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A Novel Ribonuclease from Rana Chensinensis and Its Potential for the Treatment of Human Breast Cancer
Zuozhao Wang1,2, Feng Lin1, Jingbo Liu2
11 College of Chemistry, Jilin University , Changchun, People's Republic of China .
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.
Insights
A novel Onconase, Rdchonc, derived from Rana chensinensis changbaishanensis, exhibits potent anti-cancer effects on human breast cancer cells. This ribonucleotide-based therapeutic agent demonstrates cytotoxicity and inhibits tumor cell invasion by regulating apoptosis and MEK/ERK signaling pathways.
Area of Science:
- Biochemistry
- Molecular Biology
- Oncology
Background:
- Onconase, a pancreatic ribonuclease A superfamily member, shows antitumor activity in various malignancies.
- The precise mechanisms of Onconase action on human breast cancer cells remain largely unelucidated.
- Investigating novel Onconase variants offers potential for new cancer therapies.
Purpose of the Study:
- To clone and characterize a novel Onconase, Rdchonc, from Rana chensinensis changbaishanensis.
- To evaluate the cytotoxic and anti-invasive effects of Rdchonc on human breast cancer cell lines (MCF-7 and MD-MB-231).
- To elucidate the molecular mechanisms underlying Rdchonc's anti-cancer activity.
Main Methods:
- Polymerase chain reaction (PCR) for gene cloning.
- Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) for protein expression analysis.
- Methyl thiazolyl tetrazolium (MTT) assay for cytotoxicity assessment.
- Invasion assays and Western blotting for mechanistic studies.
Main Results:
- Rdchonc was successfully cloned and expressed heterologously in Escherichia coli BL21(DE3).
- Purified Rdchonc demonstrated significant cytotoxicity against MCF-7 and MD-MB-231 human breast cancer cells.
- Rdchonc treatment reduced tumor cell invasion and modulated the phosphorylation of MEK/ERK signaling pathways.
- The anti-cancer effects were associated with the regulation of proapoptotic Bcl-2 family proteins.
Conclusions:
- Rdchonc represents a promising novel Onconase with significant cytotoxic and anti-invasive properties against human breast cancer cells.
- The findings suggest that Rdchonc exerts its anti-tumor effects through the regulation of apoptosis-related proteins and the MEK/ERK signaling pathway.
- Rdchonc holds potential as a chemotherapeutic agent for breast cancer treatment, warranting further investigation.
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