[excerpt] To function properly, proteins must fold into their proper shape.
All proteins are simple chains of amino acids that coil into specific shapes to perform their biological function.
In the folding process, proteins are assisted by molecular chaperones that function to prevent misfolding or, in the case of already misfolded proteins, to detect them and prevent their accumulation.
Faulty proteins have been implicated in such neurodegenerative diseases as Huntington's, Parkinson's and Alzheimer's.
Morimoto and colleagues have shown that elevated levels of molecular chaperones promote longevity.
The researchers focused on a master protein called heat shock factor.
This master protein responds to stressors by turning on genes that encode for molecular chaperones.
To better understand this process, Morimoto and colleagues studied Caenorhabditis elegans, a transparent roundworm used widely in genetics experiments.
C. elegans is particularly suited to genetic studies because its biochemical environment is similar to that of humans and its genome has been sequenced.
Morimoto and colleagues found that when heat shock factor was underexpressed in adult roundworms, longevity was suppressed. But when it was overexpressed, their lifespan increased, suggesting that heat shock factor has significant benefits.
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