Linkage of typically cytosolic peroxidases to erythrocyte membrane - A possible mechanism of protection in Hereditary Spherocytosis

Detalhes bibliográficos
Autor(a) principal: Rocha, Susana
Data de Publicação: 2020
Outros Autores: Rocha-Pereira, Petronila, Cleto, Maria Esmeralda Da Silva, Ferreira, Fátima, Belo, Luís, Santos-Silva, Alice
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10400.16/2488
Resumo: Hereditary Spherocytosis (HS) is a non-immune hemolytic anemia associated to oxidative stress (OS), namely to the linkage of cytosolic antioxidant enzymes to the erythrocyte membrane. Our aims were to evaluate erythrocyte OS changes and the membrane linkage of peroxiredoxin 2 (Prx2), glutathione peroxidase (GPx) and catalase (CAT) in unsplenectomized (unspl) and splenectomized (spl) HS patients and to search for associations with clinical severity (in unspl HS patients). We studied 114 HS patients (74 unspl and 40 spl) and 30 healthy individuals and we evaluated membrane bound hemoglobin (MBH), membrane lipid-peroxidation (LPO), enzymatic activities of GPx and CAT and the amounts of membrane bound Prx2, GPx and CAT, as well as, clinical and analytical parameters for characterization of HS. We found that unspl HS patients showed clear signs of anemia and in spl HS, a correction to this anemia was observed; the latter patients presented higher levels of OS biomarkers, namely, MBH and LPO. CAT was detected in the membrane of all individuals (control and HS groups), while GPx and Prx2 were only present in HS patients; moreover, their linkage to the membrane (in HS) appears to be cumulative since membrane bound peroxidases amount was higher as the number of peroxidases detected increased. MBH increased with the number/amount of membrane bound peroxidases, however LPO levels remained similar. In conclusion, our data suggest that the binding of these typically cytosolic peroxidases to erythrocyte membrane may be part of a mechanism of membrane protection to maintain its integrity by possibly regulating LPO.
id RCAP_ab3ec5f8f7d3bcbff1bb05e02dea5cf5
oai_identifier_str oai:repositorio.chporto.pt:10400.16/2488
network_acronym_str RCAP
network_name_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
repository_id_str 7160
spelling Linkage of typically cytosolic peroxidases to erythrocyte membrane - A possible mechanism of protection in Hereditary SpherocytosisCatalaseGlutathione peroxidaseLipid-peroxidationMembrane oxidative stressMembrane-bound hemoglobinPeroxiredoxin 2Hereditary Spherocytosis (HS) is a non-immune hemolytic anemia associated to oxidative stress (OS), namely to the linkage of cytosolic antioxidant enzymes to the erythrocyte membrane. Our aims were to evaluate erythrocyte OS changes and the membrane linkage of peroxiredoxin 2 (Prx2), glutathione peroxidase (GPx) and catalase (CAT) in unsplenectomized (unspl) and splenectomized (spl) HS patients and to search for associations with clinical severity (in unspl HS patients). We studied 114 HS patients (74 unspl and 40 spl) and 30 healthy individuals and we evaluated membrane bound hemoglobin (MBH), membrane lipid-peroxidation (LPO), enzymatic activities of GPx and CAT and the amounts of membrane bound Prx2, GPx and CAT, as well as, clinical and analytical parameters for characterization of HS. We found that unspl HS patients showed clear signs of anemia and in spl HS, a correction to this anemia was observed; the latter patients presented higher levels of OS biomarkers, namely, MBH and LPO. CAT was detected in the membrane of all individuals (control and HS groups), while GPx and Prx2 were only present in HS patients; moreover, their linkage to the membrane (in HS) appears to be cumulative since membrane bound peroxidases amount was higher as the number of peroxidases detected increased. MBH increased with the number/amount of membrane bound peroxidases, however LPO levels remained similar. In conclusion, our data suggest that the binding of these typically cytosolic peroxidases to erythrocyte membrane may be part of a mechanism of membrane protection to maintain its integrity by possibly regulating LPO.ElsevierRepositório Científico do Centro Hospitalar Universitário de Santo AntónioRocha, SusanaRocha-Pereira, PetronilaCleto, Maria Esmeralda Da SilvaFerreira, FátimaBelo, LuísSantos-Silva, Alice2021-07-06T17:55:50Z20202020-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10400.16/2488engRocha S, Rocha-Pereira P, Cleto E, Ferreira F, Belo L, Santos-Silva A. Linkage of typically cytosolic peroxidases to erythrocyte membrane - A possible mechanism of protection in Hereditary Spherocytosis. Biochim Biophys Acta Biomembr. 2020 Mar 1;1862(3):183172. doi: 10.1016/j.bbamem.2019.183172. Epub 2019 Dec 21. PMID: 31870655.1879-264210.1016/j.bbamem.2019.183172info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2023-10-20T11:00:52Zoai:repositorio.chporto.pt:10400.16/2488Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T20:38:42.097583Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv Linkage of typically cytosolic peroxidases to erythrocyte membrane - A possible mechanism of protection in Hereditary Spherocytosis
title Linkage of typically cytosolic peroxidases to erythrocyte membrane - A possible mechanism of protection in Hereditary Spherocytosis
spellingShingle Linkage of typically cytosolic peroxidases to erythrocyte membrane - A possible mechanism of protection in Hereditary Spherocytosis
Rocha, Susana
Catalase
Glutathione peroxidase
Lipid-peroxidation
Membrane oxidative stress
Membrane-bound hemoglobin
Peroxiredoxin 2
title_short Linkage of typically cytosolic peroxidases to erythrocyte membrane - A possible mechanism of protection in Hereditary Spherocytosis
title_full Linkage of typically cytosolic peroxidases to erythrocyte membrane - A possible mechanism of protection in Hereditary Spherocytosis
title_fullStr Linkage of typically cytosolic peroxidases to erythrocyte membrane - A possible mechanism of protection in Hereditary Spherocytosis
title_full_unstemmed Linkage of typically cytosolic peroxidases to erythrocyte membrane - A possible mechanism of protection in Hereditary Spherocytosis
title_sort Linkage of typically cytosolic peroxidases to erythrocyte membrane - A possible mechanism of protection in Hereditary Spherocytosis
author Rocha, Susana
author_facet Rocha, Susana
Rocha-Pereira, Petronila
Cleto, Maria Esmeralda Da Silva
Ferreira, Fátima
Belo, Luís
Santos-Silva, Alice
author_role author
author2 Rocha-Pereira, Petronila
Cleto, Maria Esmeralda Da Silva
Ferreira, Fátima
Belo, Luís
Santos-Silva, Alice
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv Repositório Científico do Centro Hospitalar Universitário de Santo António
dc.contributor.author.fl_str_mv Rocha, Susana
Rocha-Pereira, Petronila
Cleto, Maria Esmeralda Da Silva
Ferreira, Fátima
Belo, Luís
Santos-Silva, Alice
dc.subject.por.fl_str_mv Catalase
Glutathione peroxidase
Lipid-peroxidation
Membrane oxidative stress
Membrane-bound hemoglobin
Peroxiredoxin 2
topic Catalase
Glutathione peroxidase
Lipid-peroxidation
Membrane oxidative stress
Membrane-bound hemoglobin
Peroxiredoxin 2
description Hereditary Spherocytosis (HS) is a non-immune hemolytic anemia associated to oxidative stress (OS), namely to the linkage of cytosolic antioxidant enzymes to the erythrocyte membrane. Our aims were to evaluate erythrocyte OS changes and the membrane linkage of peroxiredoxin 2 (Prx2), glutathione peroxidase (GPx) and catalase (CAT) in unsplenectomized (unspl) and splenectomized (spl) HS patients and to search for associations with clinical severity (in unspl HS patients). We studied 114 HS patients (74 unspl and 40 spl) and 30 healthy individuals and we evaluated membrane bound hemoglobin (MBH), membrane lipid-peroxidation (LPO), enzymatic activities of GPx and CAT and the amounts of membrane bound Prx2, GPx and CAT, as well as, clinical and analytical parameters for characterization of HS. We found that unspl HS patients showed clear signs of anemia and in spl HS, a correction to this anemia was observed; the latter patients presented higher levels of OS biomarkers, namely, MBH and LPO. CAT was detected in the membrane of all individuals (control and HS groups), while GPx and Prx2 were only present in HS patients; moreover, their linkage to the membrane (in HS) appears to be cumulative since membrane bound peroxidases amount was higher as the number of peroxidases detected increased. MBH increased with the number/amount of membrane bound peroxidases, however LPO levels remained similar. In conclusion, our data suggest that the binding of these typically cytosolic peroxidases to erythrocyte membrane may be part of a mechanism of membrane protection to maintain its integrity by possibly regulating LPO.
publishDate 2020
dc.date.none.fl_str_mv 2020
2020-01-01T00:00:00Z
2021-07-06T17:55:50Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://hdl.handle.net/10400.16/2488
url http://hdl.handle.net/10400.16/2488
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Rocha S, Rocha-Pereira P, Cleto E, Ferreira F, Belo L, Santos-Silva A. Linkage of typically cytosolic peroxidases to erythrocyte membrane - A possible mechanism of protection in Hereditary Spherocytosis. Biochim Biophys Acta Biomembr. 2020 Mar 1;1862(3):183172. doi: 10.1016/j.bbamem.2019.183172. Epub 2019 Dec 21. PMID: 31870655.
1879-2642
10.1016/j.bbamem.2019.183172
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron:RCAAP
instname_str Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron_str RCAAP
institution RCAAP
reponame_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
collection Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
repository.name.fl_str_mv Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
repository.mail.fl_str_mv
_version_ 1799133647697084416