Superoxide dismutase (SOD) is an enzyme found in all living cells that helps protect the body against potentially harmful oxygen molecules, making it an important antioxidant. Thus, it helps prevent an individual’s cells from being damaged by highly unstable atoms with unpaired electrons, protecting against tissue damage, oxidative stress, and diseases are associated with oxidative stress.
There are three forms of superoxide dismutase in humans that are located in the cytoplasm of the cell (SOD1), the mitochondria (SOD2), and in the extracellular region (SOD3). Studies have found that mice lacking SOD1 developed various diseases that included hepatocellular carcinoma, a cancer of the liver. These mice experienced accelerated age-related muscle mass loss, cataract, and a shorter lifespan.
Other studies have found that mutations in SOD1 are responsible for various pathologies. A case in point would be the disease amyotrophic lateral sclerosis (ALS), a fatal motor neuron disease that causes an individual to experience weakness, muscle atrophy, muscle twitching, and other complication. Simultaneously, elevated level of CuZn-superoxide dismutase has also been found to be dangerous. Overexpression has been found to be associated with patients who have Down’s syndrome.
As for SOD2, studies have found that mice lacking SOD2 experienced high oxidative stress and died soon after birth. SOD2 is also important because it is the first enzyme to scavenge free radicals produced by oxidative phosphorylation, a natural metabolic pathway that generates cellular energy. Thus, this enzyme is vital for preventing mitochondrial enzymes from being inactivated by superoxides. By contrast, mice that did not have SOD3 were found to be more sensitive to hyperoxic injury where there was an excess of oxygen present.
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