JUPITER, FL, January 5, 2011 A scientist from the Florida campus of The Scripps Research Institute has devised a new method of analyzing and quantifying changes in proteins that result from a common chemical process. The new findings could provide new insights into the effects of a highly destructive form of stress on proteins in various disease models, particularly cancer.
The study, published January 5, 2011, in the online Early View of the journal Angewandte Chemie, was designated by the journal as a "very important paper," a distinction bestowed on less than five percent of its publications.
"This new technique allows us to home in on which proteins are modified to a significant extent during periods of stress and how that changes during disease progression," said Kate Carroll, an associate professor in the Scripps Research Department of Chemistry who conducted the study with Young Ho Seo, a research fellow at The University of Michigan. "It gives us the chance to look more closely at targets for possible therapeutic intervention. From a practical standpoint, the technique is simple and will be accessible to biologists and chemists alike."
The new technique focuses on the process of cysteine S-hydroxylation, which plays a significant role in a number of events related to physiology in both health and disease, including the regulation of signaling proteins in various disease states.
The ability of the new technique to focus on signaling pathways, particularly in diseases such as cancer, is critical.
"Chronic disease states such as cancer can involve the modification of signaling proteins through S-hydroxylation, but other housekeeping proteins may also be targets," she said. "Key to distinguishing which of these proteins may be involved in pathogenesis is the ability to measure the amount of S-hydroxylation at specific sites within a protein. Now you'll be able to tell. This should help accelerate target i
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Scripps Research Institute