Radio Show: There’s A Promising New Treatment For Prostate Cancer
Drug triggers immune cells to attack prostate cancer
A single drug compound simultaneously attacks hard-to-treat prostate cancer on several fronts, according to a new study in mice and human cells. It triggers immune cells to attack, helps the immune cells penetrate the tumor, and cuts off the tumor’s ability to burn testosterone as fuel, according to new research.
Researchers Uncover Mechanism by Which Prostate Cancer Becomes Resistant
Prostate cancer is common cancer among men. Despite the benefits of androgen deprivation therapy, drug resistance is common. Now researchers report they have discovered a mechanism by which prostate cancer cells become resistant through acetylation of the androgen receptor (AR) protein and identified a potential treatment approach that could overcome this resistance.
NXTAR, RNA molecule suppresses prostate tumor growth
A study from Washington University School of Medicine in St. Louis has identified an RNA molecule that suppresses prostate tumors. According to the research — restoring this so-called long noncoding RNA, NXTAR, could be a new strategy to treat prostate cancer that has developed resistance to hormonal therapies.
CDMRP – Transforming Healthcare through Innovative and Impactful Research
Researchers identify inhibitor that overcomes drug resistance in prostate cancer AR protein production in the presence of enzalutamide through ACK1-mediated histone phosphorylation is a new finding. The new inhibitor, (R)-9b, that the research team has developed could become a new therapeutic modality, especially for those patients not responsive to enzalutamide or have developed resistance to it. The compound will be in clinical trials in 1-2 years.
DEPARTMENT OF DEFENSE – Congressionally Directed medical Research programs
NCI NIH 2012
Cancer cells have ‘hijacked’ histone modification mechanism to lower histone levels and thus activate the growth and survival of cancer cells. The research team discovered that a modified histone itself regulates histone synthesis. The modification is histone H2B phosphorylation (in this case the process of adding a phosphate to a protein molecule) at tyrosine 37 (tyrosine is one of the amino acids), which is critical for suppression of core histone mRNA synthesis.The significance of this process in cancer cells became evident when they identified a tyrosine kinase, WEE1, as being a critical regulator of the process.