the balance of ROS in the body and are involved in various cellular processes, including lipid metabolism, inflammation, and redox signaling. There are three main isoforms of SOD in mammals: cytoplasmic Cu/ZnSOD (SOD1), mitochondrial MnSOD (SOD2), and extracellular Cu/ZnSOD (SOD3). Each isoform has a unique cellular location and function, and they collectively contribute to the overall antioxidant capacity of the body. SODs are also implicated in various diseases, including neurodegenerative disorders like amyotrophic lateral sclerosis (ALS), where mutations in the SOD1 gene can lead to protein misfolding and aggregation. Additionally, SODs have potential therapeutic applications in conditions characterized by oxidative stress, such as ischemia-reperfusion injury and inflammatory diseases.
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