University of Michigan LogoThere is a lot of buildup about beneficial oxidants in everything from face cream to cereal bars. One would be of the opinion that their target i.e. oxygen radicals are not good at all. Well, it’s supposedly true. The increase of oxygen radicals and other reactive oxygen species (ROS) in cells may add to aging and maybe even diseases such as cancer and Alzheimer’s. But in moderate amounts, ROS may also assist in keeping cells in good shape by controlling cell division, movement and other normal biological processes.

A research was conducted at the University of Michigan led by chemical biologist Kate Caroll. The research aimed to better comprehend the role of ROS in disease and the need to discover how ROS functions in healthy cells. The research provided a vital tool for that.

The tool is a small molecule known as DAz-2. It functions something like a subcellular GPS and assists the researchers home in on the particular proteins that ROS affect. Oxidation is a chemical modification process through which cells of all organisms from bacteria and yeast to humans apparently sense ROS. It influences how proteins communicate with each other.

Kate Carroll, assistant professor of chemistry and a research assistant professor in the Life Sciences Institute, commented, “While this overall phenomenon is widely accepted, scientists are still working to identify exactly which proteins are affected by ROS in living cells.”

Apparently which proteins may have been altered and exactly how and where the alteration takes place has been stalled by the lack of tools. But Carroll’s group has supposedly developed a series of chemical investigations for that purpose, of which DAz-2 is the most recent.

Carroll mentioned, “The new probes allow us to easily sort the proteins we want to analyze and study from other proteins that aren’t modified by ROS.”

Particularly, DAz-2 monitors the oxidation of the protein building block cysteine to sulfenic acid, which may control how proteins behave and connect with other proteins. Because the alteration of cysteine to sulfenic acid is so brief, it may have been hard to examine, and only lately had the scientists identified that only a few proteins experience this kind of oxidation. But by means of DAz-2, which may straightaway identify sulfenic acid in living cells, Carroll’s group has apparently recognized more than 190 proteins, involved in diverse biological processes, which may go through this variation.

Carroll is of the opinion that this tool may allow investigation of the oxidation of proteins in cellular signaling and many disease states, leading to greater understanding of how these processes operate. These findings may pave the way for new therapeutic strategies to fight diseases that involve chronic oxidative stress and may lead to a better overall understanding of how cells work.

This research was published in the journal ACS Chemical Biology.