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The 95RGD97 sequence on the Aα chain of fibrinogen is essential for binding to its erythrocyte receptor

2018Journal article Open access
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dc.contributor.authorCarvalho, Filomena Almeida
dc.contributor.authorGuedes, Ana Filipa
dc.contributor.authorDuval, Cedric
dc.contributor.authorMacrae, Fraser L.
dc.contributor.authorSwithenbank, Luke
dc.contributor.authorFarrell, David H.
dc.contributor.authorAriëns, Robert A. S.
dc.contributor.authorSantos, Nuno C.
dc.date.accessioned2019-04-04T15:53:39Z
dc.date.available2019-04-04T15:53:39Z
dc.date.issued2018
dc.description© 2018 Carvalho et al. This work is published and licensed by Dove Medical Press Limited. The full terms of this license are available at https://www.dovepress.com/terms.php and incorporate the Creative Commons Attribution – Non Commercial (unported, v3.0) License (http://creativecommons.org/licenses/by-nc/3.0/). By accessing the work you hereby accept the Terms. Non-commercial uses of the work are permitted without any further permission from Dove Medical Press Limited, provided the work is properly attributed. For permission for commercial use of this work, please see paragraphs 4.2 and 5 of our Terms (https://www.dovepress.com/terms.php).pt_PT
dc.description.abstractBACKGROUND: Erythrocyte aggregation, a cardiovascular risk factor, is increased by high plasma fibrinogen levels. Here, the effect of different fibrinogen mutations on binding to its human erythrocyte receptor was assessed in order to identify the interaction sites. METHODS: Three fibrinogen variants were tested, specifically mutated in their putative integrin recognition sites on the Aα chain (mutants D97E, D574E and D97E/D574E) and compared with wild-type fibrinogen. RESULTS: Atomic force microscopy-based force spectroscopy measurements showed a significant decrease both on the fibrinogen-erythrocyte binding force and on its frequency for fibrinogen with the D97E mutation, indicating that the corresponding arginine-glycine-aspartate sequence (residues 95-97) is involved in this interaction, and supporting that the fibrinogen receptor on erythrocytes has a β3 subunit. Changes in the fibrin clot network structure obtained with the D97E mutant were observed by scanning electron microscopy. CONCLUSION: These findings may lead to innovative perspectives on the development of new therapeutic approaches to overcome the risks of fibrinogen-driven erythrocyte hyperaggregation.pt_PT
dc.description.sponsorshipThe authors thank Teresa Freitas (IMM, FM, UL) for excellent technical assistance. This work was supported by Fundação para a Ciência e a Tecnologia – Ministério da Ciência, Tecnologia e Ensino Superior (FCT-MCTES, Portugal) grants PTDC/QUI-BIQ/119509/2010 and PTDC/BBB-BMD/6307/2014, FEDER, through POR Lisboa 2020 - Programa Operacional Regional de Lisboa, PORTUGAL 2020 and FCT-MCTES (LISBOA-01-0145-FEDER-007391), and by the Calouste Gulbenkian Foundation (Portugal). AFG also acknowledges FCT-MCTES PhD fellowship SFRH/BD/84414/2012.pt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.citationInternational Journal of Nanomedicine 2018:13 1985–1992pt_PT
dc.identifier.doi10.2147/IJN.S154523pt_PT
dc.identifier.issn1176-9114
dc.identifier.urihttp://hdl.handle.net/10451/37854
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherDove Medical Presspt_PT
dc.relationLISBOA-01-0145-FEDER-007391pt_PT
dc.relationMolecular interactions of circulating fibrinogen as a risk factor for cardiovascular and cerebrovascular pathologies
dc.relation.publisherversionhttps://www.dovepress.com/international-journal-of-nanomedicine-journalpt_PT
dc.rights.urihttp://creativecommons.org/licenses/by-nc/4.0/pt_PT
dc.subjectAtomic force microscopypt_PT
dc.subjectFibrinogenpt_PT
dc.subjectFibrin clotpt_PT
dc.subjectErythrocyte aggregationpt_PT
dc.subjectMutant proteinpt_PT
dc.titleThe 95RGD97 sequence on the Aα chain of fibrinogen is essential for binding to its erythrocyte receptorpt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.awardTitleMolecular interactions of circulating fibrinogen as a risk factor for cardiovascular and cerebrovascular pathologies
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/3599-PPCDT/PTDC%2FQUI-BIQ%2F119509%2F2010/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/3599-PPCDT/PTDC%2FBBB-BMD%2F6307%2F2014/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/SFRH/SFRH%2FBD%2F84414%2F2012/PT
oaire.citation.endPage1992pt_PT
oaire.citation.startPage1985pt_PT
oaire.citation.titleInternational Journal of Nanomedicinept_PT
oaire.citation.volume13pt_PT
oaire.fundingStream3599-PPCDT
oaire.fundingStream3599-PPCDT
oaire.fundingStreamSFRH
person.familyNameCarvalho
person.familyNameGuedes
person.familyNameSantos
person.givenNameFilomena
person.givenNameAna Filipa
person.givenNameNuno
person.identifier.ciencia-id4615-4AEC-8D91
person.identifier.ciencia-idCD13-5E3A-A3C5
person.identifier.orcid0000-0001-6088-3894
person.identifier.orcid0000-0001-6768-1718
person.identifier.orcid0000-0002-0580-0475
person.identifier.ridM-9202-2013
person.identifier.ridN-7248-2013
person.identifier.scopus-author-id7103069694
person.identifier.scopus-author-id55940818300
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
rcaap.rightsopenAccesspt_PT
rcaap.typearticlept_PT
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