## 1 Introduction  
The world major causes of death considered are arterial thrombotic events, such as myocardial infarction, ischemic stroke, and venous thromboembolism [1]. Platelets are derived from megakaryocytes,which are small and discoid in shape and have a lifespan of 7-10 days [2]. Over activation of platelets is associated with atheorthrombotic process and profoundly contribute to the pathology of venous thrombosis [3]. Platelets are adaptable fragments of cytoplasm that have the primary function of arresting bleeding. Understanding the causes of platelet activation and aggregation is imperative. Platelets are key regulators of hemostasis and thrombosis. Platelet activation is triggered by collagen along with thrombin and ADP, which are produced after the atherosclerotic vascular lesion occurred. The NF-kB signaling pathway plays a major controller of various cellular actions, including neurodegenerative, inflammatory, and vascular pathological responses [4]. NF-kB translocate from cytosol into nucleus upon activation for the events of regulating gene expression. In a normal state, NF-kB is attached with its inhibitor of kB (I\(\kappa\)B) and inactively reserved in the cytosol. I\(\kappa\)B\(\alpha\) is the most represented of the two subunits (I\(\kappa\)B\(\alpha\) and I\(\kappa\)B\(\beta\)). The I\(\kappa\)B kinase (IKK) complex phosphorylates I\(\kappa\)B upon activation, initiating proteasome-mediated degradation and freeing NF-kB for nuclear translocation [5]. Among IKK subunits (\(\alpha\), \(\beta\), and \(\gamma\)), IKK\(\beta\) is the most active. The role of NF-\(\kappa\)B in nucleated cells is well documented [6]. Therefore, the actions of NF-\(\kappa\)B have been mostly attributed to various nuclear events. Furthermore, three IKK family members are also expressed in platelets, in which \(\beta\) form being more strongly expressed than \(\alpha\) or \(\gamma\) form [7; 8]. NF-kB signaling in platelets involves IKK\(\beta\) phosphorylation, I\(\kappa\)B\(\alpha\) degradation, and p65 phosphorylation [8]. However, unlike other cells, the crowning events of NF-\(\kappa\)B signaling in platelets remain partially understood. For this purpose, several studies were performed utilizing either pharmacological inhibitors of NF-\(\kappa\)B such as BAY 11-7082 or knockout mice to unravel the role of NF-\(\kappa\)B in platelets, specifically in the context of their activation, and aggregation. Columbianadin (CBN) is a natural coumarin-type compound that is widely used to treat spasms, rheumatisms, and headaches in Chinese medicine [9]. CBN has attracted extensive attention because of its biological activities, such as inhibition of carcinomas (e.g., colon cancer, bladder carcinoma, and human leukemia) [8], and diminished nitric oxide (NO) production by downregulating inducible NO synthase [9]. Moreover, oral administration of CBN (20-60 mg/kg) exhibited inhibitory activity against lung inflammation induced by LPS in mice [10; 11]. CBN exhibited potent activity against ADP-stimulated rat platelets [5]. [PERSON] et al. [12] reported that CBN modulates platelet activation by interfering with the integrin \(\alpha_{\text{HB}}\beta_{3}\) inside-out but not outside-in signals in human platelets. CBN was found to inhibit the phosphorylation of c-Jun N-terminal kinase (JNK) 1/2 and extracellular signal-regulated kinase (ERK) 1/2. Interestingly, CBN did not inhibit p38 mitogen-activated protein kinase (MAPK) in collagen-activated platelets [12]. That study also demonstrated that CBN had remarkable activity against platelet activation through inhibition of the upstream platelet signaling pathways, such as phospholipase Cy2, protein kinase C, Akt. In that, we also noticed that CBN markedly hindered integrin \(\alpha_{\text{HB}}\beta_{3}\) activation by interfering with the binding of PAC-1 (FITC-anti-human CD41/CD61) [12]. Platelets are anucleated cells, they do not differentiate or proliferate and thus provide a favorable model for studying the nongenomic functions of NF-\(\kappa\)B.