Dementia illnesses have a significant impact on global health, with an estimated incidence of approximately 50 million individuals annually. Furthermore, the prevalence of such conditions, particularly Alzheimer's disease (AD), is on the rise. Alzheimer's disease (AD) is prevalent as a type of dementia, and it impacts a considerable percentage of individuals above the age of 65, with an estimated incidence of 10% [1]. The aforementioned affliction is a type of hereditary disorder that is recognized for its progressive and heterogeneous nature, whereby it is inherited in an autosomal dominant manner [2, 3]. There exist various theories concerning the pathogenesis of AD within the academic discourse. As posited by the "Amyloid hypothesis," the degeneration of brain tissue leading to Alzheimer's disease (AD) symptoms is brought about by the accumulation of tau protein within neurons and amyloid-β (Aβ) peptides external to neurons [4]. Moreover, several studies have demonstrated that oxidative stress plays a significant role as a causative factor in the development of pathogenesis and neuronal injuries in Alzheimer's disease [5, 6]. Tau is a protein that associates with microtubules (MTs) in neurons of both the central and peripheral nervous systems and serves to stabilize them [6]. When phosphorylation of a protein occurs abnormally, it leads to the accumulation of the protein in significant quantities within nerve cells. This state, referred to as tauopathy, triggers the formation of neurofibrillary tangles (NFT). The progression of NFT gradually disrupts synapses, causes cell death, and ultimately gives rise to disease symptoms [7]. The regulation of Tau activity is governed by a cycle of phosphorylation and dephosphorylation. The process of phosphorylation of tau has been postulated to result in dissociation of this protein from microtubule structures. The phenomenon under consideration involves the attachment of the protein to microtubules through dephosphorylation, thereby ensuring its stability [8]. Following the process of transcription, the tau gene undergoes different splicing patterns resulting in the generation of various mRNA forms that give rise to distinct tau isoforms. Alterations to the tau gene or the extent of tau phosphorylation may serve as a diagnostic indicator for multiple diseases, including Alzheimer's disease [9]. The longest isoform of this particular protein is reported to possess approximately 85 potential phosphorylation sites [10]. Multiple kinases, including Glycogen Synthase Kinase (GSK), have been identified as culprits involved in tau phosphorylation. However, it is the Protein Phosphatase 2A (PP2A) that serves as the primary phosphatase responsible for tau in the brain. Furthermore, it has been found that the expression and activity of PP2A decrease in the brain of patients with Alzheimer's disease, as reported by previous literature [11]. The aberrant expression of Glycogen Synthase Kinase-3 beta (GSK-3β), a serine-threonine kinase, has been implicated in the pathogenesis of Alzheimer's disease [12]. The phenomenon of over-expression results in hyperphosphorylation of tau, thereby instigating the development of tangles. As postulated by extant literature, GSK-3b represents a promising therapeutic target for the management of Alzheimer's disease, as demonstrated by reference [13]. Numerous phosphatases, including Protein Phosphatase 1 (PP1), Protein Phosphatase 2A (PP2A), Protein Phosphatase 2B (PP2B), and Protein Phosphatase 2C (PP2C), have demonstrated the ability to catalyze the dephosphorylation of tau. Of these phosphatases, PP2A has been found to be particularly active across a majority of tau's phosphorylation sites [14]. Several aberrations associated with PP2A phosphatase have been documented in Alzheimer's disease, encompassing diminished mRNA expression and decreased protein methylation [15]. Given the premise that current treatment modalities for Alzheimer's disease primarily focus on alleviating associated symptoms, there exists a crucial need to explore novel therapies derived from innovative resources. Plant resources have the potential to serve as viable alternatives in this context. Resveratrol, 3,5,4′-trihydroxy-trans-stilbene, is a polyphenol which is produced as a secondary metabolite in plants [16]. The primary origins of resveratrol comprise grape varieties, peanuts, pomegranates, spinach, and bananas [17, 18]. The mechanisms underlying resveratrol's efficacy in ameliorating Alzheimer's disease (AD) entail multiple elements, such as its antioxidant properties, suppression of neuronal inflammation, hindrance of tauopathy and amyloid beta (Aβ) plaque formation, which ultimately facilitate the preservation of neural survival and enhancement of cognitive function [19]. Vitis vinifera, commonly known as black grape, is a plant species that boasts a high concentration of polyphenols. It has been reported that up to 95% of these polyphenols are localized in the core and skin tissues of the fruit. The aforementioned compounds, namely resveratrol, catechin, epigalactocatechin, and epigalactocatechin-3-gallate, have been identified [20]. This investigation employed the PC12 cell line, which is among the widely utilized cell lines in neuroscience research. The popularity of PC12 cells is attributed to their exceptional adaptability for pharmacological manipulation, ease of cultivation, and ample knowledge regarding their proliferative and differentiative characteristics [21]. The compound formaldehyde was employed in the generation of an Alzheimer's disease model utilizing said cells. Formaldehyde is present both as an exogenous environmental agent and an endogenous metabolite in the organism. Recent research has indicated that the production of formaldehyde within the body can be induced through both endogenous and exogenous pathways, thereby facilitating the onset and progression of Alzheimer's disease [22]. The correlation between its toxicity and the pathogenesis of Alzheimer's disease (AD) is evidenced by the formation of beta-amyloid plaques, tau hyperphosphorylation, and neuron depletion [23]. The current study endeavors to examine the potential of resveratrol and grape extract in mitigating or hindering the symptoms of Alzheimer's disease in cloned cells. This objective is pursued by exploring the impact of these natural compounds on the pertinent genes, namely Protein Phosphatase 2A (PP2A) and Glycogen synthase kinase-3 beta (GSK-3b), as well as investigating their antioxidant properties, survival rates, cytotoxicity, and apoptotic rate within the modeled cells.