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Erythrocyte deformability dependence on band 3 protein in an in-vitro model of hyperfibrinogenemia

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Resumo:Recent evidence has shown that plasma fibrinogen, a major cardiovascular risk factor, interacts with the erythrocyte membrane and acts to influence blood flow via erythrocyte nitric oxide (NO) modulation. In the present in-vitro study, whole blood samples were harvested from healthy subjects and aliquots were incubated in the absence (control aliquots) and presence of fibrinogen at different degrees of band 3 phosphorylation, and the erythrocyte deformability was determined. The present study shows that in the presence of higher fibrinogen concentrations, similar to those found in inflammatory conditions, erythrocyte deformability is increased only when band 3 is dephosphorylated by the presence of syk inhibitor and at low shear stress. On the contrary, no changes were verified in the presence of fibrinogen when band 3 is allowed to be phosphorylated by inhibiting the phosphotyrosine phosphatase enzyme activity with calpeptin. We also observed that the presence of fibrinogen at higher concentration does not induce changes in erythrocyte deformability in the absence of modulators of the band 3 phosphorylation degree. However, the mechanisms by which fibrinogen signalling modulates erythrocyte function remain to be clarified and are currently under study.
Autores principais:Almeida, J. P. Lopes de
Outros Autores:Freitas-Santos, T.; Saldanha, C.
Assunto:Band 3 protein Erythrocyte Deformability Fibrinogen
Ano:2012
País:Portugal
Tipo de documento:artigo
Tipo de acesso:acesso restrito
Instituição associada:Universidade de Lisboa
Idioma:inglês
Origem:Repositório da Universidade de Lisboa
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author Almeida, J. P. Lopes de
author2 Freitas-Santos, T.
Saldanha, C.
author2_role author
author
author_facet Almeida, J. P. Lopes de
Freitas-Santos, T.
Saldanha, C.
author_role author
contributor_name_str_mv Repositório Científico de Acesso Aberto da ULisboa
country_str PT
creators_json_txt [{\"Person.name\":\"Almeida, J. P. Lopes de\"},{\"Person.name\":\"Freitas-Santos, T.\"},{\"Person.name\":\"Saldanha, C.\"}]
datacite.contributors.contributor.contributorName.fl_str_mv Repositório Científico de Acesso Aberto da ULisboa
datacite.creators.creator.creatorName.fl_str_mv Almeida, J. P. Lopes de
Freitas-Santos, T.
Saldanha, C.
datacite.date.Accepted.fl_str_mv 2012-01-01T00:00:00Z
datacite.date.available.fl_str_mv 2014-03-05T10:54:34Z
datacite.date.embargoed.fl_str_mv 2014-03-05T10:54:34Z
datacite.rights.fl_str_mv http://purl.org/coar/access_right/c_16ec
datacite.subjects.subject.fl_str_mv Band 3 protein
Erythrocyte
Deformability
Fibrinogen
datacite.titles.title.fl_str_mv Erythrocyte deformability dependence on band 3 protein in an in-vitro model of hyperfibrinogenemia
dc.contributor.none.fl_str_mv Repositório Científico de Acesso Aberto da ULisboa
dc.creator.none.fl_str_mv Almeida, J. P. Lopes de
Freitas-Santos, T.
Saldanha, C.
dc.date.Accepted.fl_str_mv 2012-01-01T00:00:00Z
dc.date.available.fl_str_mv 2014-03-05T10:54:34Z
dc.date.embargoed.fl_str_mv 2014-03-05T10:54:34Z
dc.format.none.fl_str_mv application/pdf
dc.identifier.none.fl_str_mv http://dx.doi.org/10.3233/CH-2010-1433
dc.language.none.fl_str_mv eng
dc.publisher.none.fl_str_mv IOS Press
dc.rights.none.fl_str_mv http://purl.org/coar/access_right/c_16ec
dc.subject.none.fl_str_mv Band 3 protein
Erythrocyte
Deformability
Fibrinogen
dc.title.fl_str_mv Erythrocyte deformability dependence on band 3 protein in an in-vitro model of hyperfibrinogenemia
dc.type.none.fl_str_mv http://purl.org/coar/resource_type/c_6501
description Recent evidence has shown that plasma fibrinogen, a major cardiovascular risk factor, interacts with the erythrocyte membrane and acts to influence blood flow via erythrocyte nitric oxide (NO) modulation. In the present in-vitro study, whole blood samples were harvested from healthy subjects and aliquots were incubated in the absence (control aliquots) and presence of fibrinogen at different degrees of band 3 phosphorylation, and the erythrocyte deformability was determined. The present study shows that in the presence of higher fibrinogen concentrations, similar to those found in inflammatory conditions, erythrocyte deformability is increased only when band 3 is dephosphorylated by the presence of syk inhibitor and at low shear stress. On the contrary, no changes were verified in the presence of fibrinogen when band 3 is allowed to be phosphorylated by inhibiting the phosphotyrosine phosphatase enzyme activity with calpeptin. We also observed that the presence of fibrinogen at higher concentration does not induce changes in erythrocyte deformability in the absence of modulators of the band 3 phosphorylation degree. However, the mechanisms by which fibrinogen signalling modulates erythrocyte function remain to be clarified and are currently under study.
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eu_rights_str_mv restrictedAccess
format article
fulltext.url.fl_str_mv https://repositorio.ulisboa.pt/bitstreams/0c0cc022-3b98-4c95-a286-3e789d651239/download
id ul_362bbc6411dedf62a2de8d2bfa28bf09
identifier.doi.fl_str_mv http://dx.doi.org/10.3233/CH-2010-1433
instacron_str ul
institution Universidade de Lisboa
instname_str Universidade de Lisboa
language eng
network_acronym_str ul
network_name_str Repositório da Universidade de Lisboa
oai_identifier_str oai:repositorio.ulisboa.pt:10451/10677
organization_str_mv urn:organizationAcronym:ul
person_str_mv Almeida, J. P. Lopes de
Freitas-Santos, T.
Saldanha, C.
publishDate 2012
publisher.none.fl_str_mv IOS Press
reponame_str Repositório da Universidade de Lisboa
repository_id_str urn:repositoryAcronym:ul
service_str_mv urn:repositoryAcronym:ul
spelling engIOS PressengRecent evidence has shown that plasma fibrinogen, a major cardiovascular risk factor, interacts with the erythrocyte membrane and acts to influence blood flow via erythrocyte nitric oxide (NO) modulation. In the present in-vitro study, whole blood samples were harvested from healthy subjects and aliquots were incubated in the absence (control aliquots) and presence of fibrinogen at different degrees of band 3 phosphorylation, and the erythrocyte deformability was determined. The present study shows that in the presence of higher fibrinogen concentrations, similar to those found in inflammatory conditions, erythrocyte deformability is increased only when band 3 is dephosphorylated by the presence of syk inhibitor and at low shear stress. On the contrary, no changes were verified in the presence of fibrinogen when band 3 is allowed to be phosphorylated by inhibiting the phosphotyrosine phosphatase enzyme activity with calpeptin. We also observed that the presence of fibrinogen at higher concentration does not induce changes in erythrocyte deformability in the absence of modulators of the band 3 phosphorylation degree. However, the mechanisms by which fibrinogen signalling modulates erythrocyte function remain to be clarified and are currently under study.application/pdfengErythrocyte deformability dependence on band 3 protein in an in-vitro model of hyperfibrinogenemiaAlmeida, J. P. Lopes deFreitas-Santos, T.Saldanha, C.HostingInstitutionOrganizationalRepositório Científico de Acesso Aberto da ULisboae-mailmailto:repositorio@reitoria.ulisboa.ptrepositorio@reitoria.ulisboa.ptHandlehttp://hdl.handle.net/10451/10677ISSNIsPartOf1386-02912014-03-05T10:54:34Z20122012-01-01T00:00:00ZDOIhttp://dx.doi.org/10.3233/CH-2010-1433http://purl.org/coar/access_right/c_16ecrestricted accessBand 3 proteinErythrocyteDeformabilityFibrinogen57892 bytesliteraturehttp://purl.org/coar/resource_type/c_6501journal articlehttp://purl.org/coar/access_right/c_16ecapplication/pdffulltexthttps://repositorio.ulisboa.pt/bitstreams/0c0cc022-3b98-4c95-a286-3e789d651239/downloadClinical Hemorheology and Microcirculation50213219
spellingShingle Erythrocyte deformability dependence on band 3 protein in an in-vitro model of hyperfibrinogenemia
Almeida, J. P. Lopes de
Band 3 protein
Erythrocyte
Deformability
Fibrinogen
status SINGLETON
subject.fl_str_mv Band 3 protein
Erythrocyte
Deformability
Fibrinogen
title Erythrocyte deformability dependence on band 3 protein in an in-vitro model of hyperfibrinogenemia
title_full Erythrocyte deformability dependence on band 3 protein in an in-vitro model of hyperfibrinogenemia
title_fullStr Erythrocyte deformability dependence on band 3 protein in an in-vitro model of hyperfibrinogenemia
title_full_unstemmed Erythrocyte deformability dependence on band 3 protein in an in-vitro model of hyperfibrinogenemia
title_short Erythrocyte deformability dependence on band 3 protein in an in-vitro model of hyperfibrinogenemia
title_sort Erythrocyte deformability dependence on band 3 protein in an in-vitro model of hyperfibrinogenemia
topic Band 3 protein
Erythrocyte
Deformability
Fibrinogen
topic_facet Band 3 protein
Erythrocyte
Deformability
Fibrinogen
url http://dx.doi.org/10.3233/CH-2010-1433
visible 1