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  4. Τμήμα Χημείας
  5. Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά). ΧΗΜ
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Please use this identifier to cite or link to this item: https://olympias.lib.uoi.gr/jspui/handle/123456789/10634
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dc.contributor.authorKoloka, V.en
dc.contributor.authorChristofidou, E. D.en
dc.contributor.authorVaxevanelis, S.en
dc.contributor.authorDimitriou, A. A.en
dc.contributor.authorTsikaris, V.en
dc.contributor.authorTselepis, A. D.en
dc.contributor.authorPanou-Pomonis, E.en
dc.contributor.authorSakarellos-Daitsiotis, M.en
dc.contributor.authorTsoukatos, D. C.en
dc.date.accessioned2015-11-24T16:57:55Z-
dc.date.available2015-11-24T16:57:55Z-
dc.identifier.issn0953-7104-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/10634-
dc.rightsDefault Licence-
dc.subjectiib3 receptoren
dc.subjectpalmitoylated peptidesen
dc.subjectiib cytoplasmic domainen
dc.subjectplatelet-aggregation inhibitoren
dc.subjectglycoprotein iib/iiiaen
dc.subjectsignal-transductionen
dc.subjectalpha-subuniten
dc.subjectalpha(iib)beta(3)en
dc.subjecttailen
dc.subjecttyrosineen
dc.subjectbindingen
dc.subjecttalinen
dc.subjectaggregationen
dc.subjectpathwaysen
dc.titleA palmitoylated peptide, derived from the acidic carboxyl-terminal segment of the integrin IIb cytoplasmic domain, inhibits platelet activationen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.primaryDoi 10.1080/09537100802266875-
heal.identifier.secondary<Go to ISI>://000260607400004-
heal.identifier.secondaryhttp://informahealthcare.com/doi/abs/10.1080/09537100802266875-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείαςel
heal.publicationDate2008-
heal.abstractPlatelet integrin IIb3 contains an acidic membrane distal motif, 1000LEEDDEEGE1008, in the cytoplasmic domain of the IIb subunit. We showed that a lipid-modified peptide corresponding to the above region, palmitoyl-K-LEEDDEEGE (pal-K-1000-1008), is platelet permeable and has inhibited platelet aggregation induced by 0.4 U/ml of thrombin (IC50 = 164 M). Moreover the peptide inhibited both Fibrinogen and PAC-1, binding to activated platelets. The non palmitoylated analog was inactive. A modified, scrambled acidic peptide (palmitoyl-K-GDDEELEEE), showed significant lower inhibitory activity than pal-K-1000-1008. A palmitoylated peptide corresponding to the membrane proximal cytoplasmic domain of IIb, 989KGVFFKR995 (pal-989-995), is known to specifically induce platelet aggregation. Pal-K-1000-1008 was an inhibitor of human washed platelet aggregation induced by pal-K-989-995 (IC50 = 15 M). Moreover, pal-K-1000-1008 inhibited phosphorylation of ERK and FAK, two protein kinases involved in platelet activation and aggregation. Our results favour the assumption that the interaction of the membrane proximal sequence 989KGVFFKR995 of the cytoplasmic domain of IIb with the acidic terminal 1000LEEDDEEGE1008 motif may be an important structural factor in platelet signaling, leading to platelet activation and aggregation.en
heal.journalNamePlateletsen
heal.journalTypepeer reviewed-
heal.fullTextAvailabilityTRUE-
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