When he’s not in the operating room performing surgery, Donald M. O’Rourke, M.D., Associate Professor of Neurosurgery at the University of Pennsylvania School of Medicine is fighting brain tumors from the research laboratory bench. He and colleagues are making inroads to understanding the basic molecular biology that makes brain tumors so hard to treat. An estimated 41,000 new cases of primary brain tumors are expected to be diagnosed in 2004, according to the American Brain Tumor Association.
Most recently, O’Rourke and Gurpreet S. Kapoor, PhD, Research Associate in O’Rourke’s laboratory, have discovered that two proteins sitting on the surface of cells are the interconnected switches for turning uncontrolled cell growth on or off in the brain and other tissues. These coupled proteins are the Epidermal Growth Factor Receptor (EGFR) and the Signal Regulatory Proteiná1 (SIRPá1). They report their findings in the September 15 issue of Cancer Research.
In past work, O’Rourke and colleagues found that if EGFR was activated, cancer cells tended to survive longer and migrate to unaffected parts of the brain to spread the cancer. In over 50 percent of glioblastomas – one type of brain cancer that is the leading cause of cancer-related deaths in males aged 20-39 – too much EGFR is produced. In other glioblastomas, too much of a variant called EGFRvIII is also produced, which is linked to poor survival and resistance to treatment in some brain-cancer patients.
Karen Kreeger | EurekAlert!
Climate Impact Research in Hannover: Small Plants against Large Waves
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Proteins must be folded correctly to fulfill their molecular functions in cells. Molecular assistants called chaperones help proteins exploit their inbuilt folding potential and reach the correct three-dimensional structure. Researchers at the Max Planck Institute of Biochemistry (MPIB) have demonstrated that actin, the most abundant protein in higher developed cells, does not have the inbuilt potential to fold and instead requires special assistance to fold into its active state. The chaperone TRiC uses a previously undescribed mechanism to perform actin folding. The study was recently published in the journal Cell.
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