- Clinical Expertise
- Research Faculty
- Appointments
- Associate Research Scientist, Columbia University Medical Center
Liang-Nian Song, Ph.D.
TEL (212) 851-4558
- PROFILE SUMMARY
- Dr. Song received his M.D. from the Second Military Medical University (SMMU) of the People’s Republic of China, his Ph.D. from the Neuroscience Institute of the SMMU, and post doctoral training in molecular biology and cancer biology from NIDDK, National Institutes of Health and Georgetown University. He was a research faculty member at Lombardi Comprehensive Cancer Center from 2002 to 2007 and has been a research faculty member at the Columbia University Medical Center since 2007.
The major focus of my interest is on the molecular basis of prostate cancer development and progression. The androgen receptor (AR), which is a member of the steroid/nuclear receptor superfamily, plays a critical role in prostate cancer. We have found that AR cross-talked with beta-catenin, which is the central mediator of canonical Wnt signaling. We demonstrated that beta-catenin functions as a specific coactivator of AR by physical association with the receptor in an androgen-dependent manner. Since our previous data suggested that there existed activating activation of beta-catenin in certain prostate patients, the physical and functional association might play a potential role in the development and progression of prostate cancer. We have also demonstrated the important role of corepressors SMRT and NCoR in the antagonistic effect of antiandrogens some of which have been widely used clinically for the treatment of prostate cancer.
The prostate-specific homeodomain protein NKX3.1 is a tumor suppressor that is commonly down-regulated in human prostate cancer. Recently, Bowen and Gelmann (Cancer Res. 2007 Jan 15; 67:455-64) found that topoisomerase I (Topo I) is one of the protein in the NKX3.1 associated protein complex in prostate cancer cells. Moreover, NKX3.1 was found to be able to enhance the phosphorylation of alternative splicing factor (ASF/SF2) by Topo I. These findings suggest that NKX3.1 may play a role in the regulation of alternative splicing of certain targets. Our ongoing studies are to verify this proposal.