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The molecular mechanisms involved in lectin-induced human platelet aggregation

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Veröffentlicht/Copyright: 5. August 2017

Abstract

We have compared the effect of three legume lectins, wheat germ agglutinin (WGA), Phaseolus vulgaris agglutinin (PHA) and Lens culinaris agglutinin (LCA), on the function of human platelets. We have found that WGA is more active than PHA in stimulating platelet activation/aggregation, while LCA has no effect. Studies on the mechanisms involved show that WGA and PHA induce phosphorylation/activation of PLCγ2 and increase [Ca2+]i. For the first time, it has been shown that Src/Syk pathway, the adapter protein SLP-76 and the exchange protein VAV, participate in the PLCγ2 activation by these lectins. Moreover WGA and PHA stimulate the PI3K/AKT pathway. PI3K, through its product phosphatidylinositol-3,4,5-trisphosphate activates Bruton’s tyrosine kinase (BTK) and contributes to PLCγ2 activation. In conclusion, our findings suggest that PLCγ2 activation induced by WGA and PHA is regulated by Src/Syk and by PI3K/BTK pathways through their concerted action.

Acknowledgments

This work was supported by the Genoa University (Fondo di Ricerca di Ateneo 2015), Italy. The authors thank Dr. Massimo Grilli (DIFAR, Dept. Pharmacy, Pharmacology Section) for supporting us with the flow cytometric analysis.

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Received: 2017-2-13
Accepted: 2017-7-31
Published Online: 2017-8-5
Published in Print: 2017-11-27

©2017 Walter de Gruyter GmbH, Berlin/Boston

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