Related Experiment Videos
[Familial amyotrophic lateral sclerosis associated with mutant Cu/Zn superoxide dismutase as a conformational
T Koide1, S Igarashi, K Kikugawa
1Department of Neurology, Niigata University, Japan.
Abstract:
To investigate the molecular mechanism of mutant Cu/Zn superoxide dismutase (SOD) associated with familial amyotrophic lateral sclerosis (FALS), mutant (A1a4Thr, Gly85Arg, Gly93Ala, and two base-pair deletion in the 126th codon), as well as wild-type (wt), Cu/Zn SODs were expressed in COS7 cells. The formation of granular cytoplasmic aggregates accompanied by collapse of the cytoplasm was observed in cells expressing mutant Cu/Zn SODs, but not in cells expressing mutant Cu/Zn SODs. The aggregates contained ribosome-like particles and endoplasmic reticulum. These results suggest the possibility that mutant Cu/Zn SODs promote the formation of aggregates which are toxic to cells.
Insights
Mutant copper-zinc superoxide dismutase (SOD) forms toxic cytoplasmic aggregates in cells, potentially driving familial amyotrophic lateral sclerosis (FALS) pathogenesis. This research sheds light on the molecular mechanisms underlying FALS disease progression.
Area of Science:
- Molecular Biology
- Neuroscience
- Cell Biology