Gals (galectins) are proteins with glycan affinity that are emerging as mediators of atherosclerosis. Despite the similarities in structure and sequence, different Gals exert distinct effects on their target cells. We have shown that Gal-1 triggers platelet activation, suggesting a role for Gals in thrombus formation. Since Gal-8 is expressed upon endothelial activation and also contributes to inflammation, to understand further the role of these lectins in haemostasis, we evaluated the effect of Gal-8 on human platelets. Gal-8 bound specific glycans in the platelet membrane and triggered spreading, calcium mobilization and fibrinogen binding. It also promoted aggregation, thromboxane generation, P-selectin expression and granule secretion. GP (glycoprotein) αIIb and Ib-V were identified as putative Gal-8 counter-receptors by MS. Studies performed using platelets from Glanzmann's thromboasthenia and Bernard–Soulier syndrome patients confirmed that GPIb is essential for transducing Gal-8 signalling. Accordingly, Src, PLC2γ (phospholipase C2γ), ERK (extracellular-signal-regulated kinase) and PI3K (phosphoinositide 3-kinase)/Akt downstream molecules were involved in the Gal-8 signalling pathway. Gal-8 fragments containing either the N- or C-terminal carbohydrate-recognition domains showed that activation is exerted through the N-terminus. Western blotting and cytometry showed that platelets not only contain Gal-8, but also expose Gal-8 after thrombin activation. These findings reveal Gal-8 as a potent platelet activator, supporting a role for this lectin in thrombosis and inflammation.
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Research Article|
November 25 2010
Human platelets express and are activated by galectin-8
Maria Albertina Romaniuk;
Maria Albertina Romaniuk
1
*Thrombosis I Laboratory, Hematological Research Institute, National Academy of Medicine, CONICET, Buenos Aires, Argentina
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Maria Virginia Tribulatti;
Maria Virginia Tribulatti
1
†Institute of Biotechnological Investigations - Technologic Institute of Chascomús-National University of San Martín, CONICET, Argentina
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Valentina Cattaneo;
Valentina Cattaneo
†Institute of Biotechnological Investigations - Technologic Institute of Chascomús-National University of San Martín, CONICET, Argentina
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Maria Jose Lapponi;
Maria Jose Lapponi
*Thrombosis I Laboratory, Hematological Research Institute, National Academy of Medicine, CONICET, Buenos Aires, Argentina
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Felisa Concepcion Molinas;
Felisa Concepcion Molinas
‡Hematology Research Section, Alfredo Lanari Institute, University of Buenos Aires, CONICET, Buenos Aires, Argentina
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Oscar Campetella;
Oscar Campetella
2
†Institute of Biotechnological Investigations - Technologic Institute of Chascomús-National University of San Martín, CONICET, Argentina
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Mirta Schattner
*Thrombosis I Laboratory, Hematological Research Institute, National Academy of Medicine, CONICET, Buenos Aires, Argentina
3To whom correspondence should be addressed (email mschattner@hematologia.anm.edu.ar).
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Publisher: Portland Press Ltd
Received:
April 09 2010
Revision Received:
September 09 2010
Accepted:
September 21 2010
Accepted Manuscript online:
September 21 2010
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© The Authors Journal compilation © 2010 Biochemical Society
2010
Biochem J (2010) 432 (3): 535–547.
Article history
Received:
April 09 2010
Revision Received:
September 09 2010
Accepted:
September 21 2010
Accepted Manuscript online:
September 21 2010
Citation
Maria Albertina Romaniuk, Maria Virginia Tribulatti, Valentina Cattaneo, Maria Jose Lapponi, Felisa Concepcion Molinas, Oscar Campetella, Mirta Schattner; Human platelets express and are activated by galectin-8. Biochem J 15 December 2010; 432 (3): 535–547. doi: https://doi.org/10.1042/BJ20100538
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