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  4. Τμήμα Ιατρικής
  5. Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά) - ΙΑΤ
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Please use this identifier to cite or link to this item: https://olympias.lib.uoi.gr/jspui/handle/123456789/20191
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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.accessioned2015-11-24T19:05:25Z-
dc.date.available2015-11-24T19:05:25Z-
dc.identifier.issn0014-2956-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/20191-
dc.rightsDefault Licence-
dc.subjectAdenosine Diphosphate/pharmacologyen
dc.subjectAmino Acid Motifs/geneticsen
dc.subjectAmino Acid Sequenceen
dc.subjectAnimalsen
dc.subjectAntibodies, Monoclonal/metabolismen
dc.subjectBinding Sitesen
dc.subjectBlood Platelets/*chemistry/*metabolismen
dc.subjectDose-Response Relationship, Drugen
dc.subjectDual Specificity Phosphatase 2en
dc.subjectFibrinogen/chemistry/drug effects/metabolismen
dc.subjectFluorescein/chemistryen
dc.subjectHumansen
dc.subjectMiceen
dc.subjectMice, Inbred BALB Cen
dc.subjectMolecular Sequence Dataen
dc.subjectPeptides/chemical synthesis/metabolism/pharmacologyen
dc.subjectPlatelet Activation/drug effects/physiologyen
dc.subjectPlatelet Aggregation/drug effects/*physiologyen
dc.subjectPlatelet Aggregation Inhibitors/pharmacologyen
dc.subjectPlatelet Glycoprotein GPIIb-IIIa Complex/*chemistry/genetics/*metabolismen
dc.subjectProtein Bindingen
dc.subjectProtein Phosphatase 2en
dc.subjectProtein Structure, Tertiaryen
dc.subjectProtein Subunitsen
dc.subjectProtein Tyrosine Phosphatases/drug effects/metabolismen
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.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.secondaryhttp://www.ncbi.nlm.nih.gov/pubmed/12950259-
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=h2lhobck&s=66b32d4716eb292ffb480d52ead08b58379761bb-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικήςel
heal.publicationDate2003-
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). Furthermore, 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.journalNameEur J Biochemen
heal.journalTypepeer-reviewed-
heal.fullTextAvailabilityTRUE-
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