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Columns::March 31, 2003
Grant will boost job choices for people with disabilities
Alan Darvill, CCRC co-director, is appointed to Regents Professorship
Two students receive Goldwater Scholarship; another named Truman Scholar
A spring break with Seoul
Former Gov. Harris will speak at spring commencement ceremony
‘Caring’ effort recognized
Campus Closeup
Administrative Changes
Kudos
Bundles of energy
Land of the Morning Calm
Campus News
Tag team
CCRC researchers help design better disease treatments
By Rory Sheats
rcomm@ovpr.uga.edu
Jim Prestegard and Michael Pierce, scientists at UGA’s Complex Carbohydrate Research Center, are using sophisticated
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Jim Prestegard
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nuclear magnetic resonance technology and a variety of other biology-based technologies to further the development of new--potentially revolutionary--cancer treatments.
Using NMR techniques, Prestegard provides detailed information on how drugs bind to proteins. Pierce then uses this information to design molecules that could prevent the spread of cancer in humans. Such molecules are potential drugs, inhibiting undesirable biological processes that lead to disease. These drugs work by physically binding to cell structures at the molecular level, just as appliances work by plugging a cord into an outlet.
“The way to make an effective disease inhibitor is to know structural information about the interaction between proteins and potential drug candidates,” Prestegard says. “The NMR technique presents information that will enable scientists to develop drugs that bind more tightly to proteins and, therefore, devise faster and more effective treatments for disease.”
Pierce, a professor of biochemistry and molecular biology, takes advantage of Prestegard’s NMR findings to study how an enzyme called GnT-V influences the spread of cancer in humans.
In January Pierce traveled to Bangalore, India, and shared his research findings at the Glyco XVII convention.
“This is an international convention held every two years that highlights the research being done in glycobiology around the world,” he says.
Pierce’s research team found that the GnT-V enzyme produces oligosaccharides--short chains of sugars on the surface of cells. They also discovered that when cells become cancerous, the GnT-V enzyme overproduces these sugars. The excess sugars change the surface of cancer cells, making them unable to bind together effectively--like mortar being weakened between bricks. As cells break away they
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Michael Pierce
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invade adjacent tissues and spread to distant sites within the body through the bloodstream and the lymph system.
The team’s latest findings were published in the December 2002 issue of Cancer Research Journal. The research, which has been funded by the National Institutes of Health, the American Cancer Society and the National Cancer Institute, also has generated numerous articles in other peer-reviewed biochemistry, biophysical and glycobiology journals.
Pierce says his research team is searching for a GnT-V inhibitor, one that could make possible the development of a drug to bind to the enzyme and retard cancer cell migrations. The GnT-V enzyme, patented through the UGA Research Foundation, is licensed to a biopharmaceutical company based in Pennsylvania. This company focuses on developing protein therapeutics that offer significant advantages, including less frequent dosing and improved patient safety.
Some of Pierce’s technology has been licensed to Oncose, a company Pierce co-founded to develop innovative diagnostic tests for early cancer detection. The Athens-based biotechnology firm takes Pierce’s UGA findings one step closer to commercial development of early cancer diagnostics.
While Pierce investigates new ways to diagnose cancer and diminish its spread, Prestegard, an Eminent Scholar of NMR Spectroscopy, supplies critical NMR data. NMR spectroscopy operates on the same principle as magnetic resonance imaging, but is used to analyze structures at the molecular and atomic levels.
“Our current 800 megahertz spectrometer has stored energy that is equilavent to an 18-wheeler going down the highway at around 40 miles per hour,” Prestegard says. A strong magnetic field--capable of erasing credit cards and pulling keys from pockets--emanates from each machine.
Until recently, X-ray crystallography was the most common procedure for obtaining structural information on proteins. However, not all proteins crystallize, and this is where the NMR technique has an advantage.
“NMR offers a complementary procedure that gives a route into protein structural information for a class of proteins that are not easily attacked by X-ray crystallography,” Prestegard says. “In addition, the NMR combines several new methods with high magnetic fields to allow us to get data in a fraction of the time required by more conventional approaches.”
NMR technology can also provide improved structural information on carbohydrates. These starch and sugar molecules are produced by glycosyltransferase enzymes such as GnT-V.
“This is a class of proteins that have not been fully explored by the scientific community,” Prestegard says. “There are currently very few drugs that bind to these proteins and the improved information provided by the NMR technology could lead to new, fertile ground in developing additional drugs.”
The power of NMR spectrometers increases with the magnetic fields at which they operate and the radio frequencies used to observe magnetic nuclei within proteins at these fields. Thanks to two grants totaling $5.2 million--$4.2 million from the National Institutes of Health and $1 million from the Georgia Research Alliance--Prestegard will soon have access to a 900-MHz spectrometer.
The new spectrometer, which features the highest magnetic field available, will be installed next winter after the Complex Carbohydrate Research Center moves into its new facility at Riverbend. This latest version of NMR technology will provide Prestegard and his research team, as well as other UGA scientists and their colleagues at 17 other research institutions, with data that feature enhanced resolution and sensitivity.
In addition to studying drug-protein interactions, NMR technology enables researchers to investigate a wide range of other biologically important processes, such as how bacteria invade cells and how hormones interact with cell receptors. |
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