Establishing a new strategy to fight Huntington’s disease — ScienceDaily
Through an international joint research effort involving ProQR Therapeutics from the Netherlands, Université Grenoble Alpes from France and the KTH Royal Institute of Technology from Sweden, the research team of Professor Ji-Soon Song from the Department of Biological and from the KAIST Institute for BioCentury of KAIST, established a noble strategy to treat Huntington’s disease. The new work has shown that the protein converted from the disease form to its disease-free form retains its original function, providing new hurdles to tackle Huntington’s disease.
This research, titled “Huntingtin isoform resistant to antisense oligonucleotide-induced pathogen proteolysis maintains huntingtin function,” co-authored by Hyeongju Kim, was published in the online edition of Journal of Clinical Investigation on August 9, 2022.
Huntington’s disease is a dominantly inherited neurodegenerative disease and is caused by a mutation in a protein called ‘huntingtin’, which adds to the protein a distinctive feature of an extended stretch of glutamine amino acids called polyglutamine. It is estimated that one in 10,000 people has Huntington’s disease in the United States. Patients would suffer a decade of regression before death, and so far there is no known cure for the disease.
Cleavage near stretched polyglutamine in mutated huntingtin is known to be the cause of Huntington’s disease. However, because the huntingtin protein is necessary for normal brain development and function, it is essential to specifically eliminate the disease-causing protein while maintaining those that still function normally. The research team showed that huntingtin delta 12, the converted form of huntingtin that resists developing cleavages at the ends of the protein, the known cause of Huntington’s disease (HD), relieved symptoms of the disease while maintaining normal huntingtin functions.
This work was supported by a Global Research Lab grant from the National Research Foundation of Korea (NRF) and a EUREKA Eurostars 2 grant from the European Union Horizon 2020.
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Materials provided by Korea Advanced Institute of Science and Technology (KAIST). Note: Content may be edited for style and length.