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The implication of α-synuclein in the development of Parkinson’s diseases is attributed to the discovery of the SNCA gene, which codes the protein. According to Abeliovich and Gitler (207), the presence of missense mutations on the gene, which tends to interfere with the sequence of the protein, leads to the development of rare autosomal dominant variants of the disease. This may also arise from the duplication or triplication of the SNCA
loci, which is responsible for the coding of the α-synuclein. However, it is essential to note that the Parkinson’s disease is mainly familial.
α-synuclein protein, according to Abeliovic and Gitler (212) is said to exhibit a prion-like spreading. Just like in the case of prions, the eα-synuclein protein is thought to change from the typical soluble form to aggregate type, which causes many diseases. The process of aggregation of a soluble form leads to the spread of the resulting aggregates and occasions widespread neuro-degeneration in the brain. This attribute, which is shared between prions and the α-synuclein protein is involved in the development of Parkinson’s disease. Therefore, α-synuclein proteins are said to be similar to the prions through this spreading.
Of the proposed therapeutic approaches, the most effective would be those that selectively affect the accumulation of α-synuclein as well or the inhibition of its fibrillation. The exploration of antibodies that work against this accumulation is a viable therapeutic approach capable of transforming their functionality. Through this, from a personal viewpoint, the genetic Parkinson’s disease would be easier to eliminate through the administration of the antibody-based agents. The approach has the potential to halt the process of Parkinson’s disease progression.
Abeliovich, Asa, and Aaron D. Gitler. "Defects in trafficking bridge Parkinson's disease pathology and genetics." Nature539.7628 (2016): 207.
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