Format

Send to

Choose Destination
Cancer Lett. 2013 May 28;332(2):175-83. doi: 10.1016/j.canlet.2010.11.006. Epub 2011 Jan 6.

Antibody-based fusion proteins to target death receptors in cancer.

Author information

1
Department of Surgery, Surgical Research Laboratories, University Medical Center Groningen, University of Groningen, Hanzeplein 1, 9713 GZ Groningen, The Netherlands.

Abstract

Ideally, an immunotoxin should be inactive 'en route', acquire activity only after tumor cell surface binding and have no off-target effects towards normal cells. In this respect, antibody-based fusion proteins that exploit the tumor-selective pro-apoptotic death ligands sFasL and sTRAIL appear promising. Soluble FasL largely lacks receptor-activating potential, whereas sTRAIL is inactive towards normal cells. Fusion proteins in which an anti-tumor antibody fragment (scFv) is fused to sFasL or sTRAIL prove to be essentially inactive when soluble, while gaining potent anti-tumor activity after selective binding to a predefined tumor-associated cell surface antigen. Importantly, off-target binding by scFv:sTRAIL to normal cells showed no signs of toxicity. In this review, we highlight the rationale and perspectives of scFv:TRAIL/scFv:sFasL based fusion proteins for cancer therapy.

PMID:
21215513
DOI:
10.1016/j.canlet.2010.11.006
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center