Redox Biochemistry and Chemistry最新文献

{"title":"Activation of cellular signalling pathways and apoptosis by the aldehyde acrolein – A major environmental hazard","authors":"Diana A. Averill-Bates,&nbsp;André Tanel","doi":"10.1016/j.rbc.2023.100019","DOIUrl":"10.1016/j.rbc.2023.100019","url":null,"abstract":"<div><p>Interest in the molecular actions of acrolein has increased in light of growing knowledge that implicates this reactive aldehyde in a wide range of pathophysiologies including neurodegenerative diseases, various lung disorders including chronic obstructive pulmonary disease, atherosclerosis, and certain cancers. This is rendered complex because acrolein exists in mixtures of environmental pollutants. Reactive α,β-unsaturated aldehydes like acrolein are major components of common environmental pollutants like cigarettes, automobile exhaust, and smoke from wood, coal, forest and house fires. It is a natural constituent of several foods and is generated in the human body during inflammation or oxidation of unsaturated lipids. Acrolein is also a toxic metabolic product of the widely used anticancer drug cyclophosphamide and is generated from the enzymatic oxidation of polyamines. It is a toxic by-product of lipid peroxidation and has been implicated as a mediator of oxidative damage in cells and tissues. The purpose of this review is to assess the literature about the activation of cell signalling pathways and transcription factors, and cell survival and cell death pathways by acrolein. Several reports show that anti-apoptosis processes dominate at lower dose exposures to acrolein, whereas pro-apoptotic processes and necrosis dominate at higher dose exposures. There has been improved understanding about the deleterious molecular and cellular mechanisms that are triggered in cells in response to acrolein injury. However, more progress is required to define the contributions of acrolein to human diseases and to design efficient therapeutic strategies based on the biochemical modulation of acrolein activity.</p></div>","PeriodicalId":101065,"journal":{"name":"Redox Biochemistry and Chemistry","volume":"7 ","pages":"Article 100019"},"PeriodicalIF":0.0,"publicationDate":"2024-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2773176623000184/pdfft?md5=9c33fed1db3a45958274b57c9b23009a&pid=1-s2.0-S2773176623000184-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"138988898","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":"Reactivity of mitochondrial peroxiredoxins with biological hydroperoxides","authors":"Madia Trujillo ,&nbsp;Lucía Piacenza ,&nbsp;Rafael Radi","doi":"10.1016/j.rbc.2023.100017","DOIUrl":"https://doi.org/10.1016/j.rbc.2023.100017","url":null,"abstract":"<div><p>Mitochondria are main sources of biological hydroperoxides, including hydrogen peroxide, peroxynitrite and various organic hydroperoxides. Most of these species are involved in the regulation of cellular functions when formed at low, physiological levels. Additionally, they can cause oxidative damage when formed at higher rates, eventually leading to mitochondrial disfunction and cytotoxicity. Different peroxidases sense the levels and catalyze the reduction of mitochondrial hydroperoxides. Among them, peroxiredoxin 3 and peroxiredoxin 5 decompose most hydrogen peroxide, peroxynitrite and free fatty acid hydroperoxides formed in the mitochondrial matrix. Kinetic considerations indicate that the role of selenol-dependent glutathione peroxidases in the reduction of these soluble hydroperoxides in mitochondria would be secondary. Glutathione peroxidase 4, which has a unique phospholipid hydroperoxide peroxidase activity, is only expressed in the mitochondria of selected tissues. Peroxiredoxin 3 catalyzes the reduction of hydroperoxides, but is also hyperoxidized and inactivated by them, in particular by free fatty acid hydroperoxides which react at high rate constants. Indeed, computer-assisted simulations support that free fatty acid hydroperoxides significantly contribute to Prdx3 hyperoxidation under biologically-relevant conditions. In addition, kinetic data indicate that hydroperoxides may partially diffuse to the cytosol. Several open questions regarding the oxidizing substrate specificities of mitochondrial peroxiredoxins and their modulation by CO₂ are presented. Thus, peroxiredoxins 3 and 5 are the main sensors of mitochondrial hydroperoxides, provide protection from their excess and also determine the ability of these reactive species to diffuse through mitochondria; these combined actions of the mitochondrial peroxiredoxins impact redox regulation and outcomes of physiological or pathological processes.</p></div>","PeriodicalId":101065,"journal":{"name":"Redox Biochemistry and Chemistry","volume":"5 ","pages":"Article 100017"},"PeriodicalIF":0.0,"publicationDate":"2023-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2773176623000160/pdfft?md5=0b54038be7d1a0f97e7ca09df880b7b9&pid=1-s2.0-S2773176623000160-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"134657763","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":"Electron paramagnetic resonance (EPR) for investigating relevant players of redox reactions: Radicals, metalloproteins and transition metal ions","authors":"Ohara Augusto,&nbsp;Daniela Ramos Truzzi,&nbsp;Edlaine Linares","doi":"10.1016/j.rbc.2023.100009","DOIUrl":"https://doi.org/10.1016/j.rbc.2023.100009","url":null,"abstract":"<div><p>Electron paramagnetic resonance (EPR) spectroscopy is unique in providing robust information about free radicals, transition metal ions and metalloenzymes, which are crucial players in redox processes. EPR had a major role in advancing the redox biology field during the 20th century, but the interest in this methodology considerably decreased in recent years. Here, we discuss potential reasons for this decline as well as potential reasons for maintaining the mind open to the many possibilities brought by EPR and associated methodologies to the redox field. We present the fundamentals of EPR using pictorial images and minimal physicochemical language. We also present EPR derived methodologies developed to detect radical metabolites, that is, direct EPR of solutions (static and continuous-flow), direct EPR of frozen solutions, spin-trapping and spin-scavenging, showing examples and discussing the advantages and drawbacks of each one. Finally, we discuss the EPR spectra of metalloproteins and metal ion complexes of biological interest, which are more complex than those of radical metabolites in solution. In addition to introduce EPR methodologies to those new to the redox field, our goal is to show that these methodologies can contribute to advance the field.</p></div>","PeriodicalId":101065,"journal":{"name":"Redox Biochemistry and Chemistry","volume":"5 ","pages":"Article 100009"},"PeriodicalIF":0.0,"publicationDate":"2023-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"49738239","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":"Could CO2 be a player in a redox relay team?","authors":"Alexander V. Peskin","doi":"10.1016/j.rbc.2023.100006","DOIUrl":"https://doi.org/10.1016/j.rbc.2023.100006","url":null,"abstract":"<div><p>It has been established that hydrogen peroxide (H₂O₂) acts as a signalling messenger by triggering the reversible oxidation of redox-regulated proteins via a redox-relay provided by peroxiredoxins (Prdxs). Exceptionally high reactivity of Prdxs with H₂O₂ exceeding other thiols by orders of magnitude places Prdxs as sensors of H₂O₂ and distributers of oxidizing equivalents to specific thiol targets which can't be oxidized by H₂O₂ directly. By this mechanism the oxidative stress response can be achieved.</p><p>Despite its involvement in oxidative stress responses, H₂O₂ is continuously generated as a normal metabolite necessary for regular cell functioning. The challenge lies in understanding how the Prdx-dependent redox relay can differentiate between basal levels of H₂O₂ and excessive amounts that lead to oxidative stress.</p><p>Peroxymonocarbonate, an oxidant formed when H₂O₂ reacts with CO₂/HCO₃⁻, emerges as a potent cellular oxidant. The peroxymonocarbonate formation could be catalysed and then consumed at localised sites by certain thiol proteins. This mechanism could prevent H₂O₂ from reacting with Prdx, thereby averting the redox-relayed activation of regulatory thiol proteins and subsequent oxidative stress response below a certain level of H₂O₂.</p></div>","PeriodicalId":101065,"journal":{"name":"Redox Biochemistry and Chemistry","volume":"5 ","pages":"Article 100006"},"PeriodicalIF":0.0,"publicationDate":"2023-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"49726774","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":"Lipid biology of plasmalogen-derived halolipids: Signature molecules of myeloperoxidase and eosinophil peroxidase activity","authors":"Reagan M. McGuffee ,&nbsp;Christy M. Hadfield ,&nbsp;David A. Ford","doi":"10.1016/j.rbc.2023.100011","DOIUrl":"https://doi.org/10.1016/j.rbc.2023.100011","url":null,"abstract":"<div><p>Myeloperoxidase and eosinophil peroxidase exert their antimicrobial functions through the oxidative actions of their hypohalous acid products. Plasmalogen phospholipids are particularly susceptible to oxidation of their vinyl ether functional group by hypohalous acids. This produces a family of halogenated lipid products with pro-inflammatory roles and potential biomarker utility. The initial product of plasmalogen oxidation by HOCl is 2-chlorofatty aldehyde, which has been shown to play a key role at the blood-endothelium interface. <em>In vitro</em> and <em>in vivo</em> studies indicate increased endothelial barrier permeability, neutrophil chemotaxis, neutrophil and platelet adherence to endothelium, and promotion of erythrocyte lysis as some of its effects. These effects may be due to protein modification by 2-chlorofatty aldehyde. 2-Chlorofatty aldehyde is metabolized by host dehydrogenases to 2-chlorofatty acid. While it is less chemically reactive, 2-chlorofatty acid has partial overlap of pro-inflammatory effects with 2-chlorofatty aldehyde and unique actions such as induction of neutrophil extracellular trap formation. The stability of 2-chlorofatty acid in plasma also makes it well-suited as a biomarker of HOCl generation, and its plasma levels may be predictive of disease outcomes. 2-Bromofatty aldehydes and acids are produced analogously from HOBr reaction with plasmalogens. Their functions have yet to be well-elucidated, though similarities with chlorolipids have been observed, and increased reactivity with proteins is expected through enhanced electrophilicity of the alpha carbon. Altogether, these halogenated lipids represent underexplored mediators of diseases involving excess hypohalous acid production.</p></div>","PeriodicalId":101065,"journal":{"name":"Redox Biochemistry and Chemistry","volume":"5 ","pages":"Article 100011"},"PeriodicalIF":0.0,"publicationDate":"2023-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"49738430","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":"Unveiling the enigmatic traits of Corynebacterium glutamicum mycoredoxin-3: A tiny redox protein displaying swapped homodimer formation and DsbA-like oxidase activity","authors":"Khadija Wahni ,&nbsp;Ekaterina Baranova ,&nbsp;Daria Ezeriņa ,&nbsp;Inge Van Molle ,&nbsp;Koen Van Laer ,&nbsp;Joris Messens","doi":"10.1016/j.rbc.2023.100014","DOIUrl":"https://doi.org/10.1016/j.rbc.2023.100014","url":null,"abstract":"<div><p>Mycoredoxins (Mrxs) are a group of small dithiol oxidoreductases that share a conserved CXXC active site sequence motif resembling glutaredoxins. They are commonly found in saprophytic microorganisms, including Actinobacteria such as <em>Mycobacterium tuberculosis</em>. Among the known mycoredoxins, <em>Corynebacterium glutamicum</em> (Cg) Mrx1, featuring a conserved CVQC active site, functions as a mycothiol-dependent monothiol oxidoreductase. On the other hand, Mrx2, also known as NrdH-redoxin and containing the same CVQC motif, exhibits dithiol oxidoreductase properties and receives electrons from thioredoxin reductase (TrxR). Recently, it has been reported that CgMrx3, featuring a CGSC motif, acts as a thioredoxin, although its structural and biophysical characteristics remain unexplored.</p><p>In this study, we successfully determined the X-ray structure of CgMrx3 at a resolution of 1.7 Å, revealing a swapped dimer arrangement. We compared the structure of CgMrx3 with those of CgMrx1 and CgMrx2 and with the AlphaFold2 predicted structure of Mrx3 from <em>Mycobaterium tuberculosis</em> (MtMrx3). We correlated the number of hydrogen bonds accepted by the nucleophilic cysteines with the relatively low pKa's determined for MtMrx3 and CgMrx3. Finally, we showed that CgMrx3 has DsbA-like oxidase activity. Taken together, our results provide valuable insights into the structural and functional characteristics of Mrx3, thereby enhancing our understanding of mycoredoxin-dependent redox biology.</p></div>","PeriodicalId":101065,"journal":{"name":"Redox Biochemistry and Chemistry","volume":"5 ","pages":"Article 100014"},"PeriodicalIF":0.0,"publicationDate":"2023-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"49726771","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":"Inter(pseudo)halogens with relevance to peroxidase-mediated reactions","authors":"Jürgen Arnhold ,&nbsp;Ernst Malle","doi":"10.1016/j.rbc.2023.100012","DOIUrl":"https://doi.org/10.1016/j.rbc.2023.100012","url":null,"abstract":"<div><p>In mammals, heme peroxidases are well known to generate oxidized (pseudo)halide products such as hypochlorous acid, hypobromous acid, oxidized iodine species, and hypothiocyanite. In addition, inter(pseudo)halogens are also oxidized (pseudo)halide compounds where two or more different (pseudo)halides are combined within a molecule without participation of other atoms. However, the information of this group of chemicals as potential products of peroxidases is limited and very fragmentary. In this review, we summarize current knowledge about chemical properties of inter(pseudo)halogens, their role as products of peroxidase-mediated conversions, and possible applications of these compounds in antimicrobial defense. The major focus is directed on bromyl chloride, cyanogen halides, and some products derived from interaction of oxidized iodine with thiocyanate.</p></div>","PeriodicalId":101065,"journal":{"name":"Redox Biochemistry and Chemistry","volume":"5 ","pages":"Article 100012"},"PeriodicalIF":0.0,"publicationDate":"2023-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"49726364","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":"Intracellular distribution of bis-allylic deuterated linoleic acid into the lipidome of human keratinocytes","authors":"Rosangela S. Santos ,&nbsp;Márcia S.F. Franco ,&nbsp;Felipe G. Ravagnani ,&nbsp;Adriano B. Chaves-Filho ,&nbsp;Sayuri Miyamoto ,&nbsp;Mauricio S. Baptista ,&nbsp;Mikhail S. Shchepinov ,&nbsp;Marcos Y. Yoshinaga","doi":"10.1016/j.rbc.2023.100005","DOIUrl":"https://doi.org/10.1016/j.rbc.2023.100005","url":null,"abstract":"<div><p>Polyunsaturated fatty acids (PUFA) are particularly susceptible to free radical-induced lipid peroxidation (LPO). Specific deuteration at bis-allylic positions of PUFA (D-PUFA) has been recently proposed as a way to inhibit the LPO. Here, a high mass resolution untargeted lipidomic analysis protocol was applied to examine the changes in the lipidome of keratinocytes supplemented with bis-allylic deuterated linoleic acid (D₂-LA). Incorporation of D₂-LA occurs preferentially in membrane phospholipids such as phosphatidylcholine and phosphatidylethanolamine, followed by triglycerides. However, the relative contribution of D₂-LA among membrane lipids is highest in cardiolipin (60%) followed by its precursor phosphatidylglycerol (50%). Cardiolipins are enriched in PUFA and exclusively located in mitochondrial membranes, thus representing major targets for lipid peroxidation. These findings indicate that D₂-LA supplementation is linked to the preservation of mitochondrial function under oxidative stress. Finally, our study highlights the suitability of high mass resolution lipidomic analysis to investigate lipid metabolism at the level of individual molecular species in stable isotope tracing experiments.</p></div>","PeriodicalId":101065,"journal":{"name":"Redox Biochemistry and Chemistry","volume":"5 ","pages":"Article 100005"},"PeriodicalIF":0.0,"publicationDate":"2023-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"49726689","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":"The oxidation of fenamic acid NSAIDs by neutrophil myeloperoxidase produces toxic reactive metabolites that induce leukemic cell death","authors":"Newton H. Tran ,&nbsp;Dinesh Babu ,&nbsp;Steven Lockhart ,&nbsp;Andrew G. Morgan ,&nbsp;Nadine Commandeur ,&nbsp;Md Harunur Rashid ,&nbsp;Béla Reiz ,&nbsp;Lusine Tonoyan ,&nbsp;Arno G. Siraki","doi":"10.1016/j.rbc.2023.100013","DOIUrl":"https://doi.org/10.1016/j.rbc.2023.100013","url":null,"abstract":"<div><p>Fenamic acids are a group of non-steroidal anti-inflammatory drugs (NSAIDs) that are among the most common drugs prescribed globally. However, they have been associated with many adverse effects, such as agranulocytosis, neutropenia, hepatotoxicity, and nephrotoxicity. The interactions between peroxidase enzymes and fenamic acid-like NSAIDs cause the formation of reactive species, potentially involved in side effects. The aim of this study was to investigate the neutrophil myeloperoxidase (MPO)-mediated bioactivation of fenamic acids based on N-phenylanthranilic acid (NPA) and its four drug analogues: flufenamic acid (FFA), mefenamic acid (MFA), meclofenamic acid (MCFA), and tolfenamic acid (TFA). We hypothesized that the enzymatic oxidation of fenamic acids by MPO/hydrogen peroxide (H₂O₂) would produce reactive metabolites, cause oxidative damage and induce cytotoxicity. We utilized UV–Vis spectrophotometry, liquid chromatography-mass spectrometry (LC-MS), and electron paramagnetic spin resonance (EPR) spectroscopy using purified MPO from human neutrophils. In addition, <em>in vitro</em> studies were performed with MPO-containing human promyelocytic leukemia (HL-60) cells for cytotoxicity and immuno-spin trapping to detect protein-free radicals. UV–Vis spectrophotometry revealed that MPO oxidized the fenamic acids. LC-MS analyses revealed the formation of dimers, hydroxylated, and quinoneimine species, and glutathione (GSH) conjugates. EPR spin trapping with DMPO using GSH revealed that fenamic acids produced glutathionyl radicals in a concentration-dependent manner. We also detected the formation of protein-free radicals in HL-60 cells, which correlated with cytotoxicity. Despite the minor structural differences between the fenamic acids, there were variations in their oxidation potential. These findings revealed a correlation between pro-oxidant metabolite reactivity and cytotoxicity caused by fenamic acid NSAIDs.</p></div>","PeriodicalId":101065,"journal":{"name":"Redox Biochemistry and Chemistry","volume":"5 ","pages":"Article 100013"},"PeriodicalIF":0.0,"publicationDate":"2023-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"49754463","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":"Arsenic exposure and increased C-reactive protein are independently associated with lower erythrocyte glutathione peroxidase activity in Bangladeshi children","authors":"Dorian M. Cheff ,&nbsp;Helena Skröder ,&nbsp;Evana Akhtar ,&nbsp;Qing Cheng ,&nbsp;Matthew D. Hall ,&nbsp;Rubhana Raqib ,&nbsp;Maria Kippler ,&nbsp;Marie Vahter ,&nbsp;Elias S.J. Arnér","doi":"10.1016/j.rbc.2023.100015","DOIUrl":"https://doi.org/10.1016/j.rbc.2023.100015","url":null,"abstract":"<div><p>Toxic metal contaminants present in food and water have widespread effects on health and disease. Chalcophiles, such as arsenic, cadmium, and mercury, show a high affinity to selenium and exposure to these metals could have a modulating effect on enzymes dependent on selenocysteine in their active sites. The aim of this study was to assess the influence of these metals on the activity of the selenoprotein glutathione peroxidase 1 (GPX1) in erythrocytes of 100 children residing in rural Bangladesh, where drinking water often contains arsenic. GPX1 expression, as measured using high-throughput immunoblotting, showed little correlation with GPX activity (<em>r</em>_<em>s</em> = 0.02, p = 0.87) in blood samples. Toxic metals and selenium measured in erythrocytes using inductively coupled plasma mass spectrometry (ICP-MS) and <em>C</em>-reactive protein (CRP) measured in plasma, were all considered as effectors of this divergence in GPX enzymatic activity. Arsenic concentrations in erythrocytes were most influential for GPX1 activity (<em>r</em>_<em>s</em> = −0.395, p &lt; 0.0001), and CRP levels also negatively impacted GPX1 activity (<em>r</em>_<em>s</em> = −0.443, p &lt; 0.0001). These effects appear independent of each other as arsenic concentrations and CRP showed no correlation (<em>r</em>_<em>s</em> = 0.124, p = 0.2204). Erythrocyte selenium, cadmium, and mercury did not show any correlation with GPX1 activity, nor with CRP or arsenic. Our findings suggest that childhood exposure to inorganic arsenic, as well as inflammation triggering the release of CRP, may negatively affect GPX1 activity in erythrocytes.</p></div>","PeriodicalId":101065,"journal":{"name":"Redox Biochemistry and Chemistry","volume":"5 ","pages":"Article 100015"},"PeriodicalIF":0.0,"publicationDate":"2023-09-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"49726672","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}