Greek scientist Nikolas Nikolaidis and his students at California State University in Fullerton have discovered how a certain protein travels within stressed cells and cancer cells — a finding which could lead to new cancer treatments.
Nikolaidis, who received his PhD from the Aristotle University of Thessaloniki, relayed that their groundbreaking research is a tale of a molecule called “Heat-shock protein,” or Hsp70 (HSPA1A), found in the wrong place at the wrong time.
The CalState team’s research describes the journey of the protein, which travels from inside the cell to the cell surface, or plasma membrane, and beyond, in cancer and stressed cells. The protein is present in cells exposed to stress, such as with fevers, or with pathological conditions such as cancer, and also when they are exposed to toxins.
This protein is a substance inside cells which helps all cancer cells survive. However, it is also present on the surface of 80% of tumors, Dr. Nikolaidis explained.
“The presence of this protein at the cell surface allows cancer cells to resist radiation therapy, increase their invasiveness and develop distant metastasis,” added Nikolaidis, a professor of biological science. “There-fore, stopping the protein from being there is a promising new treatment suitable for several cancer types.”
His team’s research focuses on defining how and why this protein, which functions to keep the cell alive, travels to the surface of cancer and stressed cells. The goal is the development of drugs which alter the location of the protein and activate the immune system to attack the cancer.
“Our most recent work describes an important part of this mechanism, which includes the interaction of the protein with specific membrane lipids,” Nikolaidis said. “The complete characterization of this mechanism would be of importance towards new, universal cancer therapeutics.”
Their latest research finding is described in a new paper published in “Biomolecules,” a peer-reviewed scientific and open-access journal. The researchers also discovered that the protein binds to a particular lipid called phosphatidylserine inside the cell.
“We found that this binding is important, if not critical, to the movement of the protein to the cell surface. Our published work delineates a major part of the pathway that this protein uses to travel and anchor at the cell membrane,” the researcher explained.
