Mapping the binding domains of the alpha(IIb) subunit - A study performed on the activated form of the platelet integrin alpha(IIb)beta(3)

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dc.contributor.authorBiris, N.en
dc.contributor.authorAbatzis, M.en
dc.contributor.authorMitsios, J. V.en
dc.contributor.authorSakarellos-Daitsiotis, M.en
dc.contributor.authorSakarellos, C.en
dc.contributor.authorTsoukatos, D.en
dc.contributor.authorTselepis, A. D.en
dc.contributor.authorMichalis, L.en
dc.contributor.authorSideris, D.en
dc.contributor.authorKonidou, G.en
dc.contributor.authorSoteriadou, K.en
dc.contributor.authorTsikaris, V.en
dc.date.accessioned2015-11-24T16:41:19Z
dc.date.available2015-11-24T16:41:19Z
dc.identifier.issn0014-2956-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/8403
dc.rightsDefault Licence-
dc.subjectalpha(iib)-binding domainsen
dc.subjectalpha(iib) mappingen
dc.subjectplatelet-aggregation inhibitorsen
dc.subjectalpha(iib)beta(3) receptoren
dc.subjectintegrin inhibitorsen
dc.subjectglycoprotein-iib-iiiaen
dc.subjectfibrinogen receptoren
dc.subjectrecognition siteen
dc.subjectcell-adhesionen
dc.subjectgpiib-iiiaen
dc.subjectglanzmanns-thrombastheniaen
dc.subjectmonoclonal-antibodyen
dc.subjectligand recognitionen
dc.subjectsynthetic peptidesen
dc.subjectrgden
dc.titleMapping the binding domains of the alpha(IIb) subunit - A study performed on the activated form of the platelet integrin alpha(IIb)beta(3)en
heal.abstractalpha(IIb)beta(3), a member of the integrin family of adhesive protein receptors, is the most abundant glycoprotein on platelet plasma-membranes and binds to adhesive proteins via the recognition of short amino acid sequences, for example the ubiquitous RGD motif. However, elucidation of the ligand-binding domains of the receptor remains controversial, mainly owing to the fact that integrins are conformationally labile during purification and storage. In this study, a detailed mapping of the extracellular region of the alpha(IIb) subunit is presented, using overlapping 20-peptides, in order to identify the binding sites of alpha(IIb) potentially involved in the platelet-aggregation event. Regions alpha(IIb) 313-332, alpha(IIb) 265-284 and alpha(IIb) 57-64 of alpha(IIb)beta(3) were identified as putative fibrinogen-binding domains because the corresponding peptides inhibited platelet aggregation and antagonized fibrinogen association, possibly by interacting with this ligand. The latter is further supported by the finding that the above peptides did not interfere with the binding of PAC-1 to the activated form of alpha(IIb)beta(3). Further more, alpha(IIb) 313-332 was found to bind to fibrinogen in a solid-phase binding assay. It should be emphasized that all the experiments in this study were carried out on activated platelets and consequently on the activated form of this integrin receptor. We hypothesize that RAD and RAE adhesive motifs, encompassed in alpha(IIb) 313-332, 265-284 and 57-64, are capable of recognizing complementary domains of fibrinogen, thus inhibiting the binding of this ligand to platelets.en
heal.accesscampus-
heal.fullTextAvailabilityTRUE-
heal.identifier.primaryDOI 10.1046/j.1432-1033.2003.03762.x-
heal.identifier.secondary<Go to ISI>://000186390000011-
heal.identifier.secondaryhttp://onlinelibrary.wiley.com/store/10.1046/j.1432-1033.2003.03762.x/asset/j.1432-1033.2003.03762.x.pdf?v=1&t=h0e0jcr4&s=db56f55ced7ce84a989b4acaaec9984d9183c663-
heal.journalNameEuropean Journal of Biochemistryen
heal.journalTypepeer reviewed-
heal.languageen-
heal.publicationDate2003-
heal.publisherBlackwell Publishingen
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείαςel
heal.typejournalArticle-
heal.type.elΆρθρο Περιοδικούel
heal.type.enJournal articleen

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