Peroxiredoxins in erythrocytes: far beyond the antioxidant role

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Autor(es): dc.contributorUniversidade Federal de São Carlos (UFSCar)-
Autor(es): dc.contributorUniversidade Estadual Paulista (UNESP)-
Autor(es): dc.contributorTrês Lagoas-
Autor(es): dc.creatorde Paula, Carla Peres-
Autor(es): dc.creatorde Oliveira da Silva, João Pedro Maia-
Autor(es): dc.creatorRomanello, Karen Simone-
Autor(es): dc.creatorBernardo, Victoria Simões-
Autor(es): dc.creatorTorres, Flaviene Felix-
Autor(es): dc.creatorda Silva, Danilo Grünig Humberto-
Autor(es): dc.creatorda Cunha, Anderson Ferreira-
Data de aceite: dc.date.accessioned2025-08-21T20:33:40Z-
Data de disponibilização: dc.date.available2025-08-21T20:33:40Z-
Data de envio: dc.date.issued2025-04-29-
Data de envio: dc.date.issued2023-10-31-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.1007/s00109-023-02368-7-
Fonte completa do material: dc.identifierhttps://hdl.handle.net/11449/305951-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/305951-
Descrição: dc.descriptionThe red blood cells (RBCs) are essential to transport oxygen (O2) and nutrients throughout the human body. Changes in the structure or functioning of the erythrocytes can lead to several deficiencies, such as hemolytic anemias, in which an increase in reactive oxidative species generation is involved in the pathophysiological process, playing a significant role in the severity of several clinical manifestations. There are important lines of defense against the damage caused by oxidizing molecules. Among the antioxidant molecules, the enzyme peroxiredoxin (Prx) has the higher decomposition power of hydrogen peroxide, especially in RBCs, standing out because of its abundance. This review aimed to present the recent findings that broke some paradigms regarding the three isoforms of Prxs found in RBC (Prx1, Prx2, and Prx6), showing that in addition to their antioxidant activity, these enzymes may have supplementary roles in transducing peroxide signals, as molecular chaperones, protecting from membrane damage, and maintenance of iron homeostasis, thus contributing to the overall survival of human RBCs, roles that seen to be disrupted in hemolytic anemia conditions.-
Descrição: dc.descriptionCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)-
Descrição: dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)-
Descrição: dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)-
Descrição: dc.descriptionGenetics and Evolution Department Biological and Health Sciences Center Federal University of São Carlos-
Descrição: dc.descriptionBiotechnology Graduate Program Exact and Technology Sciences Center Federal University of São Carlos-
Descrição: dc.descriptionEvolutionary Genetics and Molecular Biology Graduate Program Biological and Health Sciences Center Federal University of São Carlos-
Descrição: dc.descriptionDepartment of Biology Paulista State University-
Descrição: dc.descriptionFederal University of Mato Grosso do Sul Campus de Três Lagoas Três Lagoas-
Descrição: dc.descriptionDepartment of Biology Paulista State University-
Descrição: dc.descriptionFAPESP: 2011/50358-3-
Formato: dc.format1335-1353-
Idioma: dc.languageen-
Relação: dc.relationJournal of Molecular Medicine-
???dc.source???: dc.sourceScopus-
Palavras-chave: dc.subjectHemolytic anemias-
Palavras-chave: dc.subjectOxidative stress-
Palavras-chave: dc.subjectRed blood cells-
Palavras-chave: dc.subjectRedox biology-
Título: dc.titlePeroxiredoxins in erythrocytes: far beyond the antioxidant role-
Tipo de arquivo: dc.typevídeo-
Aparece nas coleções:Repositório Institucional - Unesp

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