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Collaborative research finds a poorly understood protein could aid in the battle against cancer.

Where it concerns medical research in the scope of battling one of humanity's most pervasive and deadly diseases like cancer, new nano and macroparticle treatments have been seeing the lion's share of spotlight. DailyTech has reported on several of these advances and inventions, from the tiny cell-exploding carbon nanotube to advanced lipid-based drug and imaging delivery systems.

However, while these are exciting times for the emerging field of medical nanosystems, it is not by any means the sole avenue of exploration.

Collaboration between doctors Brian Volkman, Christopher Veldkamp, and Michael Dwinell of Medical College of Wisconsin is examining the function of a protein known as CXCL12 and its effects on the spread of cancer and its possible use in as an inhibitor. Past research by Dr. Dwinell linked the expression of CXCL12, a protein known as a chemokine, to the inhibiting of breast cancer.

To more clearly understand the function of CXCL12, Dr. Volkman and his colleagues created three dimensional models of the chemokine and studied its affects and interactions with its key receptor, CXCR4. Among their findings was that while CXCL12 as a single molecule actively encourages cell migration, a key to cancer's spreading abilities, if two of the chemokines were bound together, creating what's known as a dimer, this coercion effect is all but removed.

To further solidify these synthetic dimers' functions as an avenue of study, the proteins are still able to bond with the CXCR4 receptor, thus able to perform the duties of the normally expressed single CXCL12 proteins.

“This was exciting because it was genuinely unexpected. It was the strongest suggestion yet that chemokine dimers might really be active participants in directing the migration of white blood cells and possibly other kinds of cells,” explains Dr. Volkman.

Dr. Volkman credits the discovery and success of the study to the collaboration between the different groups involved. “While we were focused on understanding details of the molecular structure of CXCL12, Dr. Dwinell’s research group had developed a sophisticated method for measuring breast cancer metastasis. So we asked him to help us design experiments to find out if his CXCL12 dimer could interfere with the spread of cancer,” he says. “Collaborations promote the exchange of ideas between scientists from different backgrounds and often lead in completely unanticipated directions.”





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