総説
神経変性疾患における銅・亜鉛スーパーオキシドディスムターゼのミスフォールディング
2020 年 60 巻 6 号 p. 338-341
詳細
2020 年 60 巻 6 号 p. 338-341
Mutations in the gene coding Cu/Zn-superoxide dismutase (SOD1) are known to cause amyotrophic lateral sclerosis (ALS), a neurodegenerative disease with no cures. SOD1 is a highly stable enzyme where copper and zinc ions bind and a disulfide bond forms, but is also known to accumulate as misfolded forms in spinal motoneurons of ALS. A key to understand such pathological changes in SOD1 is the contribution of metal binding as well as disulfide formation to the conformational stability of SOD1. In this review, I will summarize mechanisms of SOD1 misfolding in ALS where the metal binding and/or disulfide formation go awry.
