The ALS Association

Ice Bucket Challenge Progress

New Research Points to Common Cause of ALS

August 22, 2011

According to an article in the journal Nature, investigators from Northwestern University Feinberg School of Medicine have identified a new gene linked to familial ALS involved in the processing of accumulated proteins.  This provides further support for abnormal protein handling as an underlying cause of ALS.

Optimal functioning of the neurons relies on efficient recycling of the protein building blocks in the cells.  In ALS, it appears that the recycling system is abnormal.  The cell can’t repair or maintain itself and becomes severely damaged.  According to researchers, this breakdown occurs in all three forms of ALS: hereditary, which is called familial; ALS that is not hereditary, called sporadic; and ALS that targets the brain, ALS/dementia.  Investigators have identified this new gene change in familial ALS with and without frontotemporal dementia.

This discovery provides further evidence that protein mishandling is a common target for ALS and important for the development of new therapies.  Senior author Teepu Siddique, M.D., the Les Turner ALS Foundation/Herbert C. Wenske Professor of the Davee Department of Neurology and Clinical Neurosciences at Northwestern’s Feinberg School and a neurologist at Northwestern Memorial Hospital emphasized the significance of this finding bringing us closer to identifying new compounds regulating this pathway to slow or reverse disease progression in ALS.

“The identification of a new gene linked to familial ALS known to be involved in protein handling of the cell will open up a new avenue of research and bring us closer to understanding this process and what goes wrong in the disease,” commented ALS Association Chief Scientist Lucie Bruijn, Ph.D.  “We look forward to follow-on studies that bring us closer to effective therapy for the disease.”

The discovery of the breakdown in protein recycling may also have a wider role in other neurodegenerative diseases such as:  Alzheimer’s disease and frontotemporal dementia as well as Parkinson’s disease, all of which are characterized by aggregations of proteins.  The removal of damaged or misfolded proteins is critical for optimal cell functioning.

Han-Xiang Deng, M.D., lead author of the paper and associate professor of neurology at the Feinberg School, commented that the study provides robust evidence that a defect in the protein degradation pathway causes neurodegenerative disease.

Visit to read the article in Nature, visit to read a related article from the Motor Neuron Disease Association, and visit,0,6531848.story to see an article in the Chicago Tribune.

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