Based on clinical and preclinical studies from the past two decades, there is evidence that α-synuclein is the cause and driver of the disease. In 1997, aggregated α-synuclein was identified in Lewy bodies, and this raised the question of whether aggregated α-synuclein is the cause of the disease or exists as bystander or end product of the disease. Intraneuronal inclusions of aggregated proteins in PD were first reported in 1912 and were named Lewy bodies. Therefore, substantial research has been conducted to elucidate the role of α-synuclein and tau as the pathogenic causes of neurodegenerative diseases.
Additionally, distinct atypical parkinsonian syndromes, such as progressive supranuclear palsy (PSP) and corticobasal degeneration (CBD), share the common neuropathologic feature of tau deposition in the brain. Although the dominantly affected cell types and anatomical locations differ among the disorders, a common feature is the aggregation of α-synuclein in the central nervous system.
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Subsequent studies have found that a series of parkinsonian disorders with various progression rates and distinct clinical features, such as multiple system atrophy (MSA) and dementia with Lewy bodies (DLB), share common pathologic features. The neuropathological criteria of Parkinson’s disease (PD) consist of two histopathological features: the loss of dopaminergic neurons and α-synuclein deposition in the substantia nigra. Most neurodegenerative diseases involve characteristic pathologic protein aggregation in the central nervous system with a loss of neurons in characteristic anatomical locations. Keywords: Wordsaaalpha-Synuclein Immunotherapy Tau proteins.In this review, we summarize completed phase I trials and ongoing phase II trials of immunotherapies against α-synuclein and tau and further discuss concerns and hurdles to overcome in the future. Therefore, immunotherapies targeting extracellular α-synuclein and tau have been proposed as potential disease-modifying strategies.
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Furthermore, extracellular pathologic proteins have also been reported to provoke inflammatory responses that lead to neurodegeneration. Emerging evidence has suggested that pathologic α-synuclein and tau are transmitted from cell to cell and further accelerate the aggregation of pathologic proteins in neighboring cells.
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