Eupalinolide B Alleviates Oxidative Stress in LPS-Induced RAW264.7 Macrophages via Covalently Binding to PRDX4
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Le résumé fourni par la source
Background/Objectives: Eupalinolide B (EB), a natural compound derived from Eupatorium lindleyanum DC, has demonstrated multiple pharmacological activities. However, its role in modulating oxidative stress remains incompletely understood. Methods: In this study, we investigated the antioxidant effect and underlying mechanism of EB in lipopolysaccharide (LPS)-induced RAW264.7 macrophages. Results: EB significantly attenuated LPS-induced oxidative stress as evidenced by reduced levels of intracellular reactive oxygen species (ROS), nitric oxide (NO), and malondialdehyde (MDA) alongside enhanced superoxide dismutase (SOD) activity and an increased reduced/oxidized glutathione (GSH/GSSG) ratio. Using activity-based protein profiling, we identified peroxiredoxin 4 (PRDX4) as a key binding target of EB. Direct interaction was confirmed through labeling and competitive binding assays with purified PRDX4 protein. High-resolution mass spectrometry revealed that EB covalently binds to Cys54 and Cys248 residues of PRDX4. Furthermore, EB treatment upregulated PRDX4 protein expression in LPS-stimulated RAW264.7 cells. siRNA-mediated knockdown of PRDX4 significantly blunted the antioxidant effects of EB, confirming the functional relevance of this target. Conclusions: Our findings demonstrate that EB alleviates LPS-induced oxidative stress in macrophages by covalently binding to and stabilizing PRDX4, thereby enhancing cellular antioxidant capacity. This study unveils a novel mechanism whereby a natural product enhances cellular antioxidant capacity by covalently stabilizing a key peroxidase, highlighting the potential of EB as a therapeutic agent and PRDX4 as a promising target for oxidative stress-related diseases.
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Le contrôle bibliographique ouvert
DOI retrouvé dans Crossref DOI retrouvé ; titre concordant.
- Titre Crossref
- Eupalinolide B Alleviates Oxidative Stress in LPS-Induced RAW264.7 Macrophages via Covalently Binding to PRDX4
- Date Crossref
- 11/03/2026
- Éditeur
- MDPI AG
- Type
- journal-article
Ce recoupement confirme des métadonnées liées au DOI. Il ne confirme ni la méthode ni les conclusions de l’étude, et il ne compte pas comme une seconde source scientifique indépendante.
Où se fait cette recherche
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National Clinical Research pays non établi dans la noticeStructure de recherche
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Tsinghua University Department of Mechanical Engineering pays non établi dans la noticeUniversité ou école supérieure
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Chinese Academy of Medical Sciences & Peking Union Medical College pays non établi dans la noticeUniversité ou école supérieure
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China Academy of Chinese Medical Sciences pays non établi dans la noticeUniversité ou école supérieure
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Peking University School and Hospital of Stomatology Department of Periodontology pays non établi dans la noticeUniversité ou école supérieure
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State Key Laboratory for Quality Ensurance and Sustainable Use of Dao-Di Herbs pays non établi dans la noticeStructure de recherche
National Clinical Research, Department of Mechanical Engineering — Tsinghua University et Chinese Academy of Medical Sciences & Peking Union Medical College, avec 3 autres affiliations.
Une affiliation ne permet pas de déduire la nationalité d’un auteur.