Autor: |
Xiao-Ping, Zang, Naveen R, Palwai, Megan R, Lerner, Daniel J, Brackett, J Thomas, Pento, Roger G, Harrison |
Rok vydání: |
2006 |
Předmět: |
|
Zdroj: |
Anticancer research. 26(3A) |
ISSN: |
0250-7005 |
Popis: |
We previously reported that a novel fusion protein (consisting of an amino-terminal fragment of urokinase which binds to the urokinase receptor, and L-methioninase which depletes methionine and arrests the growth of methionine-dependent tumors) inhibited MCF-7 breast cancer cells in vitro.We produced this fusion protein, L-methioninase, and a mutated fusion protein without L-methioninase activity by recombinant methods. MCF-7 cell proliferation and mobility were measured in vitro in a culture wounding assay. Protein binding to MCF-7 cells was measured by immunocytochemical localization. MCF-7 tumor xenograft growth was measured in nude mice.The fusion protein was significantly more effective than L-methioninase in either the in vitro or in vivo assays. The binding assay showed that the unmutated and mutated fusion protein bound to the cells, but L-methioninase did not.Our results suggest that this fusion protein has potential as a therapeutic agent for cancer treatment. |
Databáze: |
OpenAIRE |
Externí odkaz: |
|