A mini-antibody bearing a payload of tumor-busting radiation thwarts the growth of human breast cancer in laboratory animals, according to research published in the September 1 issue of the journal Cancer Research.
The research shows that a diabody, an antibody surrogate just one third the size of native antibodies, can be used effectively as a targeting vehicle for radioimmunotherapy, said Gregory Adams, Ph.D., associate member of the Medical Science Division, Fox Chase Cancer Center, Philadelphia, Pa.
Diabodies are genetically engineered dimeric proteins produced in E. coli bacteria that contain the antigen-recognizing portion of antibodies formed by immune system cells to combat disease. The mini-antibody developed by Adams and colleagues, C6.5K-A, is a protein substitute for larger, naturally produced antibodies that specifically target the HER2/neu human tumor-associated antigen. When loaded with the beta-emitting radioisotope yttrium-90, C6.5K-A significantly inhibits the growth rate of human breast tumor xenografts in mice. "The diabodies bound to the HER2 receptor produced by certain breast tumor cells." said Adams, the lead author on the paper. "Imaging indicated that the diabody was concentrated in the mammary tumors and in the kidney where it was excreted from the body."
Russell Vanderboom, PhD | 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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