A Novel Ribonuclease from Rana Chensinensis and Its Potential for the Treatment of Human Breast Cancer.

Abstract

Onconase, a member of the pancreatic RNAase A superfamily of ribonucleases, is a chemotherapeutic agent, which has demonstrated selective antitumor activity in a variety of human malignancies. However, little is known about the mechanisms of it's action on human breast cancer cells. To investigate a novel Onconase from the frog of Rana chensinensis changbaishanensis on human breast cancer cells and the underlying mechanisms, a novel Onconase named Rdchonc from Rana chensinensis changbaishanensis was cloned by polymerase chain reaction. SDS-PAGE revealed that the Rdchonc had a high heterologous expression in Escherichia coli BL21(DE3). The MTT assay indicated that purified Rdchonc was cytotoxic to human breast cancer MCF-7 and MD-MB-231 cells. Treatment with 20 μg/mL Rdchonc protein significantly reduced the invasive capacities of MCF-7 and MD-MB-231 cells. Interestingly, the authors found that such inhibitory effort on tumor cell growth induced by Rdchonc treatment may be explained by the regulation of proapoptotic Bcl-2 family proteins and inhibition of MEK/ERK phosphorylation.