RT Journal Article
SR Electronic
T1 Influence of L-Methioninase Targeted to the Urokinase Receptor on the Proliferation and Motility of Lung and Prostate Cancer Cells
JF Anticancer Research
JO Anticancer Res
FD International Institute of Anticancer Research
SP 3435
OP 3439
VO 27
IS 5A
A1 PALWAI, NAVEEN R.
A1 ZANG, XIAO-PING
A1 HARRISON, ROGER G.
A1 PENTO, J. THOMAS
YR 2007
UL http://ar.iiarjournals.org/content/27/5A/3435.abstract
AB Background: Previously, we reported that a novel fusion protein consisting of an amino-terminal fragment of urokinase linked to the amino terminus of the enzyme L-methioninase inhibited MCF-7 breast cancer cells in vitro to a greater extent than treatment with L-methioninase. Materials and Methods: The fusion protein, L-methioninase and a mutated fusion protein without L-methioninase activity were produced by recombinant methods. The effects of fusion protein, L-methioninase, and mutated fusion protein treatment on the proliferation and motility of SK-LU-1 lung and PC-3 prostate and cancer cells were measured in vitro using a culture wounding assay. Results: The fusion protein produced a dose-dependent inhibition of the proliferation and motility of both cancer cell lines. In addition, the fusion protein was found to be significantly more effective than L-methioninase alone or mutated fusion protein. Conclusion: Our results suggest that this fusion protein has potential as a selective therapeutic agent for the treatment of various methionine-dependent cancers. Copyright© 2007 International Institute of Anticancer Research (Dr. John G. Delinassios), All rights reserved