Abstract : Tau phosphorylation indicates the pathology features of several neurodegenerative diseases such as Alzheimer's disease and frontotemporal dementia that reflect the presence of an end-staged neurofibrillary lesion. This factor determines the alteration of soluble tau protein in the neurodegeneration process and influences the tau structure, distribution, and function in the neurons. The cytosol protein is related to microtubules and regulates external transport in demonstrating additional functions of DNA stabilization and synaptic function. This factor helps to examine the test spread of tau pathology in the disease model for understanding the potential role of extracellular tau in the cell signal in pathways for the neurodegeneration process. Significant heterogeneity had been described between various tauopathies that deposit tau in pathological lesions in mass spectrometric analysis. The caspase cleavage tau fragment assists to determine the effective region of the tauopathy brain in humans for seeding nidus for the promotion of aggregation and fibrillation of full-length tau species.
The progression of neurodegenerative disease reflects the promotion of environmental and genetic factors that indicate serine, tyrosine, and threonine in tau phosphorylation. This element is used to change the structure of tau protein in the human brain and affected the communication between the brain and other human organs due to the death of neurons. The secondary data collection is utilized in this study by collecting details from journals and research articles related to the aggression of tau protein and phosphorylation in promoting neurodegenerative disease. The objective and aim of the study are to identify the impact of tau protein on neurodegenerative disease and its influence on the human brain.

Keywords : Caspase Cleavage, Neurodegeneration, Neurofibrillary Lesion, Tau Phosphorylation, Tau Protein.