ABSTRACT
Mutations to copper zinc superoxide dismutase (Cu,Zn SOD) were first linked in 1993 to a subset of dominantly inherited familial amyotrophic lateral sclerosis (FALS).1 No other linkage to antioxidant enzymes or defenses has yet been found in amyotrophic lateral sclerosis (ALS) in spite of extensive search.2 Recent experimental evidence strongly suggests that the mutations to Cu,Zn SOD cause some gain in enzymatic function rather than a loss of antioxidant function.}-~
The familial form of ALS, which is usually inherited as an autosomal dominant trait, accounts for approximately 10% of all ALS cases. In about 12% of FALS families, a structural mutation in Cu,Zn SOD can be identified.1 Carriers express the mutated gene throughout life and are generally healthy until disease onset. After diagnosis the disease progresses rapidly, with death occurring in an average of 5 years.
