Pub Date : 2026-02-11DOI: 10.1016/j.redox.2026.104052
Edwin Vázquez-Rosa, Min-Kyoo Shin, Kalyani Chaubey, Sarah Barker, Sofia G. Corella, Suwarna Chakraborty, Sunil Jamuna Tripathi, Youngmin Yu, Jiwon Hyung, Himanshu Dashora, Jing Hao, Coral J. Cintrón-Pérez, Zea Bud, Matasha Dhar, Emiko Miller, Yeojung Koh, Kate P. Lindley, Vidya Indrakumar, Rocio Aguila Rodriguez, Kranti A. Mapuskar, Joshua D. Schoenfeld, Hisashi Fujioka, Luke I. Szweda, Brigid M. Wilson, Jennifer S. Yu, Bindu D. Paul, Douglas R. Spitz, Bryan G. Allen, Andrew A. Pieper
{"title":"P7C3-A20 prevents whole brain radiotherapy-induced chronic hippocampal redox imbalance and neuropsychiatric impairment in mice","authors":"Edwin Vázquez-Rosa, Min-Kyoo Shin, Kalyani Chaubey, Sarah Barker, Sofia G. Corella, Suwarna Chakraborty, Sunil Jamuna Tripathi, Youngmin Yu, Jiwon Hyung, Himanshu Dashora, Jing Hao, Coral J. Cintrón-Pérez, Zea Bud, Matasha Dhar, Emiko Miller, Yeojung Koh, Kate P. Lindley, Vidya Indrakumar, Rocio Aguila Rodriguez, Kranti A. Mapuskar, Joshua D. Schoenfeld, Hisashi Fujioka, Luke I. Szweda, Brigid M. Wilson, Jennifer S. Yu, Bindu D. Paul, Douglas R. Spitz, Bryan G. Allen, Andrew A. Pieper","doi":"10.1016/j.redox.2026.104052","DOIUrl":"https://doi.org/10.1016/j.redox.2026.104052","url":null,"abstract":"","PeriodicalId":20998,"journal":{"name":"Redox Biology","volume":"1 1","pages":""},"PeriodicalIF":11.4,"publicationDate":"2026-02-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146152842","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2026-02-11DOI: 10.1016/j.redox.2026.104069
Sarah Jelleschitz, Christopher Kremslehner, Ionela-Mariana Nagelreiter, Michael Mildner, Melanie Salek, Christina Bauer, Alexandra Stiegler, Adrian Sandgren Fors, Michaela Schirato, Christian Freystätter, Agnès Tessier, Francesca Marcato, Gaëlle Gendronneau, Nada Andre, Youcef Ben Khalifa, Zhixu Ni, Maria Fedorova, Olga Oskolkova, Marie-Sophie Narzt, Florian Gruber
{"title":"Modification of the dermal matrix by senescence associated lipids and its functional consequence","authors":"Sarah Jelleschitz, Christopher Kremslehner, Ionela-Mariana Nagelreiter, Michael Mildner, Melanie Salek, Christina Bauer, Alexandra Stiegler, Adrian Sandgren Fors, Michaela Schirato, Christian Freystätter, Agnès Tessier, Francesca Marcato, Gaëlle Gendronneau, Nada Andre, Youcef Ben Khalifa, Zhixu Ni, Maria Fedorova, Olga Oskolkova, Marie-Sophie Narzt, Florian Gruber","doi":"10.1016/j.redox.2026.104069","DOIUrl":"https://doi.org/10.1016/j.redox.2026.104069","url":null,"abstract":"","PeriodicalId":20998,"journal":{"name":"Redox Biology","volume":"46 1","pages":""},"PeriodicalIF":11.4,"publicationDate":"2026-02-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146152827","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2026-02-09DOI: 10.1016/j.redox.2026.104074
Pedro Cisternas, Katterine Salazar, Eder Ramírez, Sebastián Elgueta, Isabelle de Lima, Valentina Muñoz, Francisco Nualart
Oxidative damage in neurodegenerative diseases activates astrocytes and perturbs antioxidant defenses. Vitamin C is the principal antioxidant in the brain. Ascorbic acid (AA, reduced form) is taken up by neurons via the sodium/vitamin C transporter 2 (SVCT2). Astrocytes take up only the oxidized form of vitamin C, dehydroascorbic acid (DHA), through glucose transporters (GLUT). AA is recycled between neurons and astrocytes, preserving antioxidant capacity and maintaining physiological DHA levels. We postulate that AA recycling modulates astrocyte energy and redox metabolism. We therefore examined the effects of AA and DHA accumulation on glycolysis, pentose phosphate pathway (PPP) activity, and glutathione (GSH) concentrations in activated astrocytes. Culture time negatively modulated DHA recycling. At 15 days in vitro (DIV), astrocytes efficiently took up physiological DHA and reduced it to AA, enhancing redox metabolism, stimulating PPP activity, and increasing intracellular GSH. At 30 DIV (cells positive for activation markers), astrocytes took up higher amounts of DHA but reduced it inefficiently; at this time point, the glycolytic rate was unchanged, PPP activity was inhibited, and GSH decreased. In both 15- and 30-DIV astrocytes, DHA stimulated lactate uptake. We propose that 30-DIV astrocytes constitute a cellular model of reactive astrocytes with impaired AA recycling, ultimately altering glycolytic and antioxidant function.
{"title":"ACTIVATED ASTROCYTES INCREASE DEHYDROASCORBIC ACID UPTAKE, CHANGING INTRACELLULAR METABOLISM AND VITAMIN C RECYCLING AND EMULATING NEUROPATHOLOGICAL CONDITIONS","authors":"Pedro Cisternas, Katterine Salazar, Eder Ramírez, Sebastián Elgueta, Isabelle de Lima, Valentina Muñoz, Francisco Nualart","doi":"10.1016/j.redox.2026.104074","DOIUrl":"https://doi.org/10.1016/j.redox.2026.104074","url":null,"abstract":"Oxidative damage in neurodegenerative diseases activates astrocytes and perturbs antioxidant defenses. Vitamin C is the principal antioxidant in the brain. Ascorbic acid (AA, reduced form) is taken up by neurons via the sodium/vitamin C transporter 2 (SVCT2). Astrocytes take up only the oxidized form of vitamin C, dehydroascorbic acid (DHA), through glucose transporters (GLUT). AA is recycled between neurons and astrocytes, preserving antioxidant capacity and maintaining physiological DHA levels. We postulate that AA recycling modulates astrocyte energy and redox metabolism. We therefore examined the effects of AA and DHA accumulation on glycolysis, pentose phosphate pathway (PPP) activity, and glutathione (GSH) concentrations in activated astrocytes. Culture time negatively modulated DHA recycling. At 15 days in vitro (DIV), astrocytes efficiently took up physiological DHA and reduced it to AA, enhancing redox metabolism, stimulating PPP activity, and increasing intracellular GSH. At 30 DIV (cells positive for activation markers), astrocytes took up higher amounts of DHA but reduced it inefficiently; at this time point, the glycolytic rate was unchanged, PPP activity was inhibited, and GSH decreased. In both 15- and 30-DIV astrocytes, DHA stimulated lactate uptake. We propose that 30-DIV astrocytes constitute a cellular model of reactive astrocytes with impaired AA recycling, ultimately altering glycolytic and antioxidant function.","PeriodicalId":20998,"journal":{"name":"Redox Biology","volume":"1 1","pages":""},"PeriodicalIF":11.4,"publicationDate":"2026-02-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146146718","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2026-02-07DOI: 10.1016/j.redox.2026.104076
Anthony W. DeMartino, David Mahan, Brendan S. Gladwin, Jacob E. Correnti, Qinzi Xu, Deborah J. Rodriguez, Ruya Liu, Elizabeth R. Rochon, Jason J. Rose, Daniel B. Kim-Shapiro, Mark T. Gladwin
{"title":"Sensitive and specific methodology for detection of labile NO-ferroheme complexes in vitro and in blood","authors":"Anthony W. DeMartino, David Mahan, Brendan S. Gladwin, Jacob E. Correnti, Qinzi Xu, Deborah J. Rodriguez, Ruya Liu, Elizabeth R. Rochon, Jason J. Rose, Daniel B. Kim-Shapiro, Mark T. Gladwin","doi":"10.1016/j.redox.2026.104076","DOIUrl":"https://doi.org/10.1016/j.redox.2026.104076","url":null,"abstract":"","PeriodicalId":20998,"journal":{"name":"Redox Biology","volume":"9 1","pages":""},"PeriodicalIF":11.4,"publicationDate":"2026-02-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146134394","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2026-02-04DOI: 10.1016/j.redox.2026.104070
Si-Won Park, Chang-Yong Choi, In-Byung Park, Seok-Jin Kang, Hyeon Jeong Lee, Ji-In Kim, Joonbeom Bae, Dongho Geum, Yong-Pil Cheon, Taehoon Chun
Deciphering the mechanism governing the temporal switch from fetal to adult hemoglobin during erythropoiesis has significant clinical relevance. Here, we identify LDB1 as a pivotal regulator of β-globin switching in erythroid progenitors. The absence of LDB1 in proerythroblasts from mouse fetal liver leads to cell cycle arrest and apoptosis due to the accumulation of reactive oxygen species (ROS), resulting from excessive heme content caused by significant overexpression of embryonic β-globin genes such as Hbb-y and Hbb-bh1. Mechanistically, LDB1 directly enhances the mRNA expression of fetal globin gene repressors, including Bcl11a, Cbfa2t3, and Sox6. Moreover, the LDB1 complex, which includes LMO2 and GATA1, binds directly to enhancer regions of Bcl11a, promoting its transcription. CRISPR/Cas9-mediated LDB1 knockout in human erythroleukemia cells confirmed LDB1 as a key enhancer of BCL11A transcription, reducing its mRNA expression while upregulating transcription of the fetal globin gene HBG. Following chromatin immunoprecipitation (ChIP) assays revealed LDB1 binding to intron 2 enhancers within the BCL11A locus, reinforcing its indispensable role in BCL11A transcription in humans. Consequently, ectopic expression of BCL11A in LDB1-deficient proerythroblasts promotes their proliferation by rescuing them from ROS-mediated apoptosis. These findings highlight the essential role of LDB1 in fetal globin silencing during erythropoiesis.
{"title":"LDB1 represses fetal hemoglobin expression by enhancing BCL11A transcription.","authors":"Si-Won Park, Chang-Yong Choi, In-Byung Park, Seok-Jin Kang, Hyeon Jeong Lee, Ji-In Kim, Joonbeom Bae, Dongho Geum, Yong-Pil Cheon, Taehoon Chun","doi":"10.1016/j.redox.2026.104070","DOIUrl":"https://doi.org/10.1016/j.redox.2026.104070","url":null,"abstract":"<p><p>Deciphering the mechanism governing the temporal switch from fetal to adult hemoglobin during erythropoiesis has significant clinical relevance. Here, we identify LDB1 as a pivotal regulator of β-globin switching in erythroid progenitors. The absence of LDB1 in proerythroblasts from mouse fetal liver leads to cell cycle arrest and apoptosis due to the accumulation of reactive oxygen species (ROS), resulting from excessive heme content caused by significant overexpression of embryonic β-globin genes such as Hbb-y and Hbb-bh1. Mechanistically, LDB1 directly enhances the mRNA expression of fetal globin gene repressors, including Bcl11a, Cbfa2t3, and Sox6. Moreover, the LDB1 complex, which includes LMO2 and GATA1, binds directly to enhancer regions of Bcl11a, promoting its transcription. CRISPR/Cas9-mediated LDB1 knockout in human erythroleukemia cells confirmed LDB1 as a key enhancer of BCL11A transcription, reducing its mRNA expression while upregulating transcription of the fetal globin gene HBG. Following chromatin immunoprecipitation (ChIP) assays revealed LDB1 binding to intron 2 enhancers within the BCL11A locus, reinforcing its indispensable role in BCL11A transcription in humans. Consequently, ectopic expression of BCL11A in LDB1-deficient proerythroblasts promotes their proliferation by rescuing them from ROS-mediated apoptosis. These findings highlight the essential role of LDB1 in fetal globin silencing during erythropoiesis.</p>","PeriodicalId":20998,"journal":{"name":"Redox Biology","volume":"91 ","pages":"104070"},"PeriodicalIF":11.9,"publicationDate":"2026-02-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146132489","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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