- September 7, 2016
- Posted by: emobile
- Category: Researcher's Corner
Emobileclinic Researchers Corner
Researchers from Brown University in the United States and the University of Leuven in Belgium have studied individual atoms in the proteins and their behaviour in living cells and unlocked new lines of treatment for fast-growing cancers such as triple negative breast cancer which has a poorer survival rate and is less well understood than other breast cancers. This finding was published in the Journal eLifes Science.
Although, doctors have emphasis the importance of the use of protein known as Ki-67 to design how aggressive a cancer is, however, they are unclear about how exactly works.
This form the basis of the work of an international team to unpicked how Ki-67 and related protein RepoMan are built and function, finding them as possible novel key targets for cancer therapy. It was discovered that the removal of RepoMan slows or stops cancer cell division, which in certain tumours goes into overdrive.
Dr Paola Vagnarelli said that if they “remove one of the proteins, the cells stop dividing so the cancer will not grow. And since we now know how they function, we can try to design specific drugs that only hit these particular proteins and do not harm normal cells, for example normal breast cells.”
He added that it a major step in unlocking new lines of treatment for fast-growing cancers such as triple negative breast cancer which has a poorer survival rate and is less well understood than other breast cancers.
To him, “for triple negative breast cancer, there are no efficient therapies,” “So knowing the molecular function of these proteins at different stages of the cell cycle, is a major hope for treating the highly aggressive triple negative breast cancer and many other cancers such as oral cancers.”
“This is a powerful approach” the study said. “It is now clear these novel unique protein interaction sites provide immediate opportunities for the design of novel highly specific therapeutics.”
Paola Vagnarelli, et.al (2016): The Ki-67 and RepoMan mitotic phosphatases assemble via an identical, yet novel mechanism. Journal of eLifeSciences, doi: 10.7554/eLife.16539