Loss of pro-apoptotic Bax and Bak increases resistance to dihydroartemisinin-mediated cytotoxicity in normoxia but not in hypoxia in HCT116 colorectal cancer cells

Bader, Sina; Wilmers, Julia; Ontikatze, Teona; Ritter, Violetta; Jendrossek, Verena; Rudner, Justine

doi:10.1016/j.freeradbiomed.2021.08.012

Cited by 4 publications

(1 citation statement)

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“…Once the apoptosis dysfunction occurs, cancer cells can progress. Cancer cells could evade apoptosis by inhibiting caspase function 23 , up-regulating anti-apoptotic BCL-2 proteins 24 , 25 , and/or loss of BAX or BAK protein to induce apoptosis 26 . All of these promote cancer cell survival and progression.…”

Section: Introductionmentioning

confidence: 99%

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

Ratanabunyong,

Siriwaseree,

Wanaragthai

et al. 2024

Sci Rep

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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 µg/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.

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