Abstract
Simple SummaryNeurodegenerative disorders are complex disorders that display a variety of clinical manifestations. The second-most common neurodegenerative disorder is Parkinson’s disease, and the leading pathological protein of the disorder is considered to be α-synuclein. Nonetheless, α-synuclein accumulation also seems to result in multiple system atrophy and dementia with Lewy bodies. In order to obtain a more proficient understanding in the pathological progression of these synucleinopathies, it is crucial to observe the post-translational modifications of α-synuclein and the conformations of α-synuclein, as well as its role in the dysfunction of cellular pathways.α-synuclein is considered the main pathological protein in a variety of neurodegenerative disorders, such as Parkinson’s disease, multiple system atrophy, and dementia with Lewy bodies. As of now, numerous studies have been aimed at examining the post-translational modifications of α-synuclein to determine their effects on α-synuclein aggregation, propagation, and oligomerization, as well as the potential cellular pathway dysfunctions caused by α-synuclein, to determine the role of the protein in disease progression. Furthermore, α-synuclein also appears to contribute to the fibrilization of tau and amyloid beta, which are crucial proteins in Alzheimer’s disease, advocating for α-synuclein’s preeminent role in neurodegeneration. Due to this, investigating the mechanisms of toxicity of α-synuclein in neurodegeneration may lead to a more proficient understanding of the timeline progression in neurodegenerative synucleinopathies and could thereby lead to the development of potent targeted therapies.
Highlights
Neurodegenerative disorders are heterogenous perplexing assemblages with disparate etiology and intermittently coinciding clinical manifestations [1]
Parkinson’s disease (PD) is distinguished by an advancing reduction of dopaminergic neurons in the substantia nigra pars compacta (Figure 1) [3]
This leads to a striatal diminishing of dopamine in a location of the brain that is accountable for regulating fine motor control, eventually resulting in the tremors, bradykinesia, and rigidity often visualized in PD patients [4]
Summary
Neurodegenerative disorders are heterogenous perplexing assemblages with disparate etiology and intermittently coinciding clinical manifestations [1]. The phosphatidylcholine headgroup is subsequently cleaved by phospholipase D (PLD), which thereby liberates phosphatidic acid and choline, which have been involved in regulated exocytosis via trafficking in the membrane [24] This function has not been entirely proven by consequential studies [25]. Α-synuclein point mutations account for a small percentage of PD, the dystrophic neurites and Lewy bodies seen in the most common type of PD, idiopathic PD, greatly imply α-synuclein [8,37]. This is further demonstrated with a plethora of monoclonal antibodies recognizing α-synuclein when they were formerly made against Lewy bodies [39]. This upholds the belief that, even though various proteins compile in PD inclusion, the αsynuclein protein preponderates [40]
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