April 2, 2013
WOOSTER, Ohio — Social networking may be much more than a human phenomenon. Researchers at The College of Wooster have used chemical tools to show that proteins in our cells engage in similar behavior, and have been for a much longer period of time — well before Mark Zuckerberg introduced the world to Facebook.
James West, assistant professor of biochemistry and molecular biology at Wooster, and his fellow researchers, which include several of his students, recently published a paper in the journal Chemical Research in Toxicology that delves into this intriguing process — one that occurs in every cell.
“We studied molecules that can link, or staple, proteins to other proteins,” says West. “What we found surprised us because the ‘staples’ in our experiments showed great accuracy in linking proteins that are known to interact with one another and function in a common process.” West’s team used these chemicals, known as protein cross-linkers, to determine a protein’s binding partners.
In their study, West and his fellow researchers were able to identify proteins that interact with thioredoxin, a protein that protects cells against oxidative damage by peroxides. “What we found was that thioredoxin is modified by cross-linkers just as it would be by peroxides, despite the fact that the cross-linkers and peroxides are quite different chemically,” says West. “With the cross-linkers in hand, we were able to use these tools to connect thioredoxin with its key ‘friends’ in cells.”
Cross-linking of thioredoxin and its partners renders these proteins ineffective in protecting the cells against oxidative damage. Proteins in the thioredoxin network are often present at high levels in cancers, where they decrease the levels of peroxides. As a result, targeting the thioredoxin ‘social network’ represents a potentially useful avenue for treating this disease.
Indeed, several cancer chemotherapies that West’s group studied are cross-linkers that modify thioredoxin and its binding partners. “The ability of these chemotherapies to cross-link proteins in thioredoxin networks together suggests one potential way that these molecules kill cancer cells is by inhibiting this network,” says West. “By studying these chemotherapeutic cross-linkers, we can better understand how related cancer chemotherapies might act in cells as well.”
In addition to the significance of the discovery, West was pleased that the project involved the intellectual and experimental efforts from two Wooster graduates and three current Wooster students, including Matthew Naticchia, a junior biochemistry and molecular biology major from Delaware, Ohio, who was the lead author on the paper. Also contributing to the research were Andrew Lamade, a senior biochemistry and molecular biology major from Medina, Ohio, and Rachelle Herrin, a sophomore chemistry major from Madison, Wis., as well as recent graduates Haley Brown and Samantha Justice, both of whom earned degrees in biochemistry and molecular biology last spring.
“For undergraduates and recent graduates to be involved in research at this level is quite impressive,” says West. “It speaks well of the rigor of Wooster’s curriculum, the dedication of our students, and the College’s commitment to supporting scientific research between students and faculty.”
1189 Beall Avenue, Wooster, Ohio 44691. (330) 263-2000
© Map and Directions | Employment | A to Z Index | Contact Us | Terms and Conditions | Email | ScotWeb | ScotBlogs | Libraries | WHN