Antioxidants最新文献

{"title":"Evolutionary Conservation of the Copper-Dependent Thiol Oxidase Activity of Selenium-Binding Proteins.","authors":"Hanna Schlemminger, Swantje Melina Lockowandt, Alina Löser, Anna Patricia Kipp, Lars-Oliver Klotz, Holger Steinbrenner","doi":"10.3390/antiox15091148","DOIUrl":"10.3390/antiox15091148","url":null,"abstract":"<p><p>Human selenium-binding protein 1 (SELENBP1) is a methanethiol oxidase (MTO), converting methanethiol (MT) to hydrogen sulfide (H₂S), hydrogen peroxide (H₂O₂) and formaldehyde (HCHO). SELENBP1 has orthologs in all domains of life. RdMTO, an orthologous enzyme recently identified in the marine bacterium <i>Roseobacter denitrificans</i>, was postulated to require the cysteine residue closest to its C-terminus, Cys448, for MT binding and to oxidize MT to sulfane sulfur (S⁰) rather than to H₂S. SELENBP1 and RdMTO exhibit ~53% sequence identity, with Cys448 (numbered Cys466 in SELENBP1) and amino acids required for copper binding being conserved. Therefore, we here compared the MTO activity of recombinant SELENBP1 and RdMTO. We found that SELENBP1, like RdMTO, converts MT as well as structurally related alkyl thiols to form H₂S, H₂O₂ and, in the case of MT, HCHO in a strictly copper-dependent manner. MTO activity of both proteins was lowered but not abrogated upon mutation of their respective C-terminal cysteine residue. Thus, the catalytic mechanism of selenium-binding proteins that act as copper-dependent MTOs appears to be evolutionarily conserved from bacteria to humans. Presumably, this enzyme is an early evolutionary invention of prokaryotes, in order to cope with toxic thiols in their environment.</p>","PeriodicalId":7984,"journal":{"name":"Antioxidants","volume":"15 9","pages":""},"PeriodicalIF":8.2,"publicationDate":"2026-09-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13603461/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149057157","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Phytochemical Investigation of <i>Crataegus almaatensis</i> Leaves: Isolation, Structural Characterization, and Antioxidant Activity of Flavonoids, Flavolignans, and Phenolic Glycosides.","authors":"Zhanar Nabiyeva, Akerke Kulaipbekova, Asylbek Kozybayev, Handi Yang, Fuhang Song, Abdyssemat Samadun, Elmira Assembayeva, Nasi Ai","doi":"10.3390/antiox15091149","DOIUrl":"10.3390/antiox15091149","url":null,"abstract":"<p><p>A systematic phytochemical investigation of the leaves of <i>Crataegus almaatensis</i> Pojark., an endemic hawthorn species native to the mountainous regions of Kazakhstan, was carried out. Multi-step chromatographic fractionation, comprising ultrasound-assisted methanol extraction, sequential liquid-liquid partitioning, silica gel column chromatography, and preparative HPLC, afforded five phenolic compounds as individual, spectroscopically homogeneous constituents from the ethyl acetate fraction. The structures of all isolated compounds were elucidated by comprehensive analysis of high-resolution mass spectrometry (HR-ESI-QTOF-MS) data and one- and two-dimensional NMR spectroscopy (¹H, ¹³C, HSQC, HMBC) in DMSO-d₆. The following compounds were identified: (-)-epicatechin, cinchonain Ia, a methoxy- and hydroxy-substituted diaryl ether β-D-glucopyranoside, kakispyrol, and a dimethoxy-substituted diaryl ether β-D-glucopyranoside. The isolated compounds belong to three chemical classes: flavanols, flavolignans, and diaryl ether-type phenolic glycosides. Evaluation of ABTS and DPPH radical-scavenging activity revealed compound-specific antioxidant profiles, with compound <b>5</b> (cinchonain Ia) showing activity comparable to the ascorbic acid standard. This study provides, for the first time, a detailed structural characterization of individual phenolic metabolites from <i>C. almaatensis</i> leaves and makes a significant contribution to understanding the chemical diversity of this endemic species.</p>","PeriodicalId":7984,"journal":{"name":"Antioxidants","volume":"15 9","pages":""},"PeriodicalIF":8.2,"publicationDate":"2026-09-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13603708/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149057215","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Natural Antioxidants and Aquatic Animal Health-2nd Edition.","authors":"Rui Jia","doi":"10.3390/antiox15091139","DOIUrl":"10.3390/antiox15091139","url":null,"abstract":"<p><p>Sustainable aquaculture demands not only high production efficiency but also the maintenance of physiological health in farmed aquatic animals [...].</p>","PeriodicalId":7984,"journal":{"name":"Antioxidants","volume":"15 9","pages":""},"PeriodicalIF":8.2,"publicationDate":"2026-09-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13603733/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149057242","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The Proteasome Safeguards Red Blood Cell Integrity During Storage and After Transfusion.","authors":"Sandy Peltier, Théo Michel, Fanny Mialane, Mickaël Marin, Michaël Dussiot, Céline Rodriguez, Monika Dzieciatkowska, Marie Tamagne, Camille Roussel, Stéphanie Vicca, Olivier Hermine, Pierre A Buffet, Benoit Vingert, Steven L Spitalnik, Angelo D'Alessandro, Michel Prudent, Pascal Amireault","doi":"10.3390/antiox15091146","DOIUrl":"10.3390/antiox15091146","url":null,"abstract":"<p><p>Pre-transfusion storage of red blood cells (RBCs) induces aging in vitro driven by metabolic and oxidative stress, limiting transfusion efficacy. Unlike nucleated cells where multiple hallmarks characterize aging, proteostasis is expected to play a main role in anucleate RBCs, including proteasomal protein degradation. Although proteasomal activity declines during aging in vitro, its role in generating downstream alterations and post-transfusion clearance remains unclear. We hypothesized that proteasome inhibition accelerates RBC aging in vitro, particularly following re-exposure to physiological conditions. We evaluated the impact of proteasome inhibition (i.e., epoxomicin) on RBC quality during storage and physiological restoration in vitro. Additionally, young and old RBC subpopulations were compared. Proteasome inhibition during storage depleted ATP and altered RBC morphology without immediate oxidative damage. Physiological restoration of proteasome-inhibited RBCs caused accelerated ATP depletion, massive protein aggregation, reduced deformability, hemolysis, and phosphatidylserine exposure, particularly in long-stored RBCs. Strikingly, RBCs aged in vivo also exhibited low proteasomal activity and behaved similarly to stored RBCs following physiological restoration. In conclusion, proteasomal dysfunction is a key hallmark of RBC aging and senescence, driving molecular and cellular modifications that mark RBCs for clearance in vivo. Therefore, enhancing proteasomal function could improve RBC storage quality and transfusion efficacy.</p>","PeriodicalId":7984,"journal":{"name":"Antioxidants","volume":"15 9","pages":""},"PeriodicalIF":8.2,"publicationDate":"2026-09-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13603181/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149057298","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Serum Redox Biomarkers in Canine Mast Cell Tumors: Exploratory Associations with Proliferative Activity and Clinicopathological Features.","authors":"Argyrios Ginoudis, Dimitra Pardali, Mathios E Mylonakis, Serafeim Chaintoutis, Dimitris Galiatsatos, Angelos-Lauris Thomas, Zoe Polizopoulou","doi":"10.3390/antiox15091142","DOIUrl":"10.3390/antiox15091142","url":null,"abstract":"<p><p>Canine mast cell tumors (MCTs) exhibit heterogeneous biological behavior and provide a clinically relevant setting in which relationships between tumor phenotype and systemic redox homeostasis can be investigated. This exploratory prospective cohort study evaluated complementary circulating redox-related biomarkers representing hydroperoxide-derived oxidant products, antioxidant capacity, lipid peroxidation-related products, and oxidative DNA damage, and examined their associations with clinicopathological features of canine MCTs. Sixty-seven dogs with cytologically and histologically confirmed cutaneous or subcutaneous MCTs were included. Clinical staging was performed using cytological evaluation of lymph nodes, liver and spleen, and excised tumors were classified according to the Patnaik and Kiupel systems. Proliferative activity was assessed using Ki-67, and surgically excised lymph nodes were classified according to the Weishaar HN system. Serum reactive oxygen metabolites (d-ROMs), malondialdehyde (MDA), 8-hydroxy-2'-deoxyguanosine (8-OHdG) and antioxidant capacity using the OXY-adsorbent test were measured before therapeutic intervention. In the unadjusted analysis, serum MDA concentrations were higher in dogs with Ki-67 >23 than in dogs with Ki-67 ≤23 (median 10.8 vs. 7.0 μmol/L; raw <i>p</i> = 0.0254); however, this comparison did not remain statistically significant after Bonferroni correction for the 12 formal inferential biomarker × clinicopathological comparisons (adjusted <i>p</i> = 0.3052). The estimated Hodges-Lehmann location shift was +3.00 μmol/L (unadjusted bootstrap 95% CI, 0.58-6.00). No evaluated biomarker-clinicopathological association remained statistically significant after multiplicity adjustment. The observed MDA-Ki-67 pattern should therefore be regarded as exploratory and hypothesis-generating rather than as evidence of established prognostic or clinical utility. Long-term data on recurrence, progression, and survival were not available; therefore, prognostic utility could not be evaluated. Larger prospective studies incorporating longitudinal outcomes are warranted.</p>","PeriodicalId":7984,"journal":{"name":"Antioxidants","volume":"15 9","pages":""},"PeriodicalIF":8.2,"publicationDate":"2026-09-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13603415/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149057256","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Biopriming with <i>Schizophyllum commune</i> Polysaccharides Modulates Antioxidant and Biochemical Responses in <i>Pisum sativum</i> L. Seedlings.","authors":"Jovana Mišković, Milena Rašeta, Gordana Gojgić-Cvijović, Marko Radenković, Nenad Krsmanović, Nemanja Živanović, Gordana Ćirić-Marjanović, Maja Milojević-Rakić, Gordana Tamindžić, Maja Karaman","doi":"10.3390/antiox15091145","DOIUrl":"10.3390/antiox15091145","url":null,"abstract":"<p><p>This study investigated the biostimulant potential of endo- and exo-polysaccharides (PSHs) obtained from two <i>Schizophyllum commune</i> strains originating from Italy (ITA) and Serbia (SRB), with a primary focus on their ability to modulate the antioxidant defense and biochemical responses of <i>Pisum sativum</i> L. seedlings under optimal and drought conditions. The PSH fractions were structurally characterized by complementary spectroscopic and microscopic approaches, revealing strain- and drying-dependent differences in their structural features. The characterized PSHs were subsequently applied as seed biopriming agents, and pea seedlings were grown under two conditions: optimal growth and drought stress. Their effects were evaluated by analyzing enzymatic and non-enzymatic antioxidant responses, together with selected physiological and biochemical traits. Among the tested treatments, exo-PSHs differentially modulated antioxidant enzymes, with SRB primarily enhancing peroxidase and glutathione peroxidase and ITA increasing ascorbate peroxidase and catalase activity. SRB PSHs, particularly exo-PSH, showed the most pronounced effects on antioxidant-related responses, enhancing ABTS scavenging activity and altering DPPH capacity by approximately 35% compared with the control. In addition, endo-PSH from the ITA strain increased chlorophyll content by 26.12% and proline levels by 1.5-fold, indicating a distinct strain-dependent effect on plant physiological responses, particularly under stress conditions. LC-MS/MS profiling of plant MeOH extracts revealed a diverse range of secondary metabolites, including phenolic compounds, e.g., liquiritigenin, ferulic, and protocatechuic acids, which may contribute to the observed antioxidant responses. Multivariate analysis further supported clear biochemical differentiation among PSH treatments and growth conditions, confirming that the responses were dependent on both PSH origin and environmental conditions. Overall, these findings demonstrate that structurally distinct <i>S. commune</i> PSHs can differentially modulate antioxidant defense and key biochemical traits in pea seedlings, supporting their potential as sustainable fungus-derived biostimulants for enhancing plant resilience under both optimal and drought conditions.</p>","PeriodicalId":7984,"journal":{"name":"Antioxidants","volume":"15 9","pages":""},"PeriodicalIF":8.2,"publicationDate":"2026-09-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13603578/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149057129","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Phytochemicals and Irisin as Multi-Target Regulators of Adipose Tissue Browning and Metabolic Reprogramming: Synergies with GLP-1 Pathways.","authors":"Nuriye Nuray Ulusu","doi":"10.3390/antiox15091143","DOIUrl":"10.3390/antiox15091143","url":null,"abstract":"<p><p><b>Background:</b> Obesity is a multifaceted metabolic disorder characterized by systemic disturbances, particularly impaired energy homeostasis, chronic low-grade inflammation, and mitochondrial dysfunction across the brain, gut, adipose tissue, and liver axes. <b>Objectives:</b> This review aims to examine the metabolic properties and molecular mechanisms of six key phytochemicals (berberine, resveratrol, catechins, capsaicin, thymoquinone, and phycocyanin) and the exercise-induced myokine irisin, and their roles in mitochondrial signaling and metabolic reprogramming. <b>Sources of Evidence:</b> A comprehensive literature search was conducted across major electronic databases, including PubMed, Web of Science, and Scopus, to identify relevant mechanistic, in vivo, and in vitro studies. <b>Results:</b> Both the selected phytochemicals and irisin act as multi-target regulators that modulate key signaling pathways, including AMPK, PI3K/Akt/mTOR, SIRT1, Nrf2, and PPARγ. These phytochemicals and irisin can drive cell- and tissue-specific metabolic reprogramming, promoting the browning of white adipocytes, suppressing de novo lipogenesis in hepatocytes, and enhancing fatty acid oxidation in skeletal myocytes. This synergistic metabolic reprogramming enhances thermogenesis and increases energy expenditure. <b>Conclusions:</b> Co-targeting redox signaling and metabolic pathways via phytochemicals and irisin offers a powerful strategy against obesity. This integrative framework restores multi-organ homeostasis, laying the groundwork for targeted metabolic therapies.</p>","PeriodicalId":7984,"journal":{"name":"Antioxidants","volume":"15 9","pages":""},"PeriodicalIF":8.2,"publicationDate":"2026-09-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13603248/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149057167","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Membrane Raft Redox Signaling Mediates Trimethylamine N-Oxide-Induced NLRP3 Inflammasome Activation and Endothelial Dysfunction.","authors":"Md Areeful Haque, Mohammad Atiqur Rahman, Inavolu Sriram Sandeep, Sindhura Pasham, Sayantap Datta, Krishna M Boini, Saisudha Koka","doi":"10.3390/antiox15091138","DOIUrl":"10.3390/antiox15091138","url":null,"abstract":"<p><p>Trimethylamine-N-oxide (TMAO), a gut microbiota-derived metabolite, is a known risk factor for cardiovascular disease. We previously showed that TMAO induces NLRP3 inflammasome activation and contributes to endothelial dysfunction. However, the upstream mechanisms linking TMAO to inflammasome activation and barrier injury remain unclear. In the present study, we examined whether membrane raft (MR) redox signaling contributes to TMAO-induced NLRP3 inflammasome activation and endothelial dysfunction. MR clustering, colocalization of MRs with NADPH oxidase subunits, inflammasome formation, and junction protein expression were assessed by Western blot analysis. RT-qPCR was performed to further assess the mRNA expression of junctional genes. Superoxide production was measured by electron spin resonance (ESR), caspase-1 activity was determined using a biochemical assay kit, IL-1β production was measured by ELISA, and endothelial permeability was evaluated using an FITC-dextran assay. TMAO increased MR clustering in endothelial cells in a dose-dependent manner. TMAO also enhanced the colocalization of MRs with p47phox and gp91phox, indicating the formation of an MR-associated redox signaling axis. In addition, TMAO increased superoxide production; promoted NLRP3 inflammasome formation; elevated caspase-1 activity and IL-1β production; reduced the expression of ZO-2, ZO-1, VE cadherin and occludin; and increased endothelial permeability. Pretreatment with the MR disruptor MCD, the NADPH oxidase inhibitor DPI, or the caspase-1 inhibitor WEHD significantly attenuated these TMAO-induced effects. These findings demonstrate that TMAO-mediated endothelial injury is dependent on the MR-associated redox signaling axis. TMAO promotes MR-associated redox signaling, leading to NADPH oxidase activation, superoxide generation, NLRP3 inflammasome activation, disruption of endothelial junction proteins, and barrier dysfunction. Targeting MR-associated signaling pathways may offer a novel therapeutic strategy to mitigate TMAO-induced vascular inflammation and endothelial dysfunction.</p>","PeriodicalId":7984,"journal":{"name":"Antioxidants","volume":"15 9","pages":""},"PeriodicalIF":8.2,"publicationDate":"2026-09-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13603778/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149057234","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"<i>Allium ursinum</i> L. as a Source of Natural Antioxidants: Phytochemical Diversity, Biological Effects, and Functional Food Applications.","authors":"Cristina Adriana Rosan, George Alin Opris, Alexandra Cristina Tocai Moțoc, Daniela Gitea, Ruben Budău, Manuel Alexandru Gitea, Simona Ioana Vicas","doi":"10.3390/antiox15091144","DOIUrl":"10.3390/antiox15091144","url":null,"abstract":"<p><p><i>Allium ursinum</i> L. (wild garlic) is a promising source of bioactive compounds for functional foods, nutraceuticals, and clean-label products. This review integrates current evidence on its phytochemical composition, biological activities, and food applications. The species contains sulfur compounds, polyphenols, vitamins, minerals, and pigments, whose levels vary with plant organ, developmental stage, environmental conditions, and processing. These constituents are associated mainly with antioxidant, antimicrobial, cardioprotective, and cytoprotective effects; however, evidence is derived predominantly from in vitro and animal studies, with limited clinical validation. In food systems, <i>A. ursinum</i> may enhance nutritional value, oxidative stability, sensory properties, and shelf life. Extraction, encapsulation, and stabilization technologies may support its use as a natural alternative to synthetic additives. Nevertheless, compositional variability, processing stability, bioavailability, authenticity, quality control, and raw-material supply remain major barriers to standardization and industrial application. Further research should combine phytochemical characterization with technological, safety, clinical, and sustainability assessments to enable reliable use of <i>A. ursinum</i> in food and nutraceutical products.</p>","PeriodicalId":7984,"journal":{"name":"Antioxidants","volume":"15 9","pages":""},"PeriodicalIF":8.2,"publicationDate":"2026-09-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13603114/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149057060","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"From Retina to Vasculature: Oxidative Stress as a Common Mechanistic Link Between Age-Related Macular Degeneration and Cardiovascular Disease.","authors":"Jan Krekora, Jarosław Drożdż, Janusz Blasiak, Kai Kaarniranta","doi":"10.3390/antiox15091140","DOIUrl":"10.3390/antiox15091140","url":null,"abstract":"<p><p>Increasing epidemiological and experimental evidence suggests that age-related macular degeneration (AMD) and cardiovascular disease (CVD) share multiple pathogenic mechanisms. Among these, oxidative stress has emerged as one of the most plausible links connecting retinal degeneration and cardiovascular pathology. Excessive production of reactive oxygen and nitrogen species, combined with declining antioxidant defenses, contributes to lipid peroxidation, mitochondrial dysfunction, chronic inflammation, complement activation, cellular senescence, and impaired cellular stress responses in both the retina and the vascular system. Notably, drusen (AMD) and atherosclerotic plaques (CVD) share several molecular constituents. Therefore, AMD and CVD may represent tissue-specific manifestations of broader age-related disturbances in redox homeostasis and inflammatory regulation. Nevertheless, the coexistence of AMD and CVD is incomplete, suggesting that genetic susceptibility, tissue-specific responses to oxidative stress, biological aging, and mechanisms of cellular resilience influence disease expression. In this review, we summarize current evidence linking AMD and CVD, examine oxidative stress-driven molecular pathways common to both disorders, discuss emerging biomarkers and therapeutic targets, and highlight important unresolved questions regarding disease heterogeneity and causal relationships. A better understanding of the shared mechanisms underlying AMD and CVD may facilitate the development of integrated preventive strategies, improved risk stratification, and more personalized therapeutic approaches for age-related diseases.</p>","PeriodicalId":7984,"journal":{"name":"Antioxidants","volume":"15 9","pages":""},"PeriodicalIF":8.2,"publicationDate":"2026-09-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13603592/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149057155","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}