December 26, 2019
Keio University
Institute for Molecular Science
Associate Professor Yoshiaki Furukawa and Assistant Professor Eiichi Tokuda (at the time of the research; currently Senior Assistant Professor at the College of Pharmacy, Nihon University) of the Keio University Faculty of Science and Technology, and Itsuki Anzai (completed his doctoral program in 2019) of the Graduate School of Science and Technology, in a joint research project with Professor Hidemi Misawa of the Keio University Faculty of Pharmacy and Professor Shuji Akiyama of the Institute for Molecular Science, National Institutes of Natural Sciences, have proposed a new mechanism by which the three-dimensional structure of the copper- and zinc-binding protein SOD1, which is involved in the onset of amyotrophic lateral sclerosis (ALS), becomes abnormal. It has been suggested that when mutations occur in the gene encoding SOD1, SOD1 with an abnormal three-dimensional structure accumulates in motor neurons, causing the onset of ALS. Although it is not yet clear what triggers the structural abnormality of SOD1, the researchers found that when copper and zinc ions dissociate from oxidized SOD1, it transforms into a toxic, abnormal structure. Given that increased oxidative stress and abnormal metal ion dynamics have been reported in many ALS patients, the proposal in this study is important for understanding the pathogenesis of ALS involving SOD1.
These research findings were obtained with support from programs such as the Grant-in-Aid for Scientific Research on Innovative Areas "Life Metal Science" from the Ministry of Education, Culture, Sports, Science and Technology (MEXT) and the Keio University Program for Promoting Core Projects (within Keio grant), and were published online in the international scientific journal Free Radical Biology and Medicine on December 19, 2019.
Please see below for the full press release.