He has labored for years over trying to understand and detail the behavior of insulin-like growth factor-1 (IGF-1) receptor, a protein which plays an important role in tumor growth. Several years ago he and his co-workers discovered that normal cells lacking the IGF-1 receptor gene could not be made to turn cancerous. He found that when they “knocked out” IGF-1 receptors in cancer cells, the cells self-destructed, meaning the IGF-1 receptor was somehow necessary for tumor cell growth. Companies are interested in targeting the IGF-1 receptor with the idea of killing cancer cells, he says.
According to Dr. Baserga, who is professor of microbiology and immunology at Jefferson Medical College of Thomas Jefferson University in Philadelphia and acting director of Jefferson’s Kimmel Cancer Center, in the past few years, scientists have learned that the IGF-1 receptor is also a key growth factor that regulates cell and body size. Deleting the genes for the IGF-1 receptor and its docking protein IRS-1 result in mouse and fly embryos that are only 50 percent of normal size.
“This tells you in essence that the IGF-1 receptor and its docking protein control 50 percent of body size in a non-redundant way,” he says. “This was an important finding because it established the role of IGF-1 receptor and IRS-1 in controlling body size.”
Reporting August 19, 2005 in the Journal of Biological Chemistry, Dr. Baserga and his co-workers provide one possible molecular explanation for how this occurs.
Steve Benowitz | EurekAlert!
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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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