NYC Healthcare News



Common soluble proteins become insoluble and form aggregates while aging: Study

October 25, 2015

They identified roughly 700 proteins in a C. elegans worm that become insoluble as the animal ages. These insoluble proteins are highly over-represented in the aggregates found in human neurodegeneration, the researchers wrote in their paper. They found that many of the proteins that became insoluble were already known to accelerate the aging process and to influence the aggregation of the major disease proteins. Yet even in the healthy aging worms, these proteins had a propensity for clumping and forming hard, rocklike structures.

The team found that this aggregation was significantly delayed or even halted by reducing insulin and IGF-1 hormone activity, whose reduction is known to extend animal lifespan and to delay the progression of Huntington's and Alzheimer's disease in animal models of neurodegenerative diseases.

While there are indisputable differences between worms and men, the roundworm C. elegans (Caenorhabditis elegans) often has led the way in advancing our understanding of human biology, notably in such areas as the mechanism of cell death, insulin pathways, the genes involved in cancer, and aging.

Some of those advances have originated in Kenyon's lab, including the discovery that blocking the activity of a single gene in C. elegans doubled the animal's lifespan. The gene, known as daf-2, encodes a receptor for insulin as well as for IGF-1. The same or related hormone pathways have since been shown to affect lifespan in fruit flies and mice, and are thought to influence lifespan in humans.

Source: University of California - San Francisco