Antheraea proylei J. Sericin Induces Apoptosis in a Caspase-dependent Manner in A549 and HeLa Cells


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Abstract

Background::In spite of much progress in cancer, the global cancer burden is still significant and increasing. Sericin, an adhesive protein of silk cocoons, has been shown to be a potential protein in various biomedical applications, including cancer therapeutics. The present study evaluates the anticancer property of sericin from cocoons of Antheraea proylei J (SAP) against human lung cancer (A549) and cervical cancer (HeLa) cell lines. This is the first report of anti-cancer activity of the non-mulberry silkworm A. proylei J.

Objective::Establish the antiproliferative potential of SAP. 2. Identify the molecular mechanism of cell death induced by SAP on two different cell lines

Aims::To investigate the anticancer activity of sericin preparation from cocoons of A. proylei.

Methods::SAP was prepared from cocoons of A. proylei J. by the process of the degumming method. Cytotoxic activity was assessed by MTT assay, and genotoxicity was assessed by comet assay. Cleavage of caspase and PARP proteins and phosphorylation of MAPK pathway members were analysed by Western blotting. Cell cycle analysis was done by flow cytometer.

Results::SAP causes cytotoxicity to A549 and HeLa cell lines with the IC50 values 3.8 and 3.9 µg/µl respectively. SAP induces apoptosis in a dose-dependent manner through caspase-3 and p38, MAPK pathways in A549 and HeLa cells. Moreover, in A549 and HeLa cells, SAP induces cell cycle arrest at the S phase in a dose-dependent manner.

Conclusion::The difference in the molecular mechanisms of apoptosis induced by SAP in A549 and HeLa cell lines may be due to the difference in the genotypes of the cancer cell lines. However, further investigation is warranted. The overall results of the present study envisage the possibility of using SAP as an anti-tumorigenic agent.

About the authors

Potsangbam Devi

Department of Biochemistry, Laboratory of Protein Biochemistry,, Manipur University

Email: info@benthamscience.net

Asem Singh

Department of Biotechnology, Cancer and Molecular Biology Division, Manipur University

Email: info@benthamscience.net

Naorem Singh

Department of Biotechnology, Cancer and Molecular Biology Division, Manipur University

Email: info@benthamscience.net

Laishram Singh

Department of Biochemistry, Laboratory of Protein Biochemistry, Manipur University

Email: info@benthamscience.net

Sanjenbam Devi

Department of Biochemistry, Laboratory of Protein Biochemistry, Manipur University

Email: info@benthamscience.net

Lisam Singh

Department of Biotechnology, Cancer and Molecular Biology Division, Manipur University

Author for correspondence.
Email: info@benthamscience.net

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