Exploring the apoptotic effects of sericin on HCT116 cells through comprehensive nanostring transcriptomics and proteomics analysis

Abstract

Sericin a silk protein from Bombyx mori (silkworms) has many applications including cosmetics anti-inflammation and anti-cancer. Sericin complexes with nanoparticles have shown promise for breast cancer cell lines. Apoptosis a programmed cell death mechanism stops cancer cell growth. This study found that Sericin urea extract significantly affected HCT116 cell viability (IC50 = 42.00 ? 0.002�g/mL) and caused apoptosis in over 80% of treated cells. S-FTIR analysis showed significant changes in Sericin-treated cells macromolecule composition particularly in the lipid and nucleic acid areas indicating major cellular modifications. A transcriptomics study found upregulation of the apoptotic signaling genes FASLG TNFSF10 CASP3 CASP7 CASP8 and CASP10. Early apoptotic proteins also showed that BAD AKT CASP9 p53 and CASP8 were significantly upregulated. A proteomics study illuminated Sericin-treated cells altered protein patterns. Our results show that Sericin activated the extrinsic apoptosis pathway via the caspase cascade (CASP8/10 and CASP3/7) and the death receptor pathway involving TNFSF10 or FASLG in HCT116 cells. Upregulation of p53 increases CASP8 which activates CASP3 and causes HCT116 cell death. This multi-omics study illuminates the molecular mechanisms of Sericin-induced apoptosis sheds light on its potential cancer treatment applications and helps us understand the complex relationship between silk-derived proteins and cellular processes. ? 2024 The Author(s).