The facility will make it possible to examine whether antioxidants help to stop aging or rather the opposite, as recent studies show
With all the publicity about the benefits of antioxidants in various products, from face cream to breakfast cereal, we are supposed to think that their targets - oxygen radicals - must be extremely harmful. This is indeed true - the accumulation of oxygen radicals and other reactive oxygen species (ROS) in cells contributes to the acceleration of their aging and probably also to the development of diseases such as cancer and Alzheimer's.
At the same time, in moderate doses, these forms help the health of the cell through the control of cell division, its movement and other biological processes that occur in it. In order to better understand the activity of these forms in diseases, scientists first need to examine how they work in healthy cells, and a research team from the University of Michigan provides an important new tool for just that.
The new tool, a small device known as DAz-2, functions as an intracellular GPS that helps researchers pinpoint the specific proteins affected by these changes. The cells of all organisms, from bacteria and yeast to humans, sense these forms through a process of chemical change known as oxidation, which affects the type of reaction of the proteins one with another.
"Although this general phenomenon is accepted by the global scientific community, scientists are still trying to get a precise identification of the proteins affected by these changes in living cells," says researcher Carroll, professor of chemistry in the University's Institute of Life Sciences. Locating the affected proteins, and knowing the exact change and its location have been limited until now due to the lack of reliable tools, but this has changed thanks to the development of a series of chemical detectors for this purpose, with the DAz-2 isolate being the latest in the series. "The new detectors allow us to easily sort the proteins that we are interested in examining and compare them to proteins that are not affected by these forms," explains the researcher.
In particular, the detector in question detects the oxidation of the protein structure unit (the amino acid) cysteine to sulfenic acid, which is able to control the behavior of the proteins and their interactions. Because the change of cysteine to sulfonic acid is so temporary, until now it has been extremely difficult to observe and scientists have located only a few proteins that have undergone such oxidation. However, by using the new detector, which directly detects the sulfonic acid in living cells, the research team was able to identify close to two hundred proteins involved in diverse biological processes, which undergo this change.
"This tool will enable a reliable study of the oxidation of the proteins used in cellular signaling processes and involved in many diseases, while gaining a greater understanding of the mechanism of their activity," explains the researcher. "These findings could pave the way for the development of innovative healing approaches to combat diseases related to prolonged oxidative stress, and for a better understanding of cell activity."
The findings were published at the beginning of this year in the scientific journal Chemistry & Biology.
