Whether it?s an unhealthy diet, childhood allergic reaction to a bee sting, or just breathing too much city smog, your cells keep track of your life.
Researchers at Johns Hopkins took advantage of a new technique that reads the makeup of proteins created by the body to identify chemical changes that nature makes to them.
“You could say [these proteins] keep a record of what has happened to them,” said Phil Cole, pharmacology department head at Johns Hopkins Medical Institute.
They published their findings in February, and in March posted an online database of the so-called phosphorylation events, including work done by others around the world. Some types of phosphorylation can cause diseases, including cancers, according to a Johns Hopkins release, so identifying them is a first step towards prevention, cures or therapies.
“Finding so many at one time is a huge advance,” said Dr. Akhilesh Pandey, associate professor at the McKusick-Nathans Institute of Genetic Medicine at Hopkins, in a statement. “What we have here is about 20 years? worth of lots of work in one searchable list.”
A report on their work was published in the Proceedings of the National Academy of Sciences. The database information appeared in Nature Biotechnology.
They accomplished the task using a technology which bombards the proteins with electrons in order to gently break them down into charged particles. According to the article, they sorted those particles by size and identifies them based on mass ? their size and weight. The process breaks up proteins more gently than previous methods while keeping chemical alterations like phosphorylation intact.
Working with human kidney cells, the Johns Hopkins team fished out the thousands of different proteins and analyzed them, identifying 1,435 phosphorylations. Comparing these 1,435 to 20 years of published data, they discovered about 80 percentof what they found never had been reported.
The team also constructed an online search tool, PhosphoMotif Finder, to allow any researcher to find potential phosphorylation sites in any protein of interest.
