Tagged and untagged TRAIL show different activity against tumor cells
- Authors:
- Kunpeng Zhao
- Yan'ge Wang
- Xueyin Wang
- Yugang Wang
- Yuanfang Ma
View Affiliations
Affiliations: Department of Cell Biology, Institute of Immunology, Medical College of Henan University, Henan 475003, P.R. China, Department of Cell Biology, Institute of Immunology, Medical College of Henan University, Henan 475003, P.R. China, Department of Immunology, Henan Medical College for Staff and Workers, Zhengzhou, Henan 451191, P.R. China, Department of Immunology, Institute of Basic Medical Sciences, Beijing 100850, P.R. China
- Published online on: September 11, 2012 https://doi.org/10.3892/ol.2012.908
-
Pages:
1301-1304
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Abstract
The tumor necrosis factor-related apoptosis‑inducing ligand (TRAIL/Apo2L) is a novel cytotoxic ligand belonging to the TNF superfamily which is currently being developed as a cancer therapeutic drug. Here, we observed the different functions of recombinant TRAIL protein with a foreign protein label and non-labeled TRAIL. We used a prokaryotic expression system to prepare two different versions of the extracellular TRAIL 114-281aa protein: TRAIL-HS, a protein modified with 6xHis-Tag and S-Tag; and TRAIL-FT, which had no foreign protein. The proteins were purified using Ni-NTA chromatography (TRAIL-HS) and cation ion‑exchange column chromatography (TRAIL-FT) and identified by SDS-PAGE and western blot analysis. We compared the abilities of the proteins to bind to death receptor 5 (DR5) by ELISA and to induce apoptosis in a normal liver cell line (Chang liver) and a human T-lymphocyte leukemia cell line (Jurkat) by MTT assay, GR staining and FACS. The results indicate that the biological functions of TRAIL-FT were superior to those of TRAIL-HS in binding and the induction of apoptosis, and may be useful to further the development and applications of TRAIL.
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