-Published a thesis in ‘Neuron’, the most prestigious journal in the field of neuroscience, a sister paper of Cell
-Collaboration with Parkinson’s disease world authority, Johns Hopkins University Professor Ted Dawson and Koh Han-seok, US “Expectation” to develop a drug that can prevent and treat the aggregation of synuclein, a major cause of Parkinson’s disease
[베리타스알파=신승희 기자] Dong-A University announced on the 6th that a research team led by Professor Dong-Hoon Kim of the Department of Pharmacology at the College of Medicine (Department of Translational Science, Graduate School) achieved research results to discover ‘TRIP12’, a regulatory protein of GCase, a risk factor for inducing Parkinson’s disease.
Professor Kim published a paper in the December issue of ‘Neuron’ in collaboration with Professor Ted Dawson, a world authority on Parkinson’s disease research, Johns Hopkins University Professor, and Johns Hopkins University Professor Koh Han-seok. ‘Neuron’ is a sister paper of ‘Cell’ and is the most prestigious journal in the field of neuroscience.
The title of this paper is ‘TRIP12 ubiquitination of glucocerebrosidase contributes to neurodegeneration in Parkinson’s disease.
The research team found that ‘TRIP12’ ubiquitin-linking enzyme plays a decisive role in the regulation of lysosomal protein ‘GCase’ in Parkinson’s disease using various experimental techniques.
Based on this achievement, the research team is planning to develop a drug that can control the decrease in GCase expression caused by TRIP12, prevent aggregation of synuclein, and treat Parkinson’s disease.
Parkinson’s disease is the second most common degenerative brain disease after Alzheimer’s disease. It is caused by the death of dopaminergic neurons in the substantia nigra region of the midbrain, and is characterized by severe trembling of the hands and feet due to a problem in muscle control.
Through previous studies, abnormal aggregation of the neuroprotein ‘synuclein’ in dopaminergic neurons was found to be the main cause of Parkinson’s disease. As the main causes of synuclein aggregation, decreased expression and dysfunction of the lysosomal protein GCase, which helps to clear unnecessary proteins in cells, have emerged, but the exact mechanism has not been studied.
Professor Kim’s research team found that TRIP12 expression was abnormally elevated in Parkinson’s disease cell and animal models, and GCase ubiquitination through TRIP12 (ubiquitination, the process of attaching ubiquitin, a small protein found in almost all tissues of eukaryotes to other proteins) and It has been verified that degradation through the proteasome (a large protein complex that degrades proteins present in cells) significantly reduces the amount of GCase.
The research team also found that abnormal aggregation of synuclein and the death of dopaminergic neurons occur through this mechanism.
Professor Kim said, “This was a research I started while I was doing my postdoctoral course at Johns Hopkins University, and I was able to finish it with the help of several professors including Dean Hwan-Tae Park of Dong-A University College of Medicine.”
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