In a new approach to developing treatments for breast cancer, prostate cancer and enlarged hearts, Loyola University Stritch School of Medicine researchers are zeroing in on a workhorse protein called RSK.
When activated, RSK is involved in cell survival, cell proliferation and cell enlargement. These properties contribute towards cancer progression, heart enlargement and tumors associated with a genetic disease called Carney complex. Loyola researchers have discovered that a regulatory protein binds to RSK. This regulatory protein effectively keeps RSK's activity in check.
In a study to be published in the Journal of Biological Chemistry, Patel and colleagues located the specific region of the regulatory protein that binds to RSK. The study was published online Jan. 4 in advance of print publication.
"The implications are widespread, and will also change textbooks for students," said Tarun Patel, PhD, chairman of the Department of Molecular Pharmacology & Therapeutics at Loyola University Chicago Stritch School of Medicine.
It was previously known that the regulatory protein that binds RSK is also associated with another enzyme known as PKA. PKA is critical in maintaining normal body functions including heart rate, contraction of the heart, blood pressure, hormone release, learning and memory. PKA also is involved in modulating tumor growth and progression. Because RSK and PKA compete for binding with the same regulatory protein, they end up modulating each other's activities.