Parkinson’s linked protein has negative impact on mitochondria; Study

By Shilpa Annie Joseph, Official Reporter
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A recent study has revealed that a protein called alpha-synuclein, which has been associated with Parkinson’s disease, has a negative impact on mitochondria and aids in the progression of the condition.

The US-based University of Buffalo (UB) researchers conducted the study titled “Differential mitochondrial roles for alpha-synuclein in DRP1-dependent fission and PINK1/Parkin-mediated oxidation” to find the connection. The study was published in the journal Cell Death and Disease.

According to the reports, “Alpha-synuclein is a soluble, natively unfolded cytosolic protein that becomes structured when bound to phospholipids. Although the protein lacks a true mitochondrial localization sequence, previous studies suggest that alpha-synuclein contains a cryptic mitochondrial targeting sequence that can facilitate anchoring alpha-synuclein to mitochondrial membranes.”

The researchers expect that these discoveries may aid in the development of medications for Parkinson’s disease, a disorder of the central nervous system that hampers movement, and is characterized by tremors.

The experiment was carried out on fruit fly larvae that had been genetically modified to produce abnormally high levels of alpha-synuclein, according to the reports.

Dr. Shermali Gunawardena
Dr. Shermali Gunawardena
Assoc. Professor – Biological Sciences

“When fruit fly larvae expressed alpha-synuclein at elevated levels similar to what is seen in Parkinson’s disease, many of the mitochondria we observed became unhealthy, and many became fragmented. Through detailed experiments, we also showed that different parts of the alpha-synuclein protein seem to be responsible for these two problems and that fragmented mitochondria can be healthy. This is a key finding because before, people thought fragmented mitochondria were unhealthy mitochondria.”

Through tests in fruit fly larvae, the scientists were able to tease out intricate details regarding interactions between alpha-synuclein and mitochondria. They found that different sections of the alpha-synuclein protein are likely responsible for causing mitochondrial fragmentation and damaging mitochondrial health.

The research also identified these sections and describes how other proteins may interact with them to drive these changes. More specifically, the proteins PINK1 and Parkin may engage with one end of alpha-synuclein to influence mitochondrial health, whereas DRP1 may connect with the other end to damage mitochondria, according to the researchers.

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