دورية أكاديمية
أعرض في EDS

Catalase, Glutathione Peroxidase, and Peroxiredoxin 2 in Erythrocyte Cytosol and Membrane in Hereditary Spherocytosis, Sickle Cell Disease, and β-Thalassemia.

التفاصيل البيبلوغرافية
العنوان: Catalase, Glutathione Peroxidase, and Peroxiredoxin 2 in Erythrocyte Cytosol and Membrane in Hereditary Spherocytosis, Sickle Cell Disease, and β-Thalassemia.
المؤلفون: Melo D; UCIBIO-Applied Molecular Biosciences Unit, Laboratory of Biochemistry, Department of Biological Sciences, Faculty of Pharmacy, University of Porto, 4051-401 Porto, Portugal.; Associate Laboratory i4HB, Institute for Health and Bioeconomy, Faculty of Pharmacy, University of Porto, 4051-401 Porto, Portugal., Ferreira F; Hematology Service, Centro Hospitalar e Universitário de São João, 4200-319 Porto, Portugal., Teles MJ; Laboratory Hematology Service, Santo António Hospital, Centro Hospitalar do Porto, 4099-001 Porto, Portugal.; Imuno-Hemotherapy Service, Santo António Hospital, Centro Hospitalar do Porto, 4099-001 Porto, Portugal., Porto G; Imuno-Hemotherapy Service, Santo António Hospital, Centro Hospitalar do Porto, 4099-001 Porto, Portugal.; Center for Predictive and Preventive Genetics (CGPP), Institute for Molecular and Cellular Biology (CGPP/IBMC), 4200-135 Porto, Portugal.; Abel Salazar Institute of Biomedical Sciences (ICBAS), University of Porto, 4050-313 Porto, Portugal., Coimbra S; UCIBIO-Applied Molecular Biosciences Unit, Laboratory of Biochemistry, Department of Biological Sciences, Faculty of Pharmacy, University of Porto, 4051-401 Porto, Portugal.; Associate Laboratory i4HB, Institute for Health and Bioeconomy, Faculty of Pharmacy, University of Porto, 4051-401 Porto, Portugal.; 1H-TOXRUN-One Health Toxicology Research Unit, University Institute of Health Sciences, CESPU, CRL, 4585-116 Gandra, Portugal., Rocha S; UCIBIO-Applied Molecular Biosciences Unit, Laboratory of Biochemistry, Department of Biological Sciences, Faculty of Pharmacy, University of Porto, 4051-401 Porto, Portugal.; Associate Laboratory i4HB, Institute for Health and Bioeconomy, Faculty of Pharmacy, University of Porto, 4051-401 Porto, Portugal., Santos-Silva A; UCIBIO-Applied Molecular Biosciences Unit, Laboratory of Biochemistry, Department of Biological Sciences, Faculty of Pharmacy, University of Porto, 4051-401 Porto, Portugal.; Associate Laboratory i4HB, Institute for Health and Bioeconomy, Faculty of Pharmacy, University of Porto, 4051-401 Porto, Portugal.
المصدر: Antioxidants (Basel, Switzerland) [Antioxidants (Basel)] 2024 May 22; Vol. 13 (6). Date of Electronic Publication: 2024 May 22.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: MDPI AG Country of Publication: Switzerland NLM ID: 101668981 Publication Model: Electronic Cited Medium: Print ISSN: 2076-3921 (Print) Linking ISSN: 20763921 NLM ISO Abbreviation: Antioxidants (Basel) Subsets: PubMed not MEDLINE
أسماء مطبوعة: Original Publication: Basel, Switzerland : MDPI AG, [2012]-
مستخلص: Catalase (CAT), glutathione peroxidase (GPx), and peroxiredoxin 2 (Prx2) can counteract the deleterious effects of oxidative stress (OS). Their binding to the red blood cell (RBC) membrane has been reported in non-immune hemolytic anemias (NIHAs). Our aim was to evaluate the relationships between CAT, GPx, and Prx2, focusing on their role at the RBC membrane, in hereditary spherocytosis (HS), sickle cell disease (SCD), β-thalassemia (β-thal), and healthy individuals. The studies were performed in plasma and in the RBC cytosol and membrane, evaluating OS biomarkers and the enzymatic activities and/or the amounts of CAT, GPx, and Prx2. The binding of the enzymes to the membrane appears to be the primary protective mechanism against oxidative membrane injuries in healthy RBCs. In HS (unsplenectomized) and β-thal, translocation from the cytosol to the membrane of CAT and Prx2, respectively, was observed, probably to counteract lipid peroxidation. RBCs from splenectomized HS patients showed the highest membrane-bound hemoglobin, CAT, and GPx amounts in the membrane. SCD patients presented the lowest amount of enzyme linkage, possibly due to structural changes induced by sickle hemoglobin. The OS-induced changes and antioxidant response were different between the studied NIHAs and may contribute to the different clinical patterns in these patients.
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معلومات مُعتمدة: UIDP/04378/2020, LA/P/0140/2020 and SFRH/BD/139622/2018 Fundação para a Ciência e Tecnologia
فهرسة مساهمة: Keywords: catalase; glutathione peroxidase; hereditary spherocytosis; oxidative stress; peroxiredoxin 2; sickle cell disease; β-thalassemia
تواريخ الأحداث: Date Created: 20240627 Latest Revision: 20240629
رمز التحديث: 20240629
مُعرف محوري في PubMed: PMC11201268
DOI: 10.3390/antiox13060629
PMID: 38929068
قاعدة البيانات: MEDLINE
الوصف
تدمد:2076-3921
DOI:10.3390/antiox13060629