Membrane association of peroxiredoxin-2 in red cells is mediated by the N-terminal cytoplasmic domain of band 3
Open accessAbstract
Band 3 (B3), the anion transporter, is an integral membrane protein that plays a key structural role by anchoring the plasma membrane to the spectrin-based membrane skeleton in the red cell. In addition, it also plays a critical role in the assembly of glycolytic enzymes to regulate red cell metabolism. However, its ability to recruit proteins that can prevent membrane oxidation has not been previously explored. In this study, using a variety of experimental approaches including cross-linking studies, fluorescence and dichroic measurements, surface plasmon resonance analysis, and proteolytic digestion assays, we document that the antioxidant protein peroxiredoxin-2 (PRDX2), the third most abundant cytoplasmic protein in RBCs, interacts with the cytoplasmic domain of B3. The surface electrostatic potential analysis and stoichiometry measurements revealed that the N-terminal peptide of B3 is involved in the interaction. PRDX2 underwent a conformational change upon its binding to B3 without losing its peroxidase activity. Hemichrome formation induced by phenylhydrazine of RBCs prevented membrane association of PRDX2, implying overlapping binding sites. Documentation of the absence of binding of PRDX2 to B3 Neapolis red cell membranes, in which the initial N-terminal 11 amino acids are deleted, enabled us to conclude that PRDX2 binds to the N-terminal cytoplasmic domain of B3 and that the first 11 amino acids of this domain are crucial for PRDX2 membrane association in intact RBCs. These findings imply yet another important role for B3 in regulating red cell membrane function.
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The association of Prx2 with the membrane makes it important for protection of RBC membrane constituents against lipid peroxidation.
“The association of Prx2 (which participates in reduction of organic peroxides, Eq. 13) with the membrane (120) makes it important for protection of RBC membrane constituents against lipid peroxidation.”
From Red Blood Cell Function and Dysfunction: Redox Regulation, Nitric Oxide Metabolism, Anemia (2017) · cites this paper as [120]
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“Noteworthy, the amount of Prx2 bound to the membrane was reduced in Fyn-/- mouse red cells, in agreement with our previous reports showing competition between Prx2 and hemichromes for band 3, their docking site [21,32,33].”
ResultSelf-citationBolotta, A., Battistelli, M., Falcieri, E., Ghezzo, A., Manara, M. C., Manfredini, S., Marini, M., Posar, A., Visconti, P., & Abruzzo, P. M. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/6430601 · Cited by 24 · see citing works
“However, in the presence of oxidative stress, the antioxidant enzyme peroxiredoxin-2 (Prx2) progressively migrates to the RBC plasma membrane, where it associates with the amino domain of band 3 [26, 27].”
BackgroundThe Reactive Species Interactome in Red Blood Cells: Oxidants, Antioxidants, and Molecular Targets
Cortese-Krott, M. M. (2023) · Antioxidants · doi:10.3390/antiox12091736 · Cited by 25 · see citing works
Sun, K., D’Alessandro, A., & Xia, Y. (2017) · Europe PMC (PubMed Central) · doi:10.2450/2017.0366-16 · Cited by 23 · see citing works
Remigante, A., Spinelli, S., Patanè, G. T., Barreca, D., Straface, E., Gambardella, L., Bozzuto, G., Caruso, D., Falliti, G., Dossena, S., et al. (2023) · Frontiers in Physiology · doi:10.3389/fphys.2023.1303815 · Cited by 23 · see citing works
Zhou, Y., Wang, Y., Su, J., Wu, Z., Wang, C., Zhong, W., Liu, X., Cui, L., Zhou, X., Ma, Y., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.18741 · Cited by 23 · see citing works
Rjeibi, I., Ncib, S., Saad, A. B., & Souid, S. (2017) · Lipids in Health and Disease · doi:10.1186/s12944-017-0596-1 · Cited by 21 · see citing works
“The excess of ROS can generate oxidative stress conditions that could damage the erythrocyte membrane lipids and proteins and possibly lead to hemolysis [36].”
BackgroundMattè, A., & Franceschi, L. D. (2019) · Current Opinion in Hematology · doi:10.1097/moh.0000000000000495 · Cited by 21 · see citing works
Cortese-Krott, M. M. (2020) · Antioxidants and Redox Signaling · doi:10.1089/ars.2020.8171 · Cited by 20 · see citing works
“Prx2 is the third most abundant protein in RBCs (after Hb and glycophorin A), is localized to the membrane of RBCs, and mainly participates in the reduction of organic peroxides (90); therefore, Prx2 protects the RBC membrane against lipid peroxidation.”
Global transformation of erythrocyte properties via engagement of an SH2-like sequence in band 3
Puchulu‐Campanella, E., Turrini, F. M., Li, Y., & Low, P. S. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1611904113 · Cited by 19 · see citing works
Self-citationRocha, S., Rocha‐Pereira, P., Cleto, E., Ferreira, F., Belo, L., & Santos‐Silva, A. (2019) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2019.183172 · Cited by 18 · see citing works
Flatt, J. F., Stevens-Hernandez, C. J., Cogan, N. M., Eggleston, D. J., Haines, N. M., Heesom, K., Picard, V., Thomas, C., & Bruce, L. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.00357 · Cited by 16 · see citing works
Nemkov, T. G., Kingsley, P. D., Dzieciątkowska, M., Malik, J. T., McGrath, K. E., Hansen, K. C., D’Alessandro, A., & Palis, J. (2022) · Blood Advances · doi:10.1182/bloodadvances.2021005975 · Cited by 14 · see citing works
Interplay between Erythrocyte Peroxidases and Membrane
Melo, D., Rocha, S., Coimbra, S., & Santos‐Silva, A. (2019) · IntechOpen eBooks · doi:10.5772/intechopen.83590 · Cited by 14 · see citing works
“This linkage of Prx2 to the membrane appears to be through the N-terminal cytoplasmic domain of band 3, which is also the site of linkage of other cytoplasmic proteins, including metHb [98].”
BackgroundFrey, B. M., Gassner, C., & Jung, H. H. (2015) · Transfusion and Apheresis Science · doi:10.1016/j.transci.2015.04.007 · Cited by 13 · see citing works
“Moreover, the cytoplasmic part of B3 as well as of other attachedmembrane proteins control a variety of metabolic pathways in RBC by binding to aldolases, kinases, oxidases and phosphatases [50–58].”
BackgroundSharapov, M. G., Goncharov, R. G., Filkov, G. I., Trofimenko, A. V., Boyarintsev, V. V., & Novoselov, V. I. (2020) · Antioxidants · doi:10.3390/antiox9080680 · Cited by 13 · see citing works
Melo, D., Ferreira, F., Teles, M. J., Porto, G., Coimbra, S., Rocha, S., & Santos‐Silva, A. (2024) · Antioxidants · doi:10.3390/antiox13060629 · Cited by 12 · see citing works
“As reported elsewhere [43,51], the membrane linkage of both Hb [51] and Prx2 [43], and possibly CAT [45], occurs through the N-terminal cytoplasmic domain of band 3.”
Functional analysis of recombinant 2‐Cys peroxiredoxin from the hard tick H aemaphysalis longicornis
Kusakisako, K., Masatani, T., Miyata, T., Galay, R. L., Maeda, H., Talactac, M. R., Tsuji, N., Mochizuki, M., Fujisaki, K., & Tanaka, T. (2015) · Insect Molecular Biology · doi:10.1111/imb.12193 · Cited by 11 · see citing works
“HsPrx2 is located in the cytosol or cell membrane of VC 2015 The Royal Entomological Society, 25, 16–23 erythrocytes (Matte et al., 2013).”
BackgroundInfluentialAdvances in T-Cell Epitope Engineering
Pentier, J. M., Sewell, A. K., & Miles, J. J. (2013) · Frontiers in Immunology · doi:10.3389/fimmu.2013.00133 · Cited by 11 · see citing works
Federti, E., Mattè, A., Riccardi, V., Peikert, K., Alper, S. L., Danek, A., Walker, R. H., Siciliano, A., Iatcenko, I., Hermann, A., et al. (2021) · Antioxidants · doi:10.3390/antiox11010076 · Cited by 11 · see citing works
Self-citationRjeibi, I., Saad, A. B., Ncib, S., Souid, S., & Alimi, H. (2017) · Journal of Food Biochemistry · doi:10.1111/jfbc.12397 · Cited by 10 · see citing works
Bellik, Y., & Iguer‐Ouada, M. (2015) · Food Chemistry · doi:10.1016/j.foodchem.2015.05.126 · Cited by 10 · see citing works
Data demonstrating the anti-oxidant role of hemopexin in the heart
Ingoglia, G., Sag, C. M., Rex, N., Franceschi, L. D., Vinchi, F., Cimino, J., Petrillo, S., Wagner, S., Kreitmeier, K., Silengo, L., et al. (2017) · Data in Brief · doi:10.1016/j.dib.2017.05.026 · Cited by 10 · see citing works
Tyrosine Phosphorylation Modulates Peroxiredoxin-2 Activity in Normal and Diseased Red Cells
Mattè, A., Federti, E., Tibaldi, E. V., Paolo, M. L. D., Bisello, G., Bertoldi, M., Carpentieri, A., Pucci, P., Iatcenko, I., Wilson, A. B., et al. (2021) · Antioxidants · doi:10.3390/antiox10020206 · Cited by 8 · see citing works
“Enzymatic activity of Prx2 on red cells from wild-type and humanized sickle cell [24,25] mice was assayed, as previously reported [15] in the presence of the coupled assay thioredoxin, thioredoxin reductase, and NADPH.”
BackgroundMethodInfluentialSelf-citationBlood donor exposome and impact of common drugs on red blood cell metabolismPreprint
Nemkov, T. G., Stefanoni, D., Bordbar, A., Issaian, A., Palsson, B. Ø., Dumont, L. J., Hay, A. M., Song, A., Xia, Y., Redzic, J. S., et al. (2020) · medRxiv · doi:10.1101/2020.08.17.20176891 · Cited by 8 · see citing works
Peroxiredoxins in erythrocytes: far beyond the antioxidant role
de Paula, C. P., da Silva, J. P. M. D. O., Romanello, K. S., Bernardo, V. S., Torres, F. F., da Silva, D. G. H., & da Cunha, A. F. (2023) · Journal of Molecular Medicine · doi:10.1007/s00109-023-02368-7 · Cited by 7 · see citing works
“Many authors have identified Prx2 oligomers associated with the erythrocyte membrane [109–112] through binding to band 3 without losing its peroxidase activity [113, 114].”
BackgroundZemlianskykh, N. G., & Babiychuk, L. A. (2019) · BIOPHYSICS · doi:10.1134/s0006350919040237 · Cited by 5 · see citing works
Bernardo, V. S., Torres, F. F., Zucão, A. C. A., Chaves, N. A., Santana, I. L. R., & da Silva, D. G. H. (2025) · Tissue and Cell · doi:10.1016/j.tice.2024.102717 · Cited by 4 · see citing works
Chen, M. Y., Hung, Y.-C., Kuo, W.-N., Hsu, H.-Y., Lee, I., Tsai, C.-Y., Majumdar, A., & Ma, T.-L. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1781288 · Cited by 3 · see citing works
“Altered melatonin secretion patterns may similarly signal compromised antioxidant and immunomodulatory capacity, predisposing periodontal and salivary tissues to in fl ammatory injury (94).”
Phage Display Identified Novel Leydig Cell Homing Peptides for Testicular Targeting
Jirwankar, Y. B., Nair, A., Marathe, S., & Dighe, V. D. (2024) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.3c00330 · Cited by 2 · see citing works
Gwoździński, K., Bujak-Pietrek, S., Pieniążek, A., & Gwoździński, Ł. (2024) · Molecules · doi:10.3390/molecules29122941 · Cited by 2 · see citing works
“A relatively small part of Prx2 is located in the plasma membrane and is associated with the cytoplasmic part of the band 3 protein [55].”
BackgroundMattè, A., Solá, L., Chiari, M., Tomelleri, C., Consonni, R., Turrini, F., & Franceschi, L. D. (2013) · Electrophoresis · doi:10.1002/elps.201300529 · Cited by 2 · see citing works
Self-citationPartial Purification of Peroxiredoxin-2 From Porcine Skeletal Muscle
Johnson, L. G., Steadham, E. M., Huff-Lonergan, E. J., & Lonergan, S. M. (2021) · Meat and Muscle Biology · doi:10.22175/mmb.12408 · Cited by 2 · see citing works
Modulation of Antioxidant Enzyme Expression of In Vitro Culture-Derived Reticulocytes
Langlands, H. D., Shoemark, D. K., & Toye, A. M. (2024) · Antioxidants · doi:10.3390/antiox13091070 · Cited by 2 · see citing works
“For Prx2, perhaps its ability to bind to the N-terminal tail of the highly abundant band 3 membrane protein and/or interactions with haemoglobin may facilitate good reticulocyte retention [33,38].”
BackgroundTranscriptional Analyses of Acute Exposure to Methylmercury on Erythrocytes of Loggerhead Sea Turtle
Hernández-Fernández, J., Velasco, A. M. P., López-Barrera, E. A., Rodríguez-Becerra, P., & Mariño‐Ramírez, L. (2021) · Toxics · doi:10.3390/toxics9040070 · Cited by 2 · see citing works
“It is important to highlight that hemoglobin (Hb) interacts with the carbonic anhydrase-1 protein, the alpha hemoglobin stabilizing protein (AHSP), and Prdx2, with which it forms high-molecular-weight complexes, attenuating the formation of ROS and, in this way, protecting RBCs from oxidative stress [137].”
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“In RBCs, it interacts with the N-terminal peptide of the cytoplasmic domain of the band 3 protein (Matte et al. 2013).”
Backgrounddos Santos, M. C., Breyer, C. A., Schultz, L., Romanello, K. S., da Cunha, A. F., Tairum, C. A., & de Oliveira, M. A. (2017) · InTech eBooks · doi:10.5772/intechopen.70401 · Cited by 1 · see citing works
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Bayer, S. B. (2015) · Otago University Research Archive (University of Otago) · Cited by 1 · see citing works
Adaptation of Erythrocytes: The Role of Hemoglobin, Nitric Oxide, and Methylglyoxal
Kosmachevskaya, O. V., & Topunov, A. F. (2024) · Applied Biochemistry and Microbiology · doi:10.1134/s0003683824605468
Pathophysiology of Beta-Thalassaemia: (Part – 2) [Chronic Anaemia/Hypoxia]
Win, N. (2025) · Myanmar Medical Journal · doi:10.64455/xmma0009
Anion exchangers of the SLC4 gene family
Parker, M. D., & Cordat, E. (2026) · Elsevier eBooks · doi:10.1016/b978-0-12-815389-5.00013-7
A novel Band 3–BLVR axis in red blood cells
Franceschi, L. D., & Iolascon, A. (2026) · Blood · doi:10.1182/blood.2026034780
- Authors
- Matte, A., Bertoldi, M., Mohandas, N., An, X., Bugatti, A., Brunati, A. M., Rusnati, M., Tibaldi, E., Siciliano, A., Turrini, F., Perrotta, S., & De Franceschi, L.
- Affiliations
- University of Verona (IT)
- New York Blood Center (US)
- University of Brescia (IT)
- University of Padua (IT)
- University of Turin (IT)
- University of Campania "Luigi Vanvitelli" (IT)
- Corresponding author
- Bertoldi, Mariarita
- ORCID
- Venue
- Free Radical Biology and Medicine
- Publisher
- Elsevier BV
- Published
- 2013-02
- Volume
- 55
- Pages
- 27-35
- ISSN
- 0891-5849 (ISSN-L)
- OpenAlex
- W2053557848
- Cited by
- 80
- References
- 45
- Citations by year
- 2026: 3 · 2025: 2 · 2024: 5 · 2023: 7 · 2022: 4 · 2021: 8 · 2020: 9 · 2019: 6 · 2018: 4 · 2017: 11 · 2016: 5 · 2015: 7 · 2014: 5 · 2013: 4
- FWCI
- 2.06
- Type
- journal article
- Language
- en
- Open access
- green
- hdl.handle.net
- Licence
- Locations
- Free Radical Biology and Medicine (publishedVersion)
- PubMed (publishedVersion)
- Institutional Research Information System (Università degli Studi di Brescia) (submittedVersion, other-oa)
- Archivio Istituzionale della Ricerca - Università degli Studi della Campania "Luigi Vanvitelli" (submittedVersion)
- Padua Research Archive (University of Padova) (submittedVersion)
- Funders
- University of Verona, to M.B. and L.D.F., PRIN 2008 to L.D.F., and Ministero Istruzione Università e Ricerca, Istituto Superiore di Sanità (AIDS Project) (FUR2010-2011)
- CARIPLO (2008–2198)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Medicine › Physiology › Erythrocyte Function and Pathophysiology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Keywords
- peroxiredoxin 2, band 3, erythrocytes, protein-protein interaction, membrane association, anion transporters, membrane oxidation, antioxidant proteins, hemichrome, phenylhydrazine, protein conformational change
- MeSH terms
- Cytoplasm, Erythrocyte Membrane, Erythrocytes, Humans, Peroxiredoxins
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