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Antioxidant Effects of Peptides
Published in Mesut Karahan, Synthetic Peptide Vaccine Models, 2021
Rümeysa Rabia Kocatürk, Fatmanur Zehra Zelka, Öznur Özge Özcan, Fadime Canbolat
Catalase (CAT) is an enzyme containing both groups found in many biological systems (Elias, Kellerby, and Decker 2008). CAT is largely found in intracellular organelles such as peroxisomes, and to a lesser extent in the mitochondria and endoplasmic reticulum and enzymatically acts as an antioxidant and molecularly catalyzes the conversion of hydrogen peroxide to water and oxygen, as in the following reaction (Limon-Pacheco and Gonsebatt 2009):
Cross Talk Between Heat Shock and Oxidative Stress Inducible Genes During Myocardial Adaptation to Ischemia
Published in John J. Lemasters, Constance Oliver, Cell Biology of Trauma, 2020
Dipak K. Das, Nilanjana Maulik
Transcription of heat shock and oxidative stress inducible genes has been observed during myocardial adaptation to ischemia. Although there is a general agreement regarding the protective role of some of the stress proteins, it is still speculative, and controversies exist on the precise role of these proteins. Repeated ischemia (5 min ischemia followed by 10 min reperfusion, repeated four times) caused the induction of the expression of mRNAs of two proto-oncogenes, c-fos and c-myc; three different HSPs (HSP 27, HSP 70, and HSP 89); and two antioxidant enzymes, Mn-SOD and catalase; in contrast, after a single episode of ischemia, only HSP 70 and catalase were expressed. Activities of Mn-SOD and catalase were stimulated only after repeated episodes of ischemia. Repeated ischemia, but not a single ischemic episode, was protective against subsequent ischemia reperfusion injury, suggesting that the expression of stress-inducible genes and enzymes could be instrumental for the myocardial protection. To further confirm this, oxidative stress and heat shock were induced by two distinct mechanisms. Animals were pretreated with interleukin-1 (IL-1) for 48 h to induce oxidative stress and with amphetamine to induce heat shock. Catalase was inducible by both oxidative stress and heat shock. Heat shock induced HSP 27, HSP 70, as well as HSP 89 genes, but HSP 27 was induced only by oxidative stress. Both heat shock and oxidative stress were protective against ischemia reperfusion injury.
Clinical Test Paradigms and Problems: Human Otoprotection Studies
Published in Stavros Hatzopoulos, Andrea Ciorba, Mark Krumm, Advances in Audiology and Hearing Science, 2020
Colleen G. Le Prell, Kathleen C. M. Campbell
Catalase speeds decomposition of hydrogen peroxide into water and oxygen (2 H2O2 → 2 H2O + O2). Catalase was first reported in the stria vascularis in guinea pigs (Spector and Carr, 1979), with subsequent corroboration by Pierson and Gray (1982), who reported catalase in both organ of Corti and stria vascularis. Catalase directly attenuated harmful effects of free radicals in the guinea pig inner ear (Clerici and Yang, 1996). Catalase was significantly depleted after the administration of the aminoglycoside antibiotic amikacin in a guinea pig model (Klemens et al., 2003) with similar decreases observed after cisplatin administration in a rat model (Rybak et al., 2000). A potential interaction between catalase and noise has also been suggested, based on decreased catalase levels in chronically noise-exposed textile workers that could reflect consumption of catalase during free radical neutralization (Yildirim et al., 2007). With respect to genes that influence catalase production, covariation in human catalase genetic polymorphisms and vulnerability to NIHL has been reported (Konings et al., 2007; Yang et al., 2015), although co-variation was not observed in another subject sample (Carlsson et al., 2005). A variety of dietary catalase supplements are available as over-the-counter products, and one combination catalase-SOD supplement appears to increase endogenous catalase production (Nelson et al., 2006); however, these supplements have not been evaluated for safety or efficacy in humans and caution is thus warranted.
Justicia carnea extracts ameliorated hepatocellular damage in streptozotocin-induced type 1 diabetic male rats via decrease in oxidative stress, inflammation and increasing other risk markers
Published in Biomarkers, 2023
John Adeolu Falode, Oluwaseun Igbekele Ajayi, Tolulope Victoria Isinkaye, Akinwunmi Oluwaseun Adeoye, Basiru Olaitan Ajiboye, Bartholomew I. C. Brai
A decrease in the defensive systems of enzymatic and non-enzymatic antioxidants is shown by the rise in MDA, which promotes lipid peroxidation (Saddala et al.2013). The antioxidant enzyme known as SOD is responsible for catalysing the conversion of superanion into hydrogen peroxide and molecular oxygen (Wang et al.2012). SOD has vital protective functions against cellular and histological harm caused by ROS. It speeds up the process of converting superoxide radicals into hydrogen peroxide, which can then be transformed into oxygen and water in the presence of other enzymes (Buldak et al.2014). An antioxidant enzyme called catalase (CAT) is almost universally found in all living things. It is crucial in the fight against conditions like diabetes and cardiovascular illnesses that are brought on by oxidative. When compared to the diabetic control (STZ-induced) group, we saw that the administration of J. carnea to diabetic rats significantly (p < 0.05) decreased the MDA, SOD, CAT and GST levels in the liver of the extract-treated groups (JCCD, JBPD and JFPD), while significantly (p < 0.05) increased the GSH levels. These findings are in line with a prior study (Ani et al.2020) that revealed the antioxidant properties of J. carnea. Similarly, metformin’s ability to protect against oxidative stress has been well-established (Nesti and Natali 2017; Loi et al.2019; Abdulkarim et al.2021).
Chronic oral exposure of aluminum chloride in rat modulates molecular and functional neurotoxic markers relevant to Alzheimer’s disease
Published in Toxicology Mechanisms and Methods, 2022
Mangaldeep Dey, Rakesh Kumar Singh
Existing literature indicates that oxidative stress and nitrosative stress is a major causative factors in aluminum-induced neurotoxicity. The two main consequences of oxidative stress are increased pro-oxidant and decreased antioxidants levels. We investigated the levels of three antioxidant markers in the brain including GSH, SOD and catalase (Figure 3(A–C)). There was a significant difference in brain GSH level was observed in this study. Exposures of aluminum, for 24 weeks resulted in a significant depletion in GSH level as compared to the control group. SOD is one of the important enzymes in maintaining the intrinsic antioxidant defense system. Chronic exposure to aluminum chloride marginally decreased the SOD level; however, it was not found to be significant. Catalase is one of the most crucial antioxidant enzymes which mitigates oxidative stress by destroying the cellular hydrogen peroxide to water. Chronic exposure to aluminum significantly decreased the catalase level in the brain compared to control rats.
Evaluation of oxidative stress biomarkers and antioxidant parameters in allergic asthma patients with different level of asthma control
Published in Journal of Asthma, 2022
Behnaz Karadogan, Sengul Beyaz, Asli Gelincik, Suna Buyukozturk, Nazli Arda
Catalase is one of the major first line antioxidants that fights oxidative stress (29). This metalloprotein breaks down hydrogen peroxide into water (50). Conflicting results have been reported about the levels of catalase activity in asthma patients. Some studies have shown lower catalase activity in BAL fluid (51), red blood cells (22,52) and serum (2) of patients with asthma. However, other studies have reported either an increase or lack of change in catalase activity in asthmatic patients (12,53). Here we found lower serum catalase activity in patients with allergic asthma than in healthy control subjects when all patients were regarded as a whole. However, our statistical comparison between the patient subgroups found that catalase activity in the PCG subgroup was, surprisingly, much higher than those of other subgroups (Figure 4). The fact that catalase activity was lower in two groups (TCG and UCG) and higher in one group (PCG) indicates that catalase activity is not a reliable marker of antioxidant response, at least in the case of allergic asthma, probably due to the variable status of oxidative stress in patients.