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Thromb Haemost 2003; 89(05): 866-874
DOI: 10.1055/s-0037-1613474
Platelets and Blood Cells
Schattauer GmbH

Green tea epigallocatechin-3-gallate inhibits platelet signalling pathways triggered by both proteolytic and non-proteolytic agonists

Renzo Deana
1   Department of Biological Chemistry and Institute of the Neuroscience of the Italian National Research Council (CNR), University of Padova, Italy
,
Loris Turetta
1   Department of Biological Chemistry and Institute of the Neuroscience of the Italian National Research Council (CNR), University of Padova, Italy
,
Arianna Donella-Deana
1   Department of Biological Chemistry and Institute of the Neuroscience of the Italian National Research Council (CNR), University of Padova, Italy
,
Massimo Donà
2   Department of Experimental Biomedical Sciences, University of Padova, Italy
,
Anna Maria Brunati
1   Department of Biological Chemistry and Institute of the Neuroscience of the Italian National Research Council (CNR), University of Padova, Italy
,
Lucia De Michiel
1   Department of Biological Chemistry and Institute of the Neuroscience of the Italian National Research Council (CNR), University of Padova, Italy
,
Spiridione Garbisa
2   Department of Experimental Biomedical Sciences, University of Padova, Italy
› Author AffiliationsFinancial support: This work was supported financially by the Italian Association for Research on Cancer, the Italian Ministry for University and Research (MIUR) and the Italian National Research Council (CNR).
Further Information

Publication History

Received 20 November 2002

Accepted after revision 20 February 2003

Publication Date:
09 December 2017 (online)

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Summary

Epigallocatechin-3-gallate (EGCG), a component of green tea, inhibits human platelet aggregation and cytosolic [Ca2+]cincreases more strongly when these processes are induced by thrombin than by the non-proteolytic thrombin receptor activating peptide (TRAP), thromboxane mimetic U46619, or fluoroaluminate. In line with the previously demonstrated EGCG anti-proteolytic activity, a marked inhibition on aggregation is obtained by pre-incubation of thrombin with EGCG prior to addition to cellular suspension. The catechin also reduces cellular Ca2+ influx following thapsigargin-induced calcium emptying of endoplasmic reticulum, and the agonist-promoted cellular protein tyrosine phosphorylation. Both tyrosine kinases Syk and Lyn, immuno-precipitated from stimulated platelets, are greatly inhibited upon cellular pre-incubation with EGCG, which also inhibits the in vitro auto-phosphorylation and exogenous activity of these two enzymes purified from rat spleen. Both thrombin-induced aggregation and [Ca2+]c increase are reduced in platelets from rats that drank green tea solutions. It is concluded that EGCG inhibits platelet activation, by hindering the thrombin proteolytic activity, and by reducing the agonist-induced [Ca2+]cincrease through inhibition of Syk and Lyn activities.

Keywords

Epigallocatechin-3-gallate (EGCG) - thrombin proteolytic activity - platelet cytosolic Ca2+ - non-receptor tyrosine kinases
 

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