Posted in | Nanoanalysis

HMS Researchers Use Single-Molecule Imaging Technique to Study Cell Receptors Motion

Harvard Medical School (HMS) researchers have found that the cell’s structural elements are critical for controlling the movement of cell surface receptors, proteins that allow cells to get signals from different parts of the living organism. This finding helps to learn about the response of cells to biochemical signals and creates an impact on drug production as well as in tumor and other disease therapy.

HMS’ professor of cell biology, Gaudenz Danuser and Jaqaman collaborated with colleagues from the University of Alberta, Edmonton, and Sergio Grinstein, a senior scientist at Toronto's Hospital for Sick Children to study the action of human macrophages receptor called as CD36, a kind of WBC playing a vital role in immune response. CD36 identifies a lipoprotein involved in atherosclerosis, which is oxidized LDL (oxLDL).

Receptors serve as antennas in the communication system of a cell. CD36 never functions alone; always a few receptors form a cluster for transmitting a signal to the cell. Previously, the receptors and cell were imagined to “rest” until it receives a chemical signal making the receptors to cluster together. However, this study clearly explains how the motion of "resting" receptor is functionally related to signal transmission to the cell.

By applying an automated algorithm for particle-tracking designed by Grinstein to surpass the challenges associated with the imaging of complicated, miniature interactions, Jaqaman examined these single-molecule’s motion pictures to detect the receptor regulation and behavior. This picture revealed three types of receptors’ movements.

The receptors are sensitive to the cytoskeleton’s actin meshwork strands near the cell surface. When the receptors wander about, they strike into these strands making them to stop, slow or change direction, whereas some of them roam freely over the cell surface. Others receptors get trapped temporarily within the cytoskeleton's actin mesh, while some others travel in linear routes.


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