"Cancer researchers want to design new therapeutic strategies in which the metastasis or spreading stage of cancer can be blocked," explains Andrew Craig, lead researcher and a professor in Queen's Department of Biochemistry and Cancer Research Institute. "Patients stand a much better chance of survival if the primary tumor is the only tumor that needs to be treated."
The regulatory protein identified by Dr Craig's team inhibits the spread of cancer cells by removing and breaking down an invasive enzyme on the surface of cancer cells. If it remains unchecked, this enzyme degrades and modifies surrounding tissues, facilitating the spread of cancer through the body.
Dr. Craig hopes that his team's findings may help develop more targeted therapies that have a specific inhibitory function on this enzyme that is implicated in certain metastatic cancers.
Traditional therapies that have been used to counteract the invasive nature of this particular enzyme also destroy other enzymes that are important for the body's normal physiological function.
The researchers examined a network of proteins that are responsible for controlling the shape of cancer cells. They focused specifically on parts of the cell that protrude into surrounding body tissues, allowing the cancer cell to degrade surrounding tissue barriers.
Normal cells also produce similar protrusions as part of a healthy physiological process that allows cells to move through body tissues during an immune response.
During the spread of cancer these normally healthy mechanisms are coopted by cancer cells, allowing the cancer to break through tissue boundaries and colonize distant tissues. This process of cancer spread is known as metastasis and is frequently the cause of cancer-related deaths.
This research, which was funded by the Canadian Breast Cancer Foundation, will be featured on the cover of the May issue of the Journal of Cell Science, one of the most prestigious international cell biology journals.
Christina Archibald | 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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