Funktionelle Proteomanalyse humaner Thrombozyten

Zusammenfassung

Thrombozyten sind als anukleäre Zellen ideale Forschungsobjekte für moderne Proteomanalysen. Trotz ihrer Bedeutung in Hämostase und Thrombose ist das Proteinrepertoire von Plättchen zu großen Teilen bislang nicht detailliert charakterisiert worden. In Vorbereitung auf bioinformatische und funktionelle Studien wurde eine Reihe von Proteomanalysen auf Thrombozytensubproteome angewendet, die ein Plasmamembranproteom sowie die Analyse von posttranslationalen Modifikationen einschließen. Auf dieser Basis konnten 489 Proteine dargestellt werden, die nicht in bisherigen Proteomansätzen charakterisiert wurden sowie über 550 Phosphorylierungs- und 326 N-Glykosylierungsstellen. Diese Ergebnisse stellen neue Ansatzpunkte für funktionelle Forschungen durch die Identifikation neuer Plättchenproteine bzw. derer Modifikationen dar.

Summary

Platelets are anucleated cells and therefore ideal research objects for modern proteome analyses. Despite their importance in thrombosis and hemostasis the protein content of platelets is still poorly characterized in major parts. In preparation for bioinformatic and functional studies a series of proteomic analyses was conducted for platelet subproteomes as well as for posttranslational modifications. Thereby, the identification of 489 proteins, over 550 phosphorylations and 326 N-glycosylation sites was possible, which were not identified in previous proteome studies of platelets. Those results represent new research possibilities for functional characterization of platelet proteins as well as their modifications.

Schlüsselwörter

Thrombozyten - Proteom - Massenspektrometrie - Phosphorylierungen - Glykosylierungen

Keywords

Platelets - proteome - mass spectrometry - phosphorylation - glycosylation

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