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Free Radicals and Antioxidants
Published in Chuong Pham-Huy, Bruno Pham Huy, Food and Lifestyle in Health and Disease, 2022
Chuong Pham-Huy, Bruno Pham Huy
In human tissues, there are three forms of superoxide dismutase, each with a specific subcellular location and different tissue distribution and also depending on the presence of metal cofactor: SOD1 is located in the cytoplasm, SOD2 in the mitochondria, and SOD3 is extracellular (12, 22, 82). They are proteins containing copper and zinc, or manganese, iron, or nickel. SOD1 and SOD3 contain copper and zinc, while SOD2 has manganese in its reactive center (82).
Oxidative Stress, Inflammation, Immune System and Hypertension
Published in Giuseppe Mancia, Guido Grassi, Konstantinos P. Tsioufis, Anna F. Dominiczak, Enrico Agabiti Rosei, Manual of Hypertension of the European Society of Hypertension, 2019
Damiano Rizzoni, Livia L. Camargo, Francisco J. Rios, Augusto C. Montezano, Rhian M. Touyz
To maintain cellular redox status, a number of antioxidant systems have evolved to prevent excessive ROS accumulation and to protect against oxidative damage (36). In particular, vascular cells possess functionally active superoxide dismutase (SOD), catalase, peroxidases, glutathione and thioredoxin. SOD, of which there are three isoforms, are especially important because they catalyze dismutation of O2− to H2O2 and localize in specific cellular compartments: cytosol for SOD1, mitochondria for SOD2 and extracellular matrix for SOD3. As such, SOD influences vascular redox signalling in a controlled and compartmentalized function.
A Potential Natural Product Combination Targeting Memory Disorders
Published in Vikas Kumar, Addepalli Veeranjaneyulu, Herbs for Diabetes and Neurological Disease Management, 2018
Manju Bhaskar, Meena Chintamaneni, Addepalli Veeranjaneyulu
SODs are the main antioxidant enzymes that convert superoxide anions to H2O2, protecting cells and tissues from ROS generated from endogenous and exogenous sources. SODs consist of three types of isoforms expressed in mammalian cells: copper/zinc SOD (CuZn-SOD, SOD1), which is located in the cytoplasm, manganese SOD (Mn-SOD, SOD2), which exists in the mitochondrial matrix, and extracellular SOD (EC-SOD, SOD3).68 SOD is considered to be one of the most vulnerable indicators as an antioxidant enzyme in AD and cognitive dementia. Several studies have shown decreased SOD in the frontal cortex of AD patients. The SOD2 activity has been reported to be reduced in AD brains. The activity of SOD in serum was reduced in both MCI and AD patients compared to controls. The reduction in SOD activity was also reported in hippocampus from MCI patients; however, total levels of SOD were reduced as well.69
Exercise training decreases oxidative stress in skeletal muscle of rats with pulmonary arterial hypertension
Published in Archives of Physiology and Biochemistry, 2022
C. U. Becker, C. L. Sartório, C. Campos-Carraro, R. Siqueira, R. Colombo, A. Zimmer, A. Belló-Klein
In a previous study of Kamezaki et al. (2008), a SOD over expression in lungs of rats with PAH induced by MCT was able to mitigate the progression of this disease, suggesting that superoxide anion may play a key role in its pathogenesis. More recently, rats with heart failure with an increased expression of SOD3 were able to improve the oxidative stress profile, exercise tolerance, in addition to reducing mitochondrial loss, and vascular rarefaction in skeletal muscle (Okutsu et al. 2014). In addition, another study, that used genetically modified SOD3 overexpression skeletal muscle of mice with multiple organ dysfunction syndrome, found high levels of this enzyme in blood and in other organs such as liver, heart, lung, and adipose tissue, reducing the overall mortality (Call et al. 2017). These studies recently emerged SOD3 as a promising protective source of several vital organs and tissues under pathological conditions because it can act on distant tissues (Yan and Spaulding 2020). In our study, although we didn’t evaluate the subunits of SOD separately, the increase in SOD activity and expression in the MCT group could bring important benefits, not only to reduce superoxide anion in the skeletal muscle, but also in organs in which it is known that oxidative stress plays a major role in the pathology of PAH, such as in heart and in lungs. Further studies should be carried out to confirm this theory.
SOD3 boosts T cell infiltration by normalizing the tumor endothelium and inducing laminin-α4
Published in OncoImmunology, 2020
Lorena Carmona-Rodríguez, Diego Martínez-Rey, Emilia Mira, Santos Mañes
The anti-oxidant enzyme SOD3 is usually downregulated in tumors, which suggests that its loss is advantageous for cancer progression.7 SOD3 catalyzes the dismutation of the superoxide radical (·O2−) in the extracellular space; this activity not only prevents oxidative damage of lipids or proteins but also preserves the bioavailability of nitric oxide (NO). NO is essential for SOD3-induced vascular normalization due to its inhibitory activity on the prolyl hydroxylase domain protein (PHD)-2. The PHD are central regulators of the hypoxia-inducible transcription factor (HIF)-α subunits, which they degrade in normoxia. High SOD3 levels, but not those of a catalytically inactive mutant, stabilize HIF-2α (but not HIF-1α) in EC in a NO-dependent manner.5 This enhances HIF-2α-induced transcription of vascular-endothelial cadherin (VEC; cadherin 5, CD144), responsible for assembly of endothelial adherens junctions (AJ) and barrier architecture. SOD3 thus reduces EC monolayer permeability, prevents VEGF-induced destabilization of AJ, improves tumor perfusion, and increases delivery of chemotherapeutic drugs, all hallmarks of vessel normalization.5 Specific HIF-2α ablation in EC prevents SOD3-induced vascular normalization in implanted tumors, which suggests that HIF-2α is a pivotal SOD3 mediator in vivo.5
First line defence antioxidants-superoxide dismutase (SOD), catalase (CAT) and glutathione peroxidase (GPX): Their fundamental role in the entire antioxidant defence grid
Published in Alexandria Journal of Medicine, 2018
The various ‘isozymes’ of SOD are encoded by different genes. According to Rosen et al., Cu/Zn-SOD is encoded by the SOD1 gene mapping to chromosome 21. MnSOD is encoded by the SOD2 gene mapping to chromosome 6. The eukaryotic extracellular SOD Cu-Zn SOD is encoded by the SOD3 gene mapping to chromosome 4.27 Substantial amount of SOD3 is found virtually in all human tissues. A number of tissues including the heart have been observed to possess the cellular resources to transcribe SOD3 mRNA from SOD DNA. This is of great importance since SOD3 is the major enzymatic antioxidant defense against vascular and cardiovascular diseases (neurological diseases, lung disease, atherosclerosis, diabetes, hypertension, inflammatory conditions and ischemia-reperfusion injury. Association between SOD deficiency and a number of pathologies has been observed in both animals and humans (Fig. 4). Lebovitz et al.28 noted neurodegeneration, myocardial injury, and perinatal death in mitochondrial superoxide dismutase-deficient mice. Zn-deficient wild-type and mutant human SOD1 have been implicated in the disease familial amyotrophic lateral sclerosis (FALS), also known as Lou Gehrig’s disease which affects the nerve cells in the spinal cord and the brain.29,30 Recently, Dayal and colleagues informed that deficiency of superoxide dismutase promoted cerebral vascular hypertrophy and vascular dysfunction in hyperhomocysteinemia.31