Insights from their study might present a novel therapeutic method for diseases such as Huntington’s and Parkinson’s.
Associate Professor Roger Pocock, from the Monash Biomedicine Discovery Institute (BDI), and colleagues from the University of Cambridge led by Professor David Rubinsztein, discovered that microRNAs are vital in controlling protein aggregates, proteins which have amassed because of a malfunction within the process of ‘folding’ that determines their shape. Their findings had been published in eLife today.
MicroRNAs, quick strands of genetic materials, are tiny, however powerful molecules that regulate many alternative genes simultaneously. The scientists sought to determine particular microRNAs which are essential for regulating protein aggregates and homed in on miR-1, which is present in low ranges in patients with neurodegenerative diseases such as Parkinson’s disease.
The researchers then confirmed that miR-1 helped defend towards poisonous protein aggregates by controlling the expression of the TBC-7 protein in worms. This protein regulates the method of autophagy, the body’s method of removing and recycling damaged cells, and is essential for clearing poisonous proteins from cells. Professor Rubinsztein then performed analysis, which showed that the same microRNA regulates a related pathway to manage autophagy in human cells.
Further work by Associate Professor Pocock’s colleagues confirmed that when human cells are equipped with a molecule known as interferon-b, the miR-1 pathway is upregulated, revealing a method of manipulating it.
The researchers have provisionally patented their findings and are in discussions with pharmaceutical firms about translating the analysis. They are going to additionally take a look at it in preclinical models for Huntington’s and Parkinson’s disease.