Parkinson disease constitutes one of the synaptopathic diseases induced through synapse defects. The condition refers to a neurodegenerative ailment associated with aggregation and misfolding of the alpha-synuclein protein of the brain. Breydo, Wu, and Uversky, 2017 define alpha-synuclein as a protein that triggers proper functioning of the brain. Alpha-synuclein role in the health is however not known and is a major area of concern to many researchers. The protein arouses a lot of interest not for anything tangible; but due to its constituent components; protein clumps and Lewy bodies which are the pathological hallmark of Parkinson’s condition (Sharma, 2018)
Such that since the discovery of alpha-synuclein protein, studies have focused to unravel the relationship between alpha-synuclein and Parkinson’s disease. The studies have focused on examining the role played by the protein in Parkinson’s disease. Along the spinning wheel of time, some scientists have managed to present evidence linking alpha-synuclein protein with the said condition, both in familial and sporadic scenarios (Rocha, De Miranda, and Sanders, 2018)
For a tentative population, research affirms that hereditary variability in the alpha-synuclein gene supports the emergence of the condition. In dismal cases of Parkinson’s disease, the alpha-synuclein genes are said to be harmful and toxic to the brain cells, by their act of secreting a lot of alpha-synuclein protein, which induces brains neuron dysfunction. Additionally, Mayer et al., 2017pinpoints out that alpha-synuclein is the basic constituent of Lewy bodies. This, therefore, is a suggestion that protein aggregation contributes to the basketry of sporadic Parkinson’s disease.
Grassi et al., 2018 observe that pathological concentration of alpha-synuclein along the brain is a potential neuropathological hallmark of Parkinson’s disease. Research compels that alpha-synuclein protein can spread from infected tissues to the healthy ones, which indeed keep on worsening the condition.
Alpha-synuclein proteins can induce toxicity to the brain cells and thus disrupting the regular distribution of synaptic vesicles and proteins membranes, and therefore leading to perforation of plasma membranes. When the plasma membranes are perforated, cellular responses are invoked which consequently cause cellular death in the body system. Moreover, the alpha-synuclein gene structure is dependent upon the membrane interactions which can speed up to hamper fibril formation.
Moreover, dysfunctional lysosomal clearance models with the body lead to the concentration of soluble alpha-synuclein oligomers which will build a base for the development of Parkinson’s disease. People with heterozygous lysosomal hydrolase mutation are 75% prone to contact sporadic Parkinson’s disease. In scientific studies, there has been an established link between alpha-synuclein aggregation and functional GCase (Doppler et al., 2016)
The premise as to whether alpha-synuclein is attached along in the mitochondria is scientifically controversial. The contemporary studies exhibit that alpha-synuclein is able to interrupt the mitochondrial protein import process in Parkinson’s disease. This finding shows the potential emergence of neurodegenerative conditions amidst the interactions between mitochondrial proteins and alpha-synuclein proteins.
Cellular functions such as cell metabolism and intracellular transport are highly dependent on microtubule changes of the cytoskeleton, which is a major component of tubulin. Rocha, De Miranda and Sanders, 2018, established that alpha-synuclein does interact with tubulin. The scholars also demonstrated that exposure to exogenous alpha-synuclein can missense gene mutations and impair microtubule verses kinesin interactions, thereby disorienting cytoskeletal motility. Additionally, many more researchers have established that tubulin is able to induce the formation of the alpha-synuclein fibril. All these studies offer a logical insinuation of the link between alpha-synuclein and the tragic Parkinson’s disease.
The specific role of the different forms of alpha-synuclein proteins in the study of Parkinson’ disease is unclear. However, the empirical studies from different cell-culture and animal experiments ranging from human patients have given a clear implication about the contributions alpha-synuclein protein to the development of Parkinson’s disease. With her peculiar nature, alpha-synuclein can react with anionic lipids which consequently will induce conformational changes of Parkinson’s condition. In reaction, the aggregate forms of soluble alpha-synuclein will affect the normal operations of both lysosomes and mitochondria, leading to Parkinson’s disease.
As presented above, the mastery of the genesis of Parkinson’s disease and the contributive factors to its development is critical towards the finding of a therapy for the same. As a hazardous condition infringing many people, there is a constant need for the scientific application to ensure the innovation of sound therapies, to bring the condition to a halt.
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