Researchers have developed a high-speed form of atomic force microscopy. For the first time, this microscope is able to reveal details about how deactivation of a key protein may lead to metastasis.

The findings also provide evidence for the mechanisms involved in a cell’s response to anti-cancer drugs.

In atomic force microscopy, a tiny vibrating probe called a cantilever passes over a material and characterizes its topography and physical properties. Before this new technology, the procedure has been too slow to record some quickly changing biological processes in action.

Before the atomic force microscopy, it was only possible to see the before and after, not what happened in between. There is evidence based on this work and researchers’ previous findings that there might be a mechanical signature to drug resistance.

Advanced models allow researchers to convert atomic force microscopy data into properties about the cell’s cortical actin cytoskeleton, which includes the motion of fibers called actin.

Kinases cause phosphorylation of proteins, a biochemical process that can alter enzymes. Kinases plays a significant role in a wide range of cellular processes.

Researchers studied breast cancer cells exposed to a chemical inhibitor that blocks the functioning of Syk, allowing the cells to metastasize. Due to the higher speed atomic force microscopy, researchers were able to observe what happens when the inhibitor is added.

After adding the inhibitor, actin bands propagate across the cell, causing the cell to change shape. Bands of actin were shown to move in a sweeping motion across the cell.

When Syk is missing or deactivated, the cells cannot metastasize. Researchers have been trying to figure out what the mechanisms are by which to get rid of this kinase in order to become highly motile and metastatic.

One goal of the research is to correlate physical properties of cells with tumor suppression and the action of the kinase on the cell.

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Gerry Oginski
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