Cell: a natural cellular mechanism to reverse protein aggregation

When you beat an egg in a pan, it only takes a few minutes for the egg white to change from a transparent mucus state to a elastic white solid, and the yolk also gradually hardens A series of physiological and chemical changes lead to the breaking of chemical bonds in the egg, the aggregation and remodeling of proteins, and you get an irreversible solid fried egg   It's easy to go from raw eggs to cooked eggs, but it's not reversible Scientists at Tel Aviv University (tau) have discovered the secret cellular pathway by which cells break "human common sense" Using natural mechanisms to reverse protein aggregation can have positive physiological effects on diseased cells, such as curing Alzheimer's disease, Parkinson's disease and mad cow disease   Professor Martin kupiec of tau School of molecular cell biology and biotechnology and research team led by Dr Kobi Simpson Lavy published the latest article in molecular cell   "The executors of most cell functions are proteins, and if they aggregate into blobs, they will be inactivated," Professor kupiec said "As we age, the propensity for protein aggregation increases, and so do various diseases, such as neurodegenerative diseases."
"In addition, when proteins misfold, cells try to unravel clumps or pile them up in other places of cells to reduce toxicity, they are also prone to malfunction, leading to the development of diseases such as Alzheimer's disease," Dr Simpson Lavy said   When Dr Simpson Lavy studied glucose metabolism in yeast cells, he stumbled upon the fact that when glucose was added to the cell culture medium, the labeled std1 protein formed a bright spot outside the cell nucleus However, std1 is usually located in the nucleus Why does it aggregate outside the nucleus?
"We want to know if protein aggregation is caused by changes in the microenvironment of cells," said Professor kupiec "Then, when the glucose in the cell was depleted, we observed that the protein aggregates disappeared and the std1 protein returned to the nucleus Therefore, we know that the accumulation of std1 protein represents the response of cells to the change of sugar content in culture medium, and its aggregation and dissolution enable cells to regulate their own gene expression according to the sugar concentration in the environment "
This study demonstrates that not all protein aggregation is harmful In this paper, the researchers found that the primary function of molecular chaperones in many neurodegenerative diseases may be involved in the regulation of non pathological protein accumulation   "In the future, we seem to be able to use this reversible pathway to change protein aggregation," Professor kupiec said "If we find an effective way to transform irreversible aggregation into reversible aggregation, we can really cure neurodegenerative diseases For example, it's like having an omelet reshape an egg "
At present, researchers are investigating the underlying causes of protein behavior changes under different conditions.