May 27, 2009

ALS study focuses on metal interaction

Researchers at the University of Texas have identified an abnormality in molecules they believe is responsible for one form of Lou Gehrig's disease.

The molecules, known as immature superoxide dismutase 1 or SOD1, can't interact normally with metals that provide stability and instead become destructive knots that are seen in one inherited form of amyotrophic lateral sclerosis, the formal name of Lou Gehrig's disease, the University of Texas Health Science Center at San Antonio reports.

The center's research, published in the journal Biochemistry, may shed new light on what triggers ALS, says lead author Duane Winkler.

His observations were made after examining new 3-dimensional images of the abnormal molecules in the center's X-ray crystallography lab.

More than 100 mutations are known to impair the function of SOD1 molecules.

The Texas study focused on mutations that prevent the molecule from interacting normally with a second molecule called CCS, short for copper chaperone for SODI.

Winkler says CCS is like a waiter serving up orders of copper and zinc.