Aspectos estruturais da membrana eritrocitária
Autor(a) principal: | |
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Data de Publicação: | 2007 |
Outros Autores: | |
Tipo de documento: | Artigo |
Idioma: | por |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://dx.doi.org/10.1590/S1516-84842007000200016 http://hdl.handle.net/11449/69605 |
Resumo: | This article describes the structures and functions of the erythrocyte membrane and its importance in transfusional medicine. The erythrocyte membrane is one of the best known membranes in terms of structure, function and genetic disorders. As any other plasma membrane, it mediates transport functions. It also provides the erythrocytes with their resilience and deformability. According to the International Society of Blood Transfusion (ISBT), more than 500 antigens are expressed in the erythrocyte membrane, and around 270 are involved in transfusion reaction cases and hemolytic diseases of the fetus and newborn. In the ISBT classification, the high frequency series is represented by antigens in more than 99% of population (high prevalence antigen). In transfusion, the absence of these antigens determines severe problems as for example, one woman without the P antigen suffered 6 repetitive miscarriages due to placental insufficiency, which was caused by an antibody formed against the absent P antigen. Some important erythrocyte membrane proteins are described here including Band 3, Glycophorins and spectrin. The most abundant integral membrane protein is Band 3 and its main function is to mediate exchange of chloride and bicarbonate anions across the plasma membrane. The second most abundant integral membrane protein in the human erythrocyte is sialoglycoprotein glycophorin A (GPA). With its high sialic acid content, GPA is the main contributor to the net negative cell-surface charge and is thus critical for minimizing cell-cell interactions and preventing red cell aggregation. Glycophorin C (GPC) is the receptor for PfEBP-2 (baebl, EBA-140), the newly identified erythrocyte binding ligand of Plasmodium falciparum. The ternary complex of spectrin, actin and 4.1R defines the nodes of the erythrocyte membrane skeletal network, and is inseparable from membrane stability when under mechanical stress. This erythrocyte membrane review is important for a better understanding of transfusion reactions, where the antibody formation against high prevalence antigens makes compatible transfusions difficult. The study of antigen diversity and biochemical characterization of different proteins will contribute to healthcare, as well as diagnosis, development of technology such as monoclonal antibody production and the therapeutic conduct of many diseases. |
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Aspectos estruturais da membrana eritrocitáriaStructural aspects of the erythrocyte membraneAntigensErythrocyte membraneGlycophorinsProteinsThis article describes the structures and functions of the erythrocyte membrane and its importance in transfusional medicine. The erythrocyte membrane is one of the best known membranes in terms of structure, function and genetic disorders. As any other plasma membrane, it mediates transport functions. It also provides the erythrocytes with their resilience and deformability. According to the International Society of Blood Transfusion (ISBT), more than 500 antigens are expressed in the erythrocyte membrane, and around 270 are involved in transfusion reaction cases and hemolytic diseases of the fetus and newborn. In the ISBT classification, the high frequency series is represented by antigens in more than 99% of population (high prevalence antigen). In transfusion, the absence of these antigens determines severe problems as for example, one woman without the P antigen suffered 6 repetitive miscarriages due to placental insufficiency, which was caused by an antibody formed against the absent P antigen. Some important erythrocyte membrane proteins are described here including Band 3, Glycophorins and spectrin. The most abundant integral membrane protein is Band 3 and its main function is to mediate exchange of chloride and bicarbonate anions across the plasma membrane. The second most abundant integral membrane protein in the human erythrocyte is sialoglycoprotein glycophorin A (GPA). With its high sialic acid content, GPA is the main contributor to the net negative cell-surface charge and is thus critical for minimizing cell-cell interactions and preventing red cell aggregation. Glycophorin C (GPC) is the receptor for PfEBP-2 (baebl, EBA-140), the newly identified erythrocyte binding ligand of Plasmodium falciparum. The ternary complex of spectrin, actin and 4.1R defines the nodes of the erythrocyte membrane skeletal network, and is inseparable from membrane stability when under mechanical stress. This erythrocyte membrane review is important for a better understanding of transfusion reactions, where the antibody formation against high prevalence antigens makes compatible transfusions difficult. The study of antigen diversity and biochemical characterization of different proteins will contribute to healthcare, as well as diagnosis, development of technology such as monoclonal antibody production and the therapeutic conduct of many diseases.Hemocentro Faculdade de Medicina de BotucatuHemocentro de BotucatuUniversidade Pierre et Marie Curie - IV, ParisDepto. de Urologia Fac. de Medicina de Botucatu (Unesp)Hosp. Das Clínicas da Faculdade de Medicina de Botucatu Divisão Hemocentro Lab. de Engenharia Celular, Distrito de Rubião Jr. s/n, 18618-000 - Botucatu-SPHemocentro Faculdade de Medicina de BotucatuDepto. de Urologia Fac. de Medicina de Botucatu (Unesp)Hosp. Das Clínicas da Faculdade de Medicina de Botucatu Divisão Hemocentro Lab. de Engenharia Celular, Distrito de Rubião Jr. s/n, 18618-000 - Botucatu-SPUniversidade Estadual Paulista (Unesp)Hemocentro de BotucatuUniversidade Pierre et Marie Curie - IVMurador, Priscila [UNESP]Deffune, Elenice [UNESP]2014-05-27T11:22:27Z2014-05-27T11:22:27Z2007-04-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article168-178application/pdfhttp://dx.doi.org/10.1590/S1516-84842007000200016Revista Brasileira de Hematologia e Hemoterapia, v. 29, n. 2, p. 168-178, 2007.1516-8484http://hdl.handle.net/11449/6960510.1590/S1516-84842007000200016S1516-848420070002000162-s2.0-373490254822-s2.0-37349025482.pdf9646764071339214Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPporRevista Brasileira de Hematologia e Hemoterapia0,335info:eu-repo/semantics/openAccess2024-09-03T14:29:54Zoai:repositorio.unesp.br:11449/69605Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestrepositoriounesp@unesp.bropendoar:29462024-09-03T14:29:54Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
Aspectos estruturais da membrana eritrocitária Structural aspects of the erythrocyte membrane |
title |
Aspectos estruturais da membrana eritrocitária |
spellingShingle |
Aspectos estruturais da membrana eritrocitária Murador, Priscila [UNESP] Antigens Erythrocyte membrane Glycophorins Proteins |
title_short |
Aspectos estruturais da membrana eritrocitária |
title_full |
Aspectos estruturais da membrana eritrocitária |
title_fullStr |
Aspectos estruturais da membrana eritrocitária |
title_full_unstemmed |
Aspectos estruturais da membrana eritrocitária |
title_sort |
Aspectos estruturais da membrana eritrocitária |
author |
Murador, Priscila [UNESP] |
author_facet |
Murador, Priscila [UNESP] Deffune, Elenice [UNESP] |
author_role |
author |
author2 |
Deffune, Elenice [UNESP] |
author2_role |
author |
dc.contributor.none.fl_str_mv |
Universidade Estadual Paulista (Unesp) Hemocentro de Botucatu Universidade Pierre et Marie Curie - IV |
dc.contributor.author.fl_str_mv |
Murador, Priscila [UNESP] Deffune, Elenice [UNESP] |
dc.subject.por.fl_str_mv |
Antigens Erythrocyte membrane Glycophorins Proteins |
topic |
Antigens Erythrocyte membrane Glycophorins Proteins |
description |
This article describes the structures and functions of the erythrocyte membrane and its importance in transfusional medicine. The erythrocyte membrane is one of the best known membranes in terms of structure, function and genetic disorders. As any other plasma membrane, it mediates transport functions. It also provides the erythrocytes with their resilience and deformability. According to the International Society of Blood Transfusion (ISBT), more than 500 antigens are expressed in the erythrocyte membrane, and around 270 are involved in transfusion reaction cases and hemolytic diseases of the fetus and newborn. In the ISBT classification, the high frequency series is represented by antigens in more than 99% of population (high prevalence antigen). In transfusion, the absence of these antigens determines severe problems as for example, one woman without the P antigen suffered 6 repetitive miscarriages due to placental insufficiency, which was caused by an antibody formed against the absent P antigen. Some important erythrocyte membrane proteins are described here including Band 3, Glycophorins and spectrin. The most abundant integral membrane protein is Band 3 and its main function is to mediate exchange of chloride and bicarbonate anions across the plasma membrane. The second most abundant integral membrane protein in the human erythrocyte is sialoglycoprotein glycophorin A (GPA). With its high sialic acid content, GPA is the main contributor to the net negative cell-surface charge and is thus critical for minimizing cell-cell interactions and preventing red cell aggregation. Glycophorin C (GPC) is the receptor for PfEBP-2 (baebl, EBA-140), the newly identified erythrocyte binding ligand of Plasmodium falciparum. The ternary complex of spectrin, actin and 4.1R defines the nodes of the erythrocyte membrane skeletal network, and is inseparable from membrane stability when under mechanical stress. This erythrocyte membrane review is important for a better understanding of transfusion reactions, where the antibody formation against high prevalence antigens makes compatible transfusions difficult. The study of antigen diversity and biochemical characterization of different proteins will contribute to healthcare, as well as diagnosis, development of technology such as monoclonal antibody production and the therapeutic conduct of many diseases. |
publishDate |
2007 |
dc.date.none.fl_str_mv |
2007-04-01 2014-05-27T11:22:27Z 2014-05-27T11:22:27Z |
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://dx.doi.org/10.1590/S1516-84842007000200016 Revista Brasileira de Hematologia e Hemoterapia, v. 29, n. 2, p. 168-178, 2007. 1516-8484 http://hdl.handle.net/11449/69605 10.1590/S1516-84842007000200016 S1516-84842007000200016 2-s2.0-37349025482 2-s2.0-37349025482.pdf 9646764071339214 |
url |
http://dx.doi.org/10.1590/S1516-84842007000200016 http://hdl.handle.net/11449/69605 |
identifier_str_mv |
Revista Brasileira de Hematologia e Hemoterapia, v. 29, n. 2, p. 168-178, 2007. 1516-8484 10.1590/S1516-84842007000200016 S1516-84842007000200016 2-s2.0-37349025482 2-s2.0-37349025482.pdf 9646764071339214 |
dc.language.iso.fl_str_mv |
por |
language |
por |
dc.relation.none.fl_str_mv |
Revista Brasileira de Hematologia e Hemoterapia 0,335 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
168-178 application/pdf |
dc.source.none.fl_str_mv |
Scopus reponame:Repositório Institucional da UNESP instname:Universidade Estadual Paulista (UNESP) instacron:UNESP |
instname_str |
Universidade Estadual Paulista (UNESP) |
instacron_str |
UNESP |
institution |
UNESP |
reponame_str |
Repositório Institucional da UNESP |
collection |
Repositório Institucional da UNESP |
repository.name.fl_str_mv |
Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP) |
repository.mail.fl_str_mv |
repositoriounesp@unesp.br |
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1810021357327482880 |