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Regulation by proteins outside cancer cells points to potential new drug target: Reprogram cancer cells to state of permanent dormancy?

Date:
July 9, 2012
Source:
University of Texas Health Science Center at San Antonio
Summary:
Proteins outside cancer cells that send signals to the cancerous cells to stop proliferating represent a potential novel target for therapeutic strategy, says a biochemist whose team made the finding.

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.

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"Because this protein cascade is outside the cells, it is likely amenable to therapeutic manipulation," said lead author Yuzuru Shiio, M.D., Ph.D., assistant professor of biochemistry at the university's Greehey Children's Cancer Research Institute. "I hope our study will ultimately lead to a therapeutic strategy to reprogram cancer cells to a state of permanent dormancy."

He cautions that the finding was observed in cell cultures and is still far from human cancer therapy. Dr. Shiio is also a member of the Cancer Therapy & Research Center (CTRC) 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, Dr. Shiio said.

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 a protein called IGFBP3 (insulin-like growth factor binding protein 3) is a key player in cancer senescence. The team then studied other proteins that work together with IGFBP3 outside of the cancer cells.

Needle in a haystack

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. It was like finding a proverbial needle in a haystack.


Story Source:

The above story is based on materials provided by University of Texas Health Science Center at San Antonio. Note: Materials may be edited for content and length.


Journal Reference:

  1. David J. Elzi, Yanlai Lai, Meihua Song, Kevin Hakala, Susan T. Weintraub, and Yuzuru Shiio. Plasminogen activator inhibitor 1 - insulin-like growth factor binding protein 3 cascade regulates stress-induced senescence. PNAS, July 9, 2012 DOI: 10.1073/pnas.1120437109

Cite This Page:

University of Texas Health Science Center at San Antonio. "Regulation by proteins outside cancer cells points to potential new drug target: Reprogram cancer cells to state of permanent dormancy?." ScienceDaily. ScienceDaily, 9 July 2012. <www.sciencedaily.com/releases/2012/07/120709155417.htm>.
University of Texas Health Science Center at San Antonio. (2012, July 9). Regulation by proteins outside cancer cells points to potential new drug target: Reprogram cancer cells to state of permanent dormancy?. ScienceDaily. Retrieved October 25, 2014 from www.sciencedaily.com/releases/2012/07/120709155417.htm
University of Texas Health Science Center at San Antonio. "Regulation by proteins outside cancer cells points to potential new drug target: Reprogram cancer cells to state of permanent dormancy?." ScienceDaily. www.sciencedaily.com/releases/2012/07/120709155417.htm (accessed October 25, 2014).

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