期刊
CANCER CELL
卷 29, 期 2, 页码 173-185出版社
CELL PRESS
DOI: 10.1016/j.ccell.2016.01.001
关键词
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资金
- Multiple Sclerosis Society of Canada
- Canadian Institute of Health Research [RPA-109759]
- Deutsche Forschungsgemeinschaft [SFB 829]
- Koln Fortune Programm of the Medical Faculty
- Netris Pharma
- CNRS
- University of Lyon
- Center Leon Berard
- Ligue Contre le Cancer
- INCA
- ANR
- ERC
- EU-FP7 HERMIONE-2MAN
- Fondation Bettencourt
- Cecile Vogt Fellowship
- CIHR
Netrin-1 has been shown to be up-regulated in a fraction of human cancers as a mechanism to allow these tumors to escape the pro-apoptotic activity of some of its main dependence receptors, the UNC5 homologs (UNC5H). Here we identify the V-2 domain of netrin-1 to be important for its interaction with the Ig1/Ig2 domains of UNC5H2. We generate a humanized anti-netrin-1 antibody that disrupts the interaction between netrin-1 and UNC5H2 and triggers death of netrin-1-expressing tumor cells in vitro. We also present evidence that combining the anti-netrin-1 antibody with epidrugs such as decitabine could be effective in treating tumors showing no or modest netrin-1 expression. These results support that this antibody is a promising drug candidate.
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