SPring-8, the large synchrotron radiation facility

   A research group led by Junichi Takagi (professor) of the Institute for Protein Research, Osaka University, clarified the crystal structure of a protein that “removes” a causative substance of Alzheimer’s disease. In many neurodegenerative diseases such as Alzheimer’s disease, fibrillar aggregates called amyloid fibers generated in the brain destroy nerve cells, leading to brain dysfunction. Because the aggregates are accumulated in the brain over a long period, it is difficult to remove such aggregates once accumulation has started. A treatment method that prevents the accumulation of aggregates is considered necessary.

This group previously reported that a membrane protein in the brain called sorLA prevents the accumulation of amyloid beta (Aβ) (a component of amyloid plaques) by trapping newly formed Aβ and transporting it to a degradation system. The research group has succeeded in solving the crystal structure of sorLA that traps Aβ, by using BL44XU at SPring-8. The findings of this study are attracting much attention because the inherited mechanism of protection against Alzheimer’s disease in the human body is clarified. The achievements of this study were published on 2 February 2015 in the British scientific journal Nature Structural & Molecular Biology.