Institut für Funktionelle Grenzflächen (IFG)

The sweeter aspects of platelet activation: A lectin-based assay reveals agonist-specific glycosylation patterns

  • Autor:

    Gupta, S. / Reviakine, I. (2014)

  • Quelle:

    Biochimica et Biophysica Acta (BBA) - General Subjects 1840 (2014),12, 3423-3433

  • Datum: 2014
  • Gupta, S. / Reviakine, I. (2014): „The sweeter aspects of platelet activation: A lectin-based assay reveals agonist-specific glycosylation patterns“. In: Biochimica et Biophysica Acta (BBA) - General Subjects 1840 (2014),12, 3423-3433

Abstract

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Background
The diversity of platelet functions implies multiple activation states arising in response to different stimuli. Distinguishing between these states has been challenging.

Methods
We used fluorescently labelled carbohydrate binding proteins lectins to investigate agonist-induced changes in platelet surface glycosylation.

Results
Each of the seven agonists we used caused a unique set of changes in platelet surface glycosylation, eliciting a unique functional state. Some of these changes could be correlated with the expression of granule-specific markers CD62P and CD63, but lectins proved much more sensitive to differences between agonists than antibodies against those markers. This sensitivity appears to arise from the relation between the surface glycosylation changes and the signalling pathways through which various agonists act. In this context it is interesting that the effects of calcium ionophore were significantly different from those of other agonists. We also found that that P-selectin (CD62P) contains haptens for lectins VFA and PTII, because these lectins compete with the anti-CD62P antibody binding and vice a versa.

Conclusions
We report for the first time that changes in platelet surface glycosylation are agonist-specific and can be distinguished using lectin-binding assays. Lectin fingerprinting represents a new research and diagnostic tool for studying platelet activation.

General significance
The observation of agonist-specific platelet surface glycosylation changes is interesting in the context of the diversity of platelet function, because surface glycans mediate contact interactions between platelets and other cells and serve as binding sites for some of the agonists (galectins).