Toxic aggregates of misfolded proteins are a hallmark of many neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS), Alzheimer’s (AD), Parkinson’s (PD), and Huntington’s (HD). A new study, published on March 13 in the journal Cell,from Adam Antebi’s laboratory at the Max Planck Institute for Biology of Ageing in Cologne, provides new insights into the quality control mechanisms that normally help protect against protein toxicity. N-acetylglucosamine, an N-linked glycan precursor, appears to be critical for preventing protein aggregates from forming and for clearing the aggregates that are already present in the cell. When this compound is added to the growth medium of distinct C. elegans models of neurotoxicity, it alleviated protein toxicity, delayed onset of paralysis, and extended lifespan. These findings suggest that activation of the hexosamine pathway by N-acetylglucosamine supplementation may be a promising avenue for therapeutic intervention in diseases associated with protein aggregate toxicity. Click here to read more.
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