## 1 Introduction  
Pleitotropic NF-\(\kappa\)B normally exists as an inactive cytoplasmic complex; its predominant form is a heterodimer composed of p50 and p65 subunits. These subunits are tightly bound to inhibitors of \(\kappa\)B (I\(\kappa\)B) proteins. NF-\(\kappa\)B activation occurs when I\(\kappa\)B\(\alpha\) is phosphorylated by the I\(\kappa\)B kinase (IKK) complex. The most active subunit of IKK (\(\alpha\), \(\beta\), and \(\gamma\)) has been identified as IKK\(\beta\). I\(\kappa\)B\(\alpha\) is the most represented of the two subunits (I\(\kappa\)B\(\alpha\) and I\(\kappa\)B\(\beta\)). It starts dissociating I\(\kappa\)B\(\alpha\) from NF-\(\kappa\)B subunits, and I\(\kappa\)B\(\alpha\) is then ubiquitinated and rapidly degraded by the proteasome associated with NF-\(\kappa\)B nuclear translocation [1]. NF-\(\kappa\)B is considered to be a prototypical proinflammatory pathway that expresses proinflammatory-related genes, such as cytokines, chemokines, and adhesion molecules [2]. Therefore, targeting NF-\(\kappa\)B may greatly influence the treatment of various inflammatory diseases. Platelets represent a critical link between inflammation and thrombosis [3]. Activated platelets stimulate thrombus formation in response to a rupture of atherosclerotic plaque, promoting cardiovascular diseases (CVDs) [4]. Several agonists, such as collagen, thrombin, arachidonic acid, and ADP-induced platelet activation, are associated with the release of various inflammatory mediators, such as P-selectin, interleukin (IL)-1\(\beta\), transforming growth factor-81 (TGF-81), matrix metalloproteinases, tumor necrosis factor (TNF)-\(\alpha\), and IL-6 [5]. Activated NF-\(\kappa\)B has been identified in human atherosclerotic plaque and has been reported to be enhanced in unstable coronary plaque [6]. Although platelets lack a nucleus, many functional transcription factors, including signal transducer and activator of transcription 3 (STAT3) and NF-\(\kappa\)B, are involved in platelet activation [7]. Activation of NF-\(\kappa\)B signaling cascades, such as IKK\(\kappa\) phosphorylation, 1\(\kappa\)B\(\alpha\) degradation, and p65 phosphorylation, plays a role in classical agonist-mediated platelet activation [7; 8; 9]. However, the detailed mechanisms through which the NF-\(\kappa\)B pathway contributes to platelet activation have not been fully elucidated. The phosphoinositide 3-kinases (PI3 Ks)/Akt pathway is activated in response to various stimulating substances, such as growth factors, cytokines, hormones, and extracellular matrix proteins; this pathway regulates a wide spectrum of cellular processes, including cell cycle progression and cell survival. PI3 Ks are a family of lipid kinases that are activated in platelets and that regulate platelet activation [10]. Akt is the main downstream effector for PI3 Ks, which is phosphorylated by protein kinase C (PKC) and by Ca\({}^{2+}\)/calmodulin-dependent protein kinase and is also amplified by platelet ADP secretion [11; 12]. Pterostilbene (PTE; trans-3,5-dimethoxy-4\({}^{\prime}\)-hydroxystilbene), a natural stilbenoid occurring in citrus types of fruits, is a dimethylated analog of resveratrol [13]. PTE exhibits numerous notable biological properties, including antiaging, anticancer, antidiabetic, and neuroprotective functions [14; 15]. Additionally, PTE inhibited the PDGF-BB-induced cell growth of vascular smooth muscle cells in rats through the inhibition of the Akt-dependent pathway [15]. As described previously [16], PTE (1-5 \(\mu\)M) exhibited powerful inhibitory activity in platelet aggregation stimulated by collagen, but not by thrombin, U46619, or arachidonic acid, in human platelets. PTE markedly reduced P-selectin expression, ATP-release, intracellular ([Ca\({}^{2+}\)]) mobilization, phospholipase C (PLC)\(\gamma\)2/PKC, and mitogen-activated protein kinase (MAPKs) phosphorylation stimulated by collagen.