Surprising findings about the genetic aberrations that cause Huntington and other neurodegenerative diseases have opened potential new routes to treatment of the conditions, German researchers report in
Franz-Ulrich Hartl, from the Max Planck Institute of Biochemistry, and colleagues found that the toxicity of expanded polyglutamine (polyQ) tracts—aberrant numbers of trinucleotide repeats in unrelated genes—arises from the soluble forms of the protein, and not their aggregates. In addition, they explained the mechanism by which molecular chaperones—a cellular defence against misfolded proteins—could modulate the disease process, suggesting future potential for therapy.
"I think our results suggest clearly that if we were able to increase the cellular capacity of the chaperone machinery, we could potentially interfere with the toxicity of these polyQ expanded proteins and perhaps other misfolded proteins," Hartl told
One suggestion for why polyQ expansion proteins are toxic to cells was that they caused aggregates to form ...
