The study explains how prostate cancer senses a drop in testosterone due to anti-hormone therapy and then begins making cholesterol — a necessary precursor to testosterone — to generate its own testosterone to fuel tumor growth. The study also points to a possible drug combination that may stop the cancer from feeding its own growth.
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.
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.
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.
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.
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.