Related Experiment Video

Updated: Oct 3, 2025

Comprehensive Analysis of Procoagulant Platelets Exhibiting Features of Necrosis, Apoptosis and Platelet Activation
04:37

Comprehensive Analysis of Procoagulant Platelets Exhibiting Features of Necrosis, Apoptosis and Platelet Activation

Published on: May 23, 2025

686

Galectin 3 enhances platelet aggregation and thrombosis via Dectin-1 activation: a translational study

Yufei Chen1,2, Wanrong Fu3, Yunbo Zheng3

  • 1Academy of Integrative Medicine, Shanghai University of Traditional Chinese Medicine, Shanghai 201203, China.

European Heart Journal
|February 15, 2022
PubMed

Insights

Galectin-3, elevated in cardiovascular disease, directly enhances platelet activation and thrombus formation. A Galectin-3 inhibitor, TD139, shows potent antithrombotic effects without increasing bleeding risk.

Area of Science:

  • Cardiovascular Biology
  • Hematology
  • Immunology

Background:

  • Galectin-3, a lectin, is elevated in cardiovascular disease and implicated in heart failure.
  • Its direct role in platelet activation and thrombosis is not well understood.
  • Platelet hyperreactivity contributes to thrombotic events in cardiovascular conditions.

Purpose of the Study:

  • To investigate the direct impact of Galectin-3 on platelet activation and thrombosis.
  • To elucidate the underlying molecular mechanisms of Galectin-3-mediated platelet responses.
  • To evaluate the therapeutic potential of Galectin-3 inhibition in preclinical models.

Main Methods:

  • Correlating plasma Galectin-3 levels with platelet aggregation and thrombus formation in coronary artery disease (CAD) patients.
  • Conducting in vitro platelet function assays and in vivo thrombosis models.
  • Utilizing Dectin-1 knockout mice and a Dectin-1 inhibitor (laminarin) to explore mechanistic pathways.
  • Assessing the efficacy and safety of the Galectin-3 inhibitor TD139 in ApoE-/- mice.

Main Results:

  • Elevated plasma Galectin-3 positively correlated with platelet aggregation and thrombus formation in CAD patients.
  • Galectin-3 directly potentiated platelet activation and in vivo thrombosis.
  • Galectin-3 activates platelets via Dectin-1, leading to spleen tyrosine kinase phosphorylation, increased intracellular calcium, protein kinase C activation, and reactive oxygen species production.
  • TD139 suppressed Galectin-3-induced platelet activation and occlusive thrombosis in mice without increasing bleeding.
  • TD139 also reduced microvascular thrombosis and protected the heart from ischemia-reperfusion injury.

Conclusions:

  • Galectin-3 is identified as a novel positive regulator of platelet hyperreactivity and thrombus formation in CAD.
  • Galectin-3 inhibitors, like TD139, demonstrate significant antithrombotic effects with a favorable safety profile regarding bleeding.
  • These findings suggest that Galectin-3 inhibitors hold therapeutic promise as antiplatelet agents for individuals with elevated Galectin-3 levels.
Abstract

Keywords:
AntithromboticCardiovascular diseasesDectin-1Galectin-3Platelet hyperreactivityTD139

More Related Videos

Ferric Chloride-induced Murine Thrombosis Models10:37

Ferric Chloride-induced Murine Thrombosis Models

Published on: September 5, 2016

22.1K
Platelet Adhesion and Aggregation Under Flow using Microfluidic Flow Cells10:10

Platelet Adhesion and Aggregation Under Flow using Microfluidic Flow Cells

Published on: October 27, 2009

18.3K

Related Concept Videos

Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...
2.9K
Antiplatelet Drugs: Prostaglandin Synthesis, P2Y12 and Glycoprotein IIb/IIIa Inhibitors01:20

Antiplatelet Drugs: Prostaglandin Synthesis, P2Y12 and Glycoprotein IIb/IIIa Inhibitors

Antiplatelet drugs emerge as frontline defenders against the insidious threat of thromboembolic diseases, where abnormal clots obstruct vital blood vessels. These drugs stand as bulwarks, inhibiting platelet aggregation and clot formation, thereby mitigating the risk of life-threatening conditions like myocardial infarction, coronary artery disease, and thrombotic strokes.
Prostaglandin synthesis inhibitors, exemplified by the widely known aspirin, wield their power by irreversibly acetylating...
682
Structure and Function of Platelets01:18

Structure and Function of Platelets

The cell fragments known as platelets are disc-shaped, with an average diameter of about 3 μm and a thickness of roughly 1 μm. They play a crucial role in the body's vascular clotting system, which also involves plasma proteins, blood cells, and blood vessel tissues.
Platelets are continually replenished, circulating in the bloodstream for 9-12 days before being removed by phagocytes, primarily in the spleen. A microliter of circulating blood contains between 150,000 and 450,000...
1.9K
Formation of the Platelet Plug01:22

Formation of the Platelet Plug

The platelet phase, the second stage of hemostasis, commences around 15-20 seconds after an injury. It follows and overlaps with the vascular phase, during which blood vessels constrict to minimize blood loss.
As the injured blood vessel contracts, endothelial cells undergo contraction, revealing collagen fibers in the basement membrane and underlying connective tissue. Furthermore, the plasma membrane of endothelial cells becomes adhesive, preparing the site for platelet adhesion. Platelets...
7.5K
Activation of Integrins01:15

Activation of Integrins

Integrins bind ligands and transmit information from outside the cell to inside or vice-versa through an "outside-in signaling" or "inside-out signaling."
In "outside-in signaling," external factors in the extracellular space bind to exposed ligand binding sites on integrins. This causes the inactive protein to undergo a conformational change to become active. Integrins are often clustered on the cell membrane. Repetitive and regularly spaced ligand binding...
3.7K
Selectins01:25

Selectins

Cell adhesion is  an essential aspect of multicellularity. While stable cell interactions usually occur between cells of the same type, transient cell interactions occur between cells of different tissue types, such as between neutrophils and endothelial cells. Selectins are one class of cell adhesion molecules (CAMs) that bind carbohydrate ligands to form transient cell adhesion. They are rod-like proteins with a long extracellular part of variable length ending with the lectin domain,...
3.5K