( an antioxidant enzyme that protects ce...)Boffins a Step Closer to Solving Puzzle of Lou Gehrig's Disease,Health

an antioxidant enzyme that protects cells from free radicals, unstable atoms or molecules that can cause cell damage. The link with ALS came when researchers sequenced the genes of people who have the inherited form of ALS and found that some of them have mutations in the gene that codes for this enzyme. While the inherited form represents only a fraction of all ALS cases, this marked the first time there was any indication of a cause for any form of ALS, Valentine said.

"We studied what happens to the protein if you have the metals, if you have no metals and if you have part of the metals," she said.

The research of the UCLA-University of Florence team has indicated it is the metal-free protein that is likely to be toxic. The protein misfolds when the copper and zinc are not present, but folds properly when they are there.

"Before copper and zinc are inserted, the protein can misfold under physiological conditions," Valentine said.

There is evidence that ALS is associated with this misfolding of the protein, which becomes toxic in some way that is not known and has properties similar to misfolded proteins associated with other neuro-degenerative disorders like Alzheimer's and Parkinson's diseases, Valentine said.

Is there a way to slow down this process to give the cell more time to eliminate the misfolded proteins in all of these diseases" Would a strategy to reduce or prevent protein misfolding work against these and other diseases" These are avenues for further investigation by researchers.

When Valentine first began working on copper-zinc superoxide dismutase, she was not a biochemist but a biological inorganic chemist and hardly knew what ALS was. She was interested in the enzyme, which is unique in that it has copper and zinc so close together.

Her laboratory isolated and characterized the enzyme, but Valentine was less interested in its biological properties t
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