Advances in redox research : an official journal of the Society for Redox Biology and Medicine and the Society for Free Radical Research-Europe最新文献

{"title":"Betaine Intervention as a Novel Approach to Preventing Doxorubicin-Induced Cardiotoxicity","authors":"Aiswarya Jaiswal ,&nbsp;Pushkar Singh Rawat ,&nbsp;Sumeet Kumar Singh ,&nbsp;Jasvinder Singh Bhatti ,&nbsp;Amit Khurana ,&nbsp;Umashanker Navik","doi":"10.1016/j.arres.2023.100084","DOIUrl":"https://doi.org/10.1016/j.arres.2023.100084","url":null,"abstract":"<div><p>The anthracycline anticancer drug doxorubicin (Dox) is widely prescribed for treating lung, ovary, breast, lymphoma, sarcoma, and pediatric cancer. Mechanistically, Dox intercalates the DNA and inhibits the topoisomerase II enzyme in fast-proliferating cancer. The clinical application of Dox is limited due to its cardiotoxicity, including congestive heart failure, alterations in myocardial structure, arrhythmia, and left ventricular dysfunction. Dox causes cardiotoxicity via various mechanisms, including oxidative stress, mitochondrial dysfunctioning, deranged Ca²⁺ homeostasis, inflammation, fibrosis, downregulating AMPK, etc. Betaine is a zwitterion-based drug known as N, N, N trimethylglycine that regulates the methionine cycle and homocysteine (a risk factor for cardiovascular disease) detoxification through betaine-homocysteine methyltransferases. Betaine is nontoxic and has several beneficial effects in different disease models. Betaine treatment decreases the amyloid β generation, reduces obesity, improves steatosis and fibrosis, and activates AMP-activated protein kinase (AMPK). Further, betaine downregulates 8‑hydroxy-2-deoxyguanosine, malondialdehyde, and upregulates catalases, glutathione peroxidase, and superoxide dismutase activity. Therefore, we hypothesized that betaine might be a rational drug candidate to effectively combat Dox-associated oxidative stress, inflammation, and mitochondrial dysfunction.</p></div>","PeriodicalId":72106,"journal":{"name":"Advances in redox research : an official journal of the Society for Redox Biology and Medicine and the Society for Free Radical Research-Europe","volume":"9 ","pages":"Article 100084"},"PeriodicalIF":0.0,"publicationDate":"2023-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"49776019","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Terpinen-4-ol, A volatile terpene molecule, extensively electrifies the biological systems against the oxidative stress-linked pathogenesis","authors":"Jobaier Ibne Deen ,&nbsp;A.N.M. Shahriar Zawad ,&nbsp;Mijbah Uddin ,&nbsp;Muhammad Abid Hasan Chowdhury ,&nbsp;Salahuddin Qader Al Araby ,&nbsp;Md. Atiar Rahman","doi":"10.1016/j.arres.2023.100082","DOIUrl":"https://doi.org/10.1016/j.arres.2023.100082","url":null,"abstract":"<div><p>Terpenes and their derivatives in essential oil have been raising an upstream interest due to their unwavering health-promoting effects and safety profiles, although the individual essential oil components are inadequately assessed for their biological potential. Terpinen-4-ol, a bioactive natural terpene-derivative unambiguously distributed in most essential oil sources, is displaying a very remarkable role as a phytometabolite. This review, therefore, deciphered the health-promoting effects of Terpinen-4-ol in oxidative stress-linked diseases including neurodegenerative disorders, cancers, cardiovascular diseases, diabetes, and inflammatory disorders. Using Google as a search engine, this systematic review unraveled 217 relevant articles out of 857 search results from Web of Science, PubMed, and ScienceDirect. Terpinen-4-ol is reported to increase superoxide dismutase, decrease glutathione-S-transferase and acetylcholine esterase, inhibit NF-κB and NLRP3 inflammasome activation pathway, downregulate the α-amylase activity and increase insulin sensitivity, and substantially inhibit the generation of inflammatory mediators such as IL-1β, IL-6, IL-10. Despite several beneficial actions of Terpinen-4-ol, it has hardly been expedited to use as pharmaceutical therapeutic target for unveiled biological activities. In that context, this review has focused on the role of Terpinen-4-ol in attenuating oxidative stress and stress-linked pathophysiological conditions unraveling a research gap on it to manifest its best pharmaceutical and therapeutic uses.</p></div>","PeriodicalId":72106,"journal":{"name":"Advances in redox research : an official journal of the Society for Redox Biology and Medicine and the Society for Free Radical Research-Europe","volume":"9 ","pages":"Article 100082"},"PeriodicalIF":0.0,"publicationDate":"2023-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"49776020","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"EGCG: The antioxidant powerhouse in lung cancer management and chemotherapy enhancement","authors":"Amit Sehgal ,&nbsp;Majaz Ahmad Bhat ,&nbsp;Deeksha Dogra ,&nbsp;Suman Rawat ,&nbsp;Sunil Kumar Dhatwalia","doi":"10.1016/j.arres.2023.100085","DOIUrl":"https://doi.org/10.1016/j.arres.2023.100085","url":null,"abstract":"<div><p>Lung cancer is the main cause of cancer-related deaths throughout the world. Its treatment involves intensive cycles of chemotherapy and radiotherapy, which are associated with serious adverse effects. EGCG, an active component of green tea/white tea, regulates cell molecular pathways of apoptosis, angiogenesis, proliferation, differentiation, and self-renewal ability of cancer stem cells. It also acts as a pro-oxidant that can cause cell death in cancer cells via apoptosis. It can control lung carcinogenesis by altering the molecules involved in multiple signal transduction pathways like Ras-GTPase, ERK, COX2, VEGF, and protein kinases. Moreover, it can also affect other signalling molecules or pathways such as DNMT1, MAPK, NF-κB, Bcl/Bax, HIF-1α, EGFR, Akt/PI3, Wnt/β-catenin, caspases, NEAT1, TGF-β, HDGF, and CLOCK. Recent studies on cell lines and animals have focused on the role of EGCG in enhancing the efficacy of chemotherapeutic drugs and reducing their adverse effects. The low bioavailability and rapid metabolism of EGCG can act as a hurdle in the translation of this agent from lab to bedside. The uses of synthetic agents such as COMT inhibitors and nano-drug delivery tools have been shown to enhance the plasma levels of EGCG and its cancer preventive and therapeutic ability.</p></div>","PeriodicalId":72106,"journal":{"name":"Advances in redox research : an official journal of the Society for Redox Biology and Medicine and the Society for Free Radical Research-Europe","volume":"9 ","pages":"Article 100085"},"PeriodicalIF":0.0,"publicationDate":"2023-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2667137923000255/pdfft?md5=716f139a1f09137a3cdd5ec838398cb3&pid=1-s2.0-S2667137923000255-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"92019990","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Regulation of metabolism, stress response, and sod1 activity by cytosolic thioredoxins in yeast depends on growth phase","authors":"Cecilia Picazo ,&nbsp;C. Alicia Padilla ,&nbsp;Brian McDonagh ,&nbsp;Emilia Matallana ,&nbsp;José A. Bárcena ,&nbsp;Agustín Aranda","doi":"10.1016/j.arres.2023.100081","DOIUrl":"https://doi.org/10.1016/j.arres.2023.100081","url":null,"abstract":"<div><p>Reactive Oxygen Species (ROS) can be harmful compounds that can cause damage to macromolecules like lipids, proteins, and DNA when their levels exceed cellular defense mechanisms. Cells have protection and ROS detoxification systems, including thioredoxin and glutaredoxin systems, to counteract oxidative stress. The role of cytosolic thioredoxin system (cTRX) was investigated in different growth phases using a mutant strain lacking both <em>TRX1</em> and <em>TRX2</em>. The mutant showed a defect in survival during the non-dividing state or stationary phase. The levels of glutathione, an antioxidant, in the mutants were higher in both total and reduced glutathione, indicating an increase in oxidative response. The mutant also showed an increase in protein-bound glutathione, suggesting a compensatory mechanism to counter balance oxidative stress. Proteomic analysis revealed changes in the expression of various proteins in the absence of cytosolic thioredoxins. Upregulated proteins in both exponential and stationary phases were mainly related to oxidative stress response and metabolism. Downregulated proteins in both phases were associated with glycerol metabolism, glycolysis, and ATP synthesis. These changes indicated a compensatory response to redox imbalance caused by the absence of cytosolic thioredoxins. Further analysis focused on the reversible oxidation of cysteine residues in proteins. Several proteins were identified with cysteines susceptible to reversible oxidation, and their oxidation status was affected by the absence of cytosolic thioredoxins. Notably, cysteine 146 of cytosolic Superoxide Dismutase 1 (Sod1) was more oxidized in growth phase, while oxidation of ribosomal proteins was seen only in exponential phase.</p><p>Overall, this study provides insights into the role of cytosolic thioredoxin system in growth, aging, in maintaining redox balance, protecting against oxidative stress as well as its impact on <em>SOD1</em> activity and glutathionylation.</p></div>","PeriodicalId":72106,"journal":{"name":"Advances in redox research : an official journal of the Society for Redox Biology and Medicine and the Society for Free Radical Research-Europe","volume":"9 ","pages":"Article 100081"},"PeriodicalIF":0.0,"publicationDate":"2023-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"49776022","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"High–intensity exercise training induces the oxidative modification of malate dehydrogenase 2 in skeletal muscles","authors":"Maki Takami ,&nbsp;Wataru Aoi ,&nbsp;Chinatsu Ando ,&nbsp;Yoji Kato ,&nbsp;Yukiko Kobayashi ,&nbsp;Masashi Kuwahata","doi":"10.1016/j.arres.2023.100076","DOIUrl":"10.1016/j.arres.2023.100076","url":null,"abstract":"<div><p>High–intensity exercise training abrogates the aerobic metabolic system in skeletal muscles. Mitochondria play a crucial role in aerobic metabolism and regulate energy supply for muscle contraction. Although the detailed mechanism of mitochondrial dysfunction remains unknown, excessive reactive oxygen species (ROS) generated in response to high–intensity exercise may be involved. Herein, we examined the oxidative modification of mitochondrial proteins in mouse muscle following high–intensity exercise training. Male ICR mice (10–week–old) were divided into sedentary and high–intensity exercise groups. Mice in the exercise group received treadmill training five times per week for two weeks. The levels of oxidative protein modifications and the factors related to mitochondrial biogenesis and dynamics in the gastrocnemius muscle were measured. The levels of hexanoyl lysine adduct (HEL) and 4–hydroxy–2–nonenal (HNE) modified proteins tended to be higher in the muscle mitochondrial fraction, but not whole extractions, of the exercise group than in that of the sedentary group. Specifically, HEL and HNE modifications of malate dehydrogenase 2 (MDH2), a citric acid cycle–related enzyme, were particularly higher in the exercise group mice. Although mitochondrial biogenesis factors were upregulated by exercise, higher phosphorylation of dynamin–related protein 1 (Ser637) was observed in the exercise group. These results suggest that oxidative modification of MDH2 impairs the metabolic system following high–intensity exercise training, which may be associated with attenuated adaptation.</p></div>","PeriodicalId":72106,"journal":{"name":"Advances in redox research : an official journal of the Society for Redox Biology and Medicine and the Society for Free Radical Research-Europe","volume":"9 ","pages":"Article 100076"},"PeriodicalIF":0.0,"publicationDate":"2023-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"41654193","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Effect of dichlorvos on kidney functions with reference to altered AChE gene expression in mice","authors":"Sonam Agarwal ,&nbsp;Renu Bist ,&nbsp;Himani Kuntal ,&nbsp;D.K. Bhatt","doi":"10.1016/j.arres.2023.100078","DOIUrl":"10.1016/j.arres.2023.100078","url":null,"abstract":"<div><h3>Background</h3><p>The dichlorvos is reported to cause toxic effects by inducing oxidative stress via modification in antioxidant enzymes. Besides, the neurotransmitters (NTs) linked enzyme acetylcholinesterase (AChE) is also inhibited in the kidneys of dichlorvos treated mice. The exact mechanism of toxic action of dichlorvos on AChE gene expression is not clearly understood.</p></div><div><h3>Purpose</h3><p>The present study is aimed to elucidate a possible mechanism by which dichlorvos induces nephrotoxicity in mice. Moreover, it is further clarified that how AChE gene expression gets modified in dichlorvos treated mice.</p></div><div><h3>Study design and methods</h3><p>The study was carried out on healthy male mice, 4–5 weeks old weighing 21±1 g. The animals were equally divided into two groups. The first group served as control, whereas the animals of the second group were given dichlorvos 40 mg/kg b.w. i.p. for 21 days.</p></div><div><h3>Results</h3><p>The treatment of dichlorvos revealed decline in various antioxidants such as catalase (CAT), superoxide dismutase (SOD), glutathione peroxidase (GP_X), glutathione-S-transferase (GST) and reduced glutathione (GSH) in mice kidneys. The significance level of these antioxidants ranged from <em>P</em>&lt; 0.05 to <em>P</em>&lt;0.001.</p></div><div><h3>Conclusion</h3><p>The dichlorvos is causing increase in production of highly reactive oxygen species (ROS) owing to inhibition of antioxidant enzymes studied in the present study. The ROS being highly reactive molecules AChE gene seems to be mutated. This is reflected in the modulation of kidney functions by increasing levels of urea, uric acid and creatinine.</p></div>","PeriodicalId":72106,"journal":{"name":"Advances in redox research : an official journal of the Society for Redox Biology and Medicine and the Society for Free Radical Research-Europe","volume":"9 ","pages":"Article 100078"},"PeriodicalIF":0.0,"publicationDate":"2023-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"41796313","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Stability of aqueous solutions of ascorbate for basic research and for intravenous administration","authors":"Brett A. Wagner,&nbsp;Garry R. Buettner","doi":"10.1016/j.arres.2023.100077","DOIUrl":"10.1016/j.arres.2023.100077","url":null,"abstract":"<div><p>Ascorbate (vitamin C) can rapidly oxidize in many near-neutral pH, aqueous solutions. We report on the stability of ascorbate solutions prepared for infusion into patients using standard pharmacy protocols, for example, 75 g of ascorbate/L in water for infusion. The concentration of ascorbate was monitored for changes over time using direct UV–Vis spectroscopy. The pH of the solution was about 5.7 with no significant change over 24 h. There was only an approximate loss of 1% per day over the first 3 days of storage. This information allows decisions on how far ahead of need such preparations can be made. We also provide laboratory approaches to minimize or control the rate of oxidation of ascorbate solutions for use in chemical and biochemical studies as well as preclinical animal studies. The goal is to have the amount of ascorbate intended to be used in experiments be the actual amount available.</p></div>","PeriodicalId":72106,"journal":{"name":"Advances in redox research : an official journal of the Society for Redox Biology and Medicine and the Society for Free Radical Research-Europe","volume":"9 ","pages":"Article 100077"},"PeriodicalIF":0.0,"publicationDate":"2023-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10552410/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"41160690","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Heme induced cell death: You can run from TLR4 but you cannot hide from ROS","authors":"Rafael Cardoso Maciel Costa Silva","doi":"10.1016/j.arres.2023.100073","DOIUrl":"10.1016/j.arres.2023.100073","url":null,"abstract":"<div><p>Heme is the prosthetic group of several enzymes and proteins, including cytochrome c oxidase and hemoglobin. During hemolytic events, high amounts of heme derived from hemoglobin can be released from red blood cells, contributing to the pathogenesis of different hemolytic diseases. Heme-induced cell death is an important player in this situation, and different studies report that heme stimulus can lead to distinct types of regulated cell death. Here, I hypothesize that, when incubated in the presence of high heme concentration, macrophages display concomitant and distinct types of cell death, including necroptosis and a yet to be identified type of cell death. This hypothesis is based on recently published results discussed throughout this manuscript.</p></div>","PeriodicalId":72106,"journal":{"name":"Advances in redox research : an official journal of the Society for Redox Biology and Medicine and the Society for Free Radical Research-Europe","volume":"9 ","pages":"Article 100073"},"PeriodicalIF":0.0,"publicationDate":"2023-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"43620021","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"NOX1 and PRDX6 synergistically support migration and invasiveness of hepatocellular carcinoma cells through enhanced NADPH oxidase activity","authors":"Daniel J. Lagal ,&nbsp;J. Antonio Bárcena ,&nbsp;Raquel Requejo-Aguilar ,&nbsp;C. Alicia Padilla ,&nbsp;Thomas L. Leto","doi":"10.1016/j.arres.2023.100080","DOIUrl":"10.1016/j.arres.2023.100080","url":null,"abstract":"<div><p>The NADPH oxidase 1 (NOX1) complex formed by proteins NOX1, p22phox, NOXO1, NOXA1, and RAC1 plays an important role in the generation of superoxide and other reactive oxygen species (ROS) which are involved in normal and pathological cell functions due to their effects on diverse cell signaling pathways. Cell migration and invasiveness are at the origin of tumor metastasis during cancer progression which involves a process of cellular de-differentiation known as the epithelial-mesenchymal transition (EMT). During EMT cells lose their polarized epithelial phenotype and express mesenchymal marker proteins that enable cytoskeletal rearrangements promoting cell migration, expression and activation of matrix metalloproteinases (MMPs), tissue remodeling, and cell invasion during metastasis. In this work, we explored the importance of the peroxiredoxin 6 (PRDX6)-NOX1 enzyme interaction leading to NOXA1 protein stabilization and increased levels of superoxide produced by NOX in hepatocarcinoma cells. This increase was accompanied by higher levels of N-cadherin and MMP2, correlating with a greater capacity for cell migration and invasiveness of SNU475 hepatocarcinoma cells. The increase in superoxide and the associated downstream effects on cancer progression were suppressed when phospholipase A₂ or peroxidase activities of PRDX6 were abolished by site-directed mutagenesis, reinforcing the importance of these catalytic activities in supporting NOX1-based superoxide generation. Overall, these results demonstrate a clear functional cooperation between NOX1 and PRDX6 catalytic activities which generate higher levels of ROS production, resulting in a more aggressive tumor phenotype.</p></div>","PeriodicalId":72106,"journal":{"name":"Advances in redox research : an official journal of the Society for Redox Biology and Medicine and the Society for Free Radical Research-Europe","volume":"9 ","pages":"Article 100080"},"PeriodicalIF":0.0,"publicationDate":"2023-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"45901091","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Ascorbate mediates the non-enzymatic reduction of nitrite to nitric oxide","authors":"Juan Du ,&nbsp;Milos R. Filipović ,&nbsp;Brett A. Wagner ,&nbsp;Garry R. Buettner","doi":"10.1016/j.arres.2023.100079","DOIUrl":"10.1016/j.arres.2023.100079","url":null,"abstract":"<div><p>Nitric oxide (NO^•) generated by nitric oxide synthases is involved in many physiological and pathophysiological processes. However, non-enzymatic formation of NO^• also occurs <em>in vivo</em>. Here we investigated the production of NO^• from nitrite, as facilitated by ascorbate, over the pH range of 2.4–7.4. Using a nitric oxide electrode, we observed at low pH a rapid generation of NO^• from nitrite and ascorbate that slows with increasing pH. The formation of NO^• was confirmed by its reaction with oxyhemoglobin. In the ascorbate/nitrite system a steady-state level of NO^• was achieved, suggesting that a futile redox cycle of nitrite-reduction by ascorbate and NO^•-oxidation by dioxygen was established. However, at pH-values of around 7 and greater, the direct reduction of nitrite by ascorbate is very slow; thus, this route to the non-enzymatic production of NO^• is not likely to be significant process <em>in vivo</em> in environments having a pH around 7.4. The production of nitric oxide by nitrite and ascorbate would be important only in areas of lower pH, <em>e.g.</em> stomach/digestive system, sites of inflammation, and areas of hypoxia such as tumor tissue. In patients receiving very large doses of ascorbate delivered by intravenous infusion, plasma levels of ascorbate on the order of 20 - 30 mM can be achieved. After infusion, levels of nitrate and nitrite in plasma were unchanged. Thus, in blood and tissue that maintain a pH of about 7.4, the reduction of nitrite to nitric oxide by ascorbate appears to be insignificant, even at very large, pharmacological levels of ascorbate.</p></div>","PeriodicalId":72106,"journal":{"name":"Advances in redox research : an official journal of the Society for Redox Biology and Medicine and the Society for Free Radical Research-Europe","volume":"9 ","pages":"Article 100079"},"PeriodicalIF":0.0,"publicationDate":"2023-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10486277/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10605702","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}