These properties account for 69% of longevitiy in patients with the familiar version of disease, according to PLOS Biology paper.



A group of researchers attribute longevity in amyotrophic lateral sclerosis (ALS) patients to a couple of properties of the SOD1 protein. They report that both the stickiness of SOD1 and its decreased stability account for 69% of survival data from familial ALS. This provides evidence that SOD1 stability and its aggregation propensity are the main toxic causes of ALS.


SOD1 is an enzyme that neutralizes potentially dangerous molecules, but ALS-causing mutant enzymes gain an unknown toxic function.


It has been shown that in about 20% of ALS patients who have a family history of ALS, the underlying mutation causing the disease is a change in the gene for SOD1, according to the scientists. SOD1 has been shown to be mutated in at least 119 different ways in different ALS patients.


The current study looked at the difference in disease progression in patients with differing mutations. The team found that those mutations that made SOD1 more likely to unfold from its normal structure, and those that made it more likely that SOD1 would stick to other unfolded SOD1 molecules correlated with reduced survival times post disease onset


The research was conducted by investigators at Brandeis University and Brigham and Women’s Hospital Results appear in this week’s issue of PLoS Biology.