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Scientists Identify Protein That Plays Crucial Role in Lou Gehrig's Disease
ALS is a fatal neurodegenerative disease caused by the death of motor neurons in the brain and spinal cord that control muscle movements from walking and swallowing to breathing.
Since the last three years, Brandeis chemist Jeff Agar and his colleagues have studied the rare, familial form of ALS (fALS) as a window into the sporadic form of ALS, which accounts for 90 percent of all cases. Fifteen years ago it was discovered that mutations in the gene that makes the protein, superoxide dismutase, are responsible for inherited ALS, but how they lead to ALS is still a mystery.
Knowledge about the mechanisms at work in inherited ALS will clear the way to understanding and treating sporadic ALS as clinical symptoms are identical in both forms of the disease.
In this research it was demonstrated that fALS is caused by two synergistic properties of the protein superoxide dismutase, creating toxic levels of the protein in motor neurons.
"We discovered that increased protein unfolding and the propensity of the proteins to aggregate, (to clump together) are the major factors in the familial form of ALS," explained Agar.
This propensity of proteins to unfold and clump together amounts to what scientists call a ''toxic gain of function, in which a protein takes on a new role, unrelated to the one it is supposed to perform in healthy cells.
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