The immunoregulatory glycan-binding protein galectin-1 triggers human platelet activation
Platelet activation is a critical process during inflammation, thrombosis, and cancer. Here, we show that galectin-1, an endogenous lectin with immunoregulatory properties, plays a key role in human platelet activation and function. Galectin-1 binds to human platelets in a carbohydrate-dependent man...
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| Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_08926638_v22_n4_p1113_Pacienza |
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todo:paper_08926638_v22_n4_p1113_Pacienza2023-10-03T15:41:36Z The immunoregulatory glycan-binding protein galectin-1 triggers human platelet activation Pacienza, N. Pozner, R.G. Bianco, G.A. D'Atri, L.P. Croci, D.O. Negrotto, S. Malaver, E. Gómez, R.M. Rabinovich, G.A. Schattner, M. Hemostasis Inflammation Lectin P-selectin adenosine diphosphate adenosine triphosphate calcium ion carbohydrate binding protein cyclic nucleotide F actin galectin 1 glycan glycoprotein IIIa PADGEM protein thrombin article cell interaction controlled study human human cell immunoregulation leukocyte normal human polymerization priority journal protein binding protein induction thrombocyte activation thrombocyte aggregation thrombocyte function thrombocyte release reaction upregulation Actins Adenosine Diphosphate Binding Sites Blood Platelets Flow Cytometry Galectin 1 Humans Integrin beta3 Leukocytes Microscopy, Confocal P-Selectin Platelet Activation Platelet Aggregation Signal Transduction Platelet activation is a critical process during inflammation, thrombosis, and cancer. Here, we show that galectin-1, an endogenous lectin with immunoregulatory properties, plays a key role in human platelet activation and function. Galectin-1 binds to human platelets in a carbohydrate-dependent manner and synergizes with ADP or thrombin to induce platelet aggregation and ATP release. Furthermore, galectin-1 induces F-actin polymerization, up-regulation of P-selectin, and GPIIIa expression; promotes shedding of microvesicles; and triggers conformational changes in GPIIb/IIIa. In addition, exposure to this lectin favors the generation of leukocyte-platelet aggregates. A further mechanistic analysis revealed the involvement of Ca2+ and cyclic nucleotide-dependent pathways in galectin-1-mediated control of platelet activation. Finally, expression of endogenous galectin-1 in human platelets contributes to ADP-induced aggregation. Our study reveals a novel unrecognized role for galectin-1 in the control of platelet physiology with potential implications in thrombosis, inflammation, and metastasis. © FASEB. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_08926638_v22_n4_p1113_Pacienza |
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Universidad de Buenos Aires |
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I-28 |
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R-134 |
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Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Hemostasis Inflammation Lectin P-selectin adenosine diphosphate adenosine triphosphate calcium ion carbohydrate binding protein cyclic nucleotide F actin galectin 1 glycan glycoprotein IIIa PADGEM protein thrombin article cell interaction controlled study human human cell immunoregulation leukocyte normal human polymerization priority journal protein binding protein induction thrombocyte activation thrombocyte aggregation thrombocyte function thrombocyte release reaction upregulation Actins Adenosine Diphosphate Binding Sites Blood Platelets Flow Cytometry Galectin 1 Humans Integrin beta3 Leukocytes Microscopy, Confocal P-Selectin Platelet Activation Platelet Aggregation Signal Transduction |
| spellingShingle |
Hemostasis Inflammation Lectin P-selectin adenosine diphosphate adenosine triphosphate calcium ion carbohydrate binding protein cyclic nucleotide F actin galectin 1 glycan glycoprotein IIIa PADGEM protein thrombin article cell interaction controlled study human human cell immunoregulation leukocyte normal human polymerization priority journal protein binding protein induction thrombocyte activation thrombocyte aggregation thrombocyte function thrombocyte release reaction upregulation Actins Adenosine Diphosphate Binding Sites Blood Platelets Flow Cytometry Galectin 1 Humans Integrin beta3 Leukocytes Microscopy, Confocal P-Selectin Platelet Activation Platelet Aggregation Signal Transduction Pacienza, N. Pozner, R.G. Bianco, G.A. D'Atri, L.P. Croci, D.O. Negrotto, S. Malaver, E. Gómez, R.M. Rabinovich, G.A. Schattner, M. The immunoregulatory glycan-binding protein galectin-1 triggers human platelet activation |
| topic_facet |
Hemostasis Inflammation Lectin P-selectin adenosine diphosphate adenosine triphosphate calcium ion carbohydrate binding protein cyclic nucleotide F actin galectin 1 glycan glycoprotein IIIa PADGEM protein thrombin article cell interaction controlled study human human cell immunoregulation leukocyte normal human polymerization priority journal protein binding protein induction thrombocyte activation thrombocyte aggregation thrombocyte function thrombocyte release reaction upregulation Actins Adenosine Diphosphate Binding Sites Blood Platelets Flow Cytometry Galectin 1 Humans Integrin beta3 Leukocytes Microscopy, Confocal P-Selectin Platelet Activation Platelet Aggregation Signal Transduction |
| description |
Platelet activation is a critical process during inflammation, thrombosis, and cancer. Here, we show that galectin-1, an endogenous lectin with immunoregulatory properties, plays a key role in human platelet activation and function. Galectin-1 binds to human platelets in a carbohydrate-dependent manner and synergizes with ADP or thrombin to induce platelet aggregation and ATP release. Furthermore, galectin-1 induces F-actin polymerization, up-regulation of P-selectin, and GPIIIa expression; promotes shedding of microvesicles; and triggers conformational changes in GPIIb/IIIa. In addition, exposure to this lectin favors the generation of leukocyte-platelet aggregates. A further mechanistic analysis revealed the involvement of Ca2+ and cyclic nucleotide-dependent pathways in galectin-1-mediated control of platelet activation. Finally, expression of endogenous galectin-1 in human platelets contributes to ADP-induced aggregation. Our study reveals a novel unrecognized role for galectin-1 in the control of platelet physiology with potential implications in thrombosis, inflammation, and metastasis. © FASEB. |
| format |
JOUR |
| author |
Pacienza, N. Pozner, R.G. Bianco, G.A. D'Atri, L.P. Croci, D.O. Negrotto, S. Malaver, E. Gómez, R.M. Rabinovich, G.A. Schattner, M. |
| author_facet |
Pacienza, N. Pozner, R.G. Bianco, G.A. D'Atri, L.P. Croci, D.O. Negrotto, S. Malaver, E. Gómez, R.M. Rabinovich, G.A. Schattner, M. |
| author_sort |
Pacienza, N. |
| title |
The immunoregulatory glycan-binding protein galectin-1 triggers human platelet activation |
| title_short |
The immunoregulatory glycan-binding protein galectin-1 triggers human platelet activation |
| title_full |
The immunoregulatory glycan-binding protein galectin-1 triggers human platelet activation |
| title_fullStr |
The immunoregulatory glycan-binding protein galectin-1 triggers human platelet activation |
| title_full_unstemmed |
The immunoregulatory glycan-binding protein galectin-1 triggers human platelet activation |
| title_sort |
immunoregulatory glycan-binding protein galectin-1 triggers human platelet activation |
| url |
http://hdl.handle.net/20.500.12110/paper_08926638_v22_n4_p1113_Pacienza |
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