A protein called alpha-synuclein is found to be adversely affecting both the health and movement of mitochondria. This protein is linked to Parkinson's Disease.
A Medical Express report specified that within cells, organelles, also known as mitochondria, perform various important tasks. Such structures are generating energy, not to mention helping keep the interior environment of the cells, in a healthy equilibrium state, among other tasks.
The results came from experiments engaging genetically engineered fruit fly larvae. Such genetic engineering was conducted for the production of remarkably high protein amounts, also known as alpha-synuclein.
According to biological sciences associate professor Shermali Gunawardena, Ph.D., from the University of Buffalo College of Arts and Sciences, when fruit fly larvae expressed the said protein at high levels, akin to what is observed in Parkinson's disease, many of the mitochondria they observed turned unhealthy, and a lot became disjointed.
Alpha-Synuclein Responsible for the Problems
Through detailed investigations, the study authors also discovered the different parts of the alpha-synuclein protein appear to be accountable for the said two problems and that the latter-mentioned can, in fact, be healthy.
Gunawardena explained that they consider their discovery a key finding since before, people thought fragmented or disjointed mitochondria were unhealthy.
The outcomes could be of interest in the context of developing drugs, as irregular aggregates of the said protein in brain cells are a trademark of Parkinson's disease, and mitochondrial impairment has also been seen in patients.
TJ Krzystek, UB Ph.D. candidate in biological sciences said, this particular study showcases the benefit of using fruit fly larvae as a model organism to examine how neurons turn impaired during devastating illnesses like Parkinson's disease.
Protein for Improving Mitochondrial Health in Parkinson's Patients
Even though this approach, Krzystek explained, they pieced together a new insight into how the protein alpha-synuclein associated with Parkinson's disease disrupts the health and movement of mitochondria, the epicenter for the production of energy in cells.
Krzystek added they believe the study emphasizes a promising path that can be discovered for possible therapeutics targeted at enhancing mitochondrial health in Parkinson's patients.
The study, Differential mitochondrial roles for α-synuclein in DRP1-dependent fission and PINK1/Parkin-mediated oxidation, was published in the Cell Death and Disease journal.
Interactions Between the Protein and Mitochondria
Through series of tests in fruit fly larvae, the scientists were able to tease out complicated details about interactions between mitochondria and alpha-synuclein.
For instance, according to a similar report from The Wyoming News Station, the research not just concludes that different sections of the alpha-synuclein protein are possibly responsible for resulting in mitochondrial fragmentation and impairing mitochondrial health.
Furthermore, the study has identified such sections and describes how other proteins may have interacted with them to initiate the changes.
Scientists explain proteins PINK1 and Parkin, in particular, both associated with Parkinson's disease, may interrelate with one end of alpha-synuclein to impact mitochondrial health, whereas DRP1 protein may interact with the other end to disrupt mitochondria.
The study's co-first author, Rupkatha Banerjee, Ph.D., explained mitochondrial damages have long been associated with Parkinson's disease's pathogenesis.
Nonetheless, alpha-synuclein's role in mitochondrial quality control thus far has not been extensively investigated. This research untangles the complicated molecular mechanisms wherein various regions of the protein exert unique impacts on mitochondrial health, which brings into light a possible pathway that could be aimed at discovering new treatment interventions in Parkinson's disease.
Related information about alpha-synuclein and Parkinson's disease is shown on Parkinson's UK's YouTube video below:
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