## 1 Introduction  
Platelets play a central role in hemostasis, a vital physiological process that prevents excessive blood loss by forming a platelet plug at sites of vascular injury. During vascular damage, circulating platelets adhere to exposed subendothelial components, are activated by adhesive proteins or soluble agonists, and aggregate to form a hemostatic plug [1]. However, dysregulated platelet activation and aggregation can result in pathological thrombus formation and vascular occlusion, which are major contributors to thrombotic disorders, including myocardial infarction, ischemic stroke, and deep vein thrombosis [2]. Therefore, maintaining a delicate balance between platelet adhesion and aggregation is crucial to prevent thrombotic events while preserving normal hemostatic function. Platelets express diverse receptors that mediate their adhesion and aggregation in response to vascular injury. Among these, Glycoprotein VI (GPVI) is critical for collagen-induced platelet activation, whereas G-protein-coupled receptors (GPCRs) respond to soluble agonists such as thrombin, ADP, and thromboxane A\({}_{2}\) (TXA\({}_{2}\)) [3, 4, 5, 6]. Although these pathways differ in their initial signaling mechanisms, they converge on shared intracellular processes that drive platelet aggregation, granule secretion, and integrin \(\alpha\)Ilb\(\beta\)3 activation. Activated platelets generate second messengers, including diacylglycerollycerol (DAG) and inositol 1,4,5-trisphosphate (IP3), from the membrane phospholipid phosphatidylinositol 4,5-bisphosphate (PIP2) [7]. DAG and IP3 are essential for platelet function, facilitating protein kinase C (PKC) activation and intracellular calcium mobilization, respectively [3; 8; 9]. Additionally, DAG contributes to TXA\({}_{2}\) synthesis, while PIP2 is converted into phosphatidylinositol 3,4,5-trisphosphate (PIP3) by phosphoinositide 3-kinase (PI3K), enabling the activation of protein kinase B (Akt), a regulator of platelet spreading and integrin-mediated inside-out signaling [10]. In contrast, cyclic AMP (cAMP) signaling negatively regulates platelet activation by inhibiting intracellular calcium mobilization and integrin activation [11; 12]. The Korean dandelion (_Taraxacum coreannu Nakai, T. coreannum_) is widely consumed in traditional Korean cuisine, where its leaves, stems, and flowers are incorporated into soups, pickles, teas, and salads. Beyond its culinary applications, _T. coreannum_ is valued for its nutritional and health-promoting properties. Previous studies have highlighted its therapeutic potential in treating conditions such as gastritis, gastric ulcers, and tonsillitis, attributing these effects to its anti-inflammatory, antioxidant, and apoptotic properties [13; 14]. These properties are particularly relevant to platelet activation and thrombosis, as oxidative stress and inflammation play key roles in thrombus formation. Antioxidants can mitigate platelet activation by reducing reactive oxygen species (ROS), while anti-inflammatory compounds may inhibit pro-thrombotic mediators, such as Cyclooxygenase-2 (COX-2) and NF-kB [15; 16]. Although the bioactive components of _T. coreannum_ have not been extensively characterized, previous research suggests that it contains significant levels of flavonoids (luteolin, quercetin, apigenin), phenolic acids (chlorogenic acid, caffe acid), and terpenoids, which have demonstrated anti-inflammatory, antioxidant, and cardiovascular-protective effects [13; 17; 18; 19; 20]. These compounds are known to modulate key platelet activation pathways, including PI3K/Akt and COX-1 signaling, suggesting their potential contribution to the observed antiplatelet effects of _T. coreannum_ extract (TCE). However, despite these potential mechanisms, there is a notable lack of studies examining the direct effects of _T. coreannum_ on platelet aggregation and thrombus formation. Addressing this gap is essential to understanding its potential as a therapeutic agent in thrombotic disorders.