Please use this identifier to cite or link to this item: https://olympias.lib.uoi.gr/jspui/handle/123456789/10542
Full metadata record
DC FieldValueLanguage
dc.contributor.authorMitsios, J. V.en
dc.contributor.authorTambaki, A. P.en
dc.contributor.authorAbatzis, M.en
dc.contributor.authorBiris, N.en
dc.contributor.authorSakarellos-Daitsiotis, M.en
dc.contributor.authorSakarellos, C.en
dc.contributor.authorSoteriadou, K.en
dc.contributor.authorGoudevenos, J.en
dc.contributor.authorElisaf, M.en
dc.contributor.authorTsoukatos, D.en
dc.contributor.authorTsikaris, V.en
dc.contributor.authorTselepis, A. D.en
dc.date.accessioned2015-11-24T16:57:09Z-
dc.date.available2015-11-24T16:57:09Z-
dc.identifier.issn0014-2956-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/10542-
dc.rightsDefault Licence-
dc.subjectintegrin inhibitorsen
dc.subjectpeptidesen
dc.subjectplatelet activation inhibitorsen
dc.subjectalpha(iib)beta(3) receptoren
dc.subjectglycoprotein-iib-iiiaen
dc.subjectligand-bindingen
dc.subjectintegrin alpha(iib)beta(3)en
dc.subjectgamma-chainen
dc.subjectreceptoren
dc.subjectsiteen
dc.subjectrecognitionen
dc.subjectsequenceen
dc.subjectdomainen
dc.subjectaggregationen
dc.titleEffect of synthetic peptides corresponding to residues 313-332 of the alpha(IIb) subunit on platelet activation and fibrinogen binding to alpha(IIb)beta(3)en
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.primaryDOI 10.1111/j.1432-1033.2004.03990.x-
heal.identifier.secondary<Go to ISI>://000188819700021-
heal.identifier.secondaryhttp://onlinelibrary.wiley.com/store/10.1111/j.1432-1033.2004.03990.x/asset/j.1432-1033.2004.03990.x.pdf?v=1&t=h0e0nme0&s=fd1b113d3d77b19eaae24654eacb532c1fcd03f2-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείαςel
heal.publicationDate2004-
heal.abstractThe platelet integrin receptor alpha(IIb)beta(3) plays a critical role in thrombosis and haemostasis by mediating interactions between platelets and several ligands but primarily fibrinogen. It has been shown previously that the YMESRADR KLAEVGRVYLFL (313-332) sequence of the alpha(IIb) subunit plays an important role in platelet activation, fibrinogen binding and alpha(IIb)beta(3)-mediated outside-in signalling. Furthermore, we recently showed that the 20-residue peptide (20-mer) alpha(IIb) 313-332, is a potent inhibitor of platelet aggregation and fibrinogen binding to alpha(IIb)beta(3), interacting with fibrinogen rather than the receptor. In an effort to determine the sequence and the minimum length required for the biological activity of the above 20-mer, we synthesized seven octapeptides, each overlapping by six residues, covering the entire sequence and studied their effect on platelet activation as well as fibrinogen binding to activated platelets. We show for the first time that octapeptides containing the RAD sequence are capable of inhibiting platelet aggregation and secretion as well as fibrinogen binding to the activated alpha(IIb)beta(3), possibly interacting with the ligand rather than the receptor. This suggests that the RAD sequence, common to all the inhibitory peptides, is critical for their biological activity. However, the presence of the YMES sequence, adjacent to RAD, significantly increases the peptide's biological potency. The development of such inhibitors derived from the 313-332 region of the alpha(IIb) subunit may be advantageous against the RGD-like antagonists as they could inhibit platelet activation without interacting with alpha(IIb)beta(3), thus failing to further induce alpha(IIb)beta(3)-mediated outside-in signalling.en
heal.publisherBlackwell Publishingen
heal.journalNameEuropean Journal of Biochemistryen
heal.journalTypepeer reviewed-
heal.fullTextAvailabilityTRUE-
Appears in Collections:Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά). ΧΗΜ

Files in This Item:
File Description SizeFormat 
Mitsios-2004-Effect of synthetic.pdf306.1 kBAdobe PDFView/Open    Request a copy


This item is licensed under a Creative Commons License Creative Commons