- Clinical Expertise
- Research Faculty
- Appointments
- Associate Research Scientist, Columbia University Medical Center
Bowen Cai, M.D.
TEL (212) 851-4559
- PROFILE SUMMARY
- Dr. Cai received her undergraduate and medical doctor degrees from the Beijing Medical University. She also received a Master of Science degree from the Department of Cancer Pharmacology, Institute of Chinese Materia Medica, Chinese Academy of Traditional Chinese Medicine. Her post doctoral training in prostate cancer study was completed at the Division of Oncology, Lombardi Comprehensive Cancer Center of Georgetown University. She was also a faculty member of Georgetown University. She has been a faculty member of the Herbert Irving Comprehensive Cancer Center, Division of Hematology/Oncology, Department of Medicine of Columbia University since March of 2007.
Our primary research interest is to understand the molecular mechanisms by which NKX3.1 mediates tumor suppression, and in particular to elucidate its role in DNA damage repair. In seeking to elucidate the tumor suppression function of NKX3.1, our research approach is to identify the NKX3.1 interacting proteins and explore the functional significance of their associations on tumor suppression.
Using an NKX3.1 affinity column, we isolated topoisomerase I (Topo I) from a PC-3 prostate cancer cell extract. Topo I is an ubiquitous enzyme that is required for multiple DNA metabolism processes such as: replication, transcription, recombination or chromatin assembly and DNA repair. We demonstrate that NKX3.1 interacts with Topo I to enhance formation of the Topo I-DNA complex and to increase Topo I cleavage of DNA. Endogenous Topo I and NKX3.1 could be coimmunoprecipitated from LNCaP cells, where NKX3.1 and Topo I were found to colocalize in the nucleus and comigrate within the nucleus in response to either gamma-irradiation or mitomycin C exposure, two DNA-damaging agents. Our study suggests that a homeodomain protein can modify the activity of Topo I, and may have implications for organ-specific DNA replication, transcription, or DNA repair.
Our current study is to identify the role of NKX3.1 in DNA damage repair as part of its function in tumor suppression. The study is involved in characterizing NKX3.1 as a regulator in DNA damage repair and defining the potential molecular mechanism through which NKX3.1 and Topo I coordinate to mediate repair of DNA DSBs.