Abstract:
:Receptor of human interleukin 4 (hIL4R) has been found to be present on many types of cancer, so it may be a good target for cancer therapy. Here, fusion toxin gene DT4H has been constructed by fusing DNA sequence encoding the first 389 amino acids of diphtherial toxin (DT), which can not bind its own receptor, to human interleukin 4 (hIL4) gene. In order to improve the affinity of fusion toxin for hIL4R, a circularly permuted form of hIL4 (cpIL4) was used. The fusion gene was expressed in Escherichia coli where the fusion toxin DT4H was highly expressed. Purified DT4H was very cytotoxic to cancer cell line U251 cells, and moderate cytotoxic to HepG2 and MCF-7 cells. SGC-7901 cells were insensitive to it. The cytotoxic action of DT4H was specific because it was blocked by excess hIL4. These results suggest that DT4H may be a useful agent in the treatment of certain malignancies.
journal_name
Acta Biochim Biophys Sin (Shanghai)journal_title
Acta biochimica et biophysica Sinicaauthors
Zhang YJ,Hu XB,Li SX,Tian LP,Yang SL,Gong Ydoi
10.1093/abbs/36.6.437subject
Has Abstractpub_date
2004-06-01 00:00:00pages
437-42issue
6eissn
1672-9145issn
1745-7270journal_volume
36pub_type
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