Vision to reprogram cancer cells to state of permanent dormancy
Regulation by proteins outside cancer cells points to potential new drug target
- Date : 13 Jul 2012
- Topic : Breast cancer
Protein interactions outside breast cancer cells can send signals to the cancer cells to permanently stop proliferating, a new study showed in the School of Medicine at The University of Texas Health Science Center, San Antonio, USA. The researchers hope that their study will ultimately lead to a therapeutic strategy to reprogram cancer cells to a state of permanent dormancy. However, they caution that the finding was observed in cell cultures and is still far from human cancer therapy.
According to lead author Dr Yuzuru Shiio, assistant professor of biochemistry at the university's Greehey Children's Cancer Research Institute, this protein cascade is outside the cells, and it is likely amenable to therapeutic manipulation. Dr Shiio is also a member of the Cancer Therapy & Research Center at the UT Health Science Center, a National Cancer Institute Designated Cancer Center.
Senescence is poorly understood
Upon successful chemotherapy, cancer cells either die or permanently stop proliferation. The latter phenomenon is called senescence and is poorly understood.
Using cultured breast cancer cells as a model, the team found that upon chemotherapeutic drug treatment these cells released factors that stop proliferation. By analyzing which proteins are released under this stress, the team discovered that insulin-like growth factor binding protein 3 (IGFBP3) is a key player in cancer senescence. The team then studied other proteins that work together with IGFBP3 outside of the cancer cells.
Using powerful, large-scale analysis called proteomics, the researchers literally picked out the increased abundance of this one protein, IGFBP3, among a thousand other proteins outside of the cells.
USA National Institutes of Health grants AG029587, CA125020 and CA137568 to Dr Shiio and an institutional grant, CA054174 (Cancer Therapy & Research Center at the UT Health Science Center San Antonio - Mass Spectrometry Shared Resource and Pathology Core Laboratory), supported this research in part.
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