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The type-1 ribosome-inactivating protein OsRIP1 triggers caspase-independent apoptotic-like death in HeLa cells

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Abstract
Ribosome-inactivating proteins (RIPs) are capable of removing a specific adenine from 285 ribosomal RNA, thus inhibiting protein biosynthesis in an irreversible manner. In this study, recombinant OsRIP1, a type 1 RIP from rice (Oryza saliva L.), was investigated for its anti-proliferative properties. Human cervical cancer HeLa cells were incubated in the presence of OsRIP1 for 24-72 h. OsRIP1 treatment yielded an anti-proliferation response of the HeLa cells and resulted in apoptotic-like blebbing of the plasma membrane without causing DNA fragmentation. OsRIP1 labeled with FITC accumulated at the cell surface. Pull-down assays identified ASPP1 (Apoptosis-Stimulating Protein of p53 1) and IFITM3 (interferon-induced transmembrane protein 3) as potential interaction partners for OsRIP1. Transcript levels for several critical genes related to different signaling pathways were quantified by RT-qPCR. OsRIP1 provoked HeLa cells to undergo caspase-independent cell death, associated with a significant transcriptional upregulation of the apoptotic gene PUMA, interferon regulatory factor 1 (IRF1) and the autophagy-related marker LC3. No changes in caspase activities were observed. Together, these data suggest that apoptotic-like events were involved in OsRIP1-driven caspase-independent cell death that might trigger the IRF1 signaling pathway and LC3-mediated autophagy.
Keywords
Toxicology, General Medicine, Food Science, Ribosome-inactivating protein, Anti-cancer, Caspase independent apoptosis, Cell blebbing, Cell death, FUSION PROTEIN, CYCLE ARREST, DNA-DAMAGE, CANCER, NECROPTOSIS, EXPRESSION, MITOPHAGY, CLEAVAGE, SURVIVAL, DOMAIN

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MLA
Chen, Simin, et al. “The Type-1 Ribosome-Inactivating Protein OsRIP1 Triggers Caspase-Independent Apoptotic-like Death in HeLa Cells.” FOOD AND CHEMICAL TOXICOLOGY, vol. 157, 2021, doi:10.1016/j.fct.2021.112590.
APA
Chen, S., Figueiredo Lossio, C., Verbeke, I., Verduijn, J., Parakhonskiy, B., Van der Meeren, L., … Van Damme, E. (2021). The type-1 ribosome-inactivating protein OsRIP1 triggers caspase-independent apoptotic-like death in HeLa cells. FOOD AND CHEMICAL TOXICOLOGY, 157. https://doi.org/10.1016/j.fct.2021.112590
Chicago author-date
Chen, Simin, Claudia Figueiredo Lossio, Isabel Verbeke, Joost Verduijn, Bogdan Parakhonskiy, Louis Van der Meeren, Pengyu Chen, Jeroen De Zaeytijd, Andre Skirtach, and Els Van Damme. 2021. “The Type-1 Ribosome-Inactivating Protein OsRIP1 Triggers Caspase-Independent Apoptotic-like Death in HeLa Cells.” FOOD AND CHEMICAL TOXICOLOGY 157. https://doi.org/10.1016/j.fct.2021.112590.
Chicago author-date (all authors)
Chen, Simin, Claudia Figueiredo Lossio, Isabel Verbeke, Joost Verduijn, Bogdan Parakhonskiy, Louis Van der Meeren, Pengyu Chen, Jeroen De Zaeytijd, Andre Skirtach, and Els Van Damme. 2021. “The Type-1 Ribosome-Inactivating Protein OsRIP1 Triggers Caspase-Independent Apoptotic-like Death in HeLa Cells.” FOOD AND CHEMICAL TOXICOLOGY 157. doi:10.1016/j.fct.2021.112590.
Vancouver
1.
Chen S, Figueiredo Lossio C, Verbeke I, Verduijn J, Parakhonskiy B, Van der Meeren L, et al. The type-1 ribosome-inactivating protein OsRIP1 triggers caspase-independent apoptotic-like death in HeLa cells. FOOD AND CHEMICAL TOXICOLOGY. 2021;157.
IEEE
[1]
S. Chen et al., “The type-1 ribosome-inactivating protein OsRIP1 triggers caspase-independent apoptotic-like death in HeLa cells,” FOOD AND CHEMICAL TOXICOLOGY, vol. 157, 2021.
@article{8730604,
  abstract     = {{Ribosome-inactivating proteins (RIPs) are capable of removing a specific adenine from 285 ribosomal RNA, thus inhibiting protein biosynthesis in an irreversible manner. In this study, recombinant OsRIP1, a type 1 RIP from rice (Oryza saliva L.), was investigated for its anti-proliferative properties. Human cervical cancer HeLa cells were incubated in the presence of OsRIP1 for 24-72 h. OsRIP1 treatment yielded an anti-proliferation response of the HeLa cells and resulted in apoptotic-like blebbing of the plasma membrane without causing DNA fragmentation. OsRIP1 labeled with FITC accumulated at the cell surface. Pull-down assays identified ASPP1 (Apoptosis-Stimulating Protein of p53 1) and IFITM3 (interferon-induced transmembrane protein 3) as potential interaction partners for OsRIP1. Transcript levels for several critical genes related to different signaling pathways were quantified by RT-qPCR. OsRIP1 provoked HeLa cells to undergo caspase-independent cell death, associated with a significant transcriptional upregulation of the apoptotic gene PUMA, interferon regulatory factor 1 (IRF1) and the autophagy-related marker LC3. No changes in caspase activities were observed. Together, these data suggest that apoptotic-like events were involved in OsRIP1-driven caspase-independent cell death that might trigger the IRF1 signaling pathway and LC3-mediated autophagy.}},
  articleno    = {{112590}},
  author       = {{Chen, Simin and Figueiredo Lossio, Claudia and Verbeke, Isabel and Verduijn, Joost and Parakhonskiy, Bogdan and Van der Meeren, Louis and Chen, Pengyu and De Zaeytijd, Jeroen and Skirtach, Andre and Van Damme, Els}},
  issn         = {{0278-6915}},
  journal      = {{FOOD AND CHEMICAL TOXICOLOGY}},
  keywords     = {{Toxicology,General Medicine,Food Science,Ribosome-inactivating protein,Anti-cancer,Caspase independent apoptosis,Cell blebbing,Cell death,FUSION PROTEIN,CYCLE ARREST,DNA-DAMAGE,CANCER,NECROPTOSIS,EXPRESSION,MITOPHAGY,CLEAVAGE,SURVIVAL,DOMAIN}},
  language     = {{eng}},
  pages        = {{11}},
  title        = {{The type-1 ribosome-inactivating protein OsRIP1 triggers caspase-independent apoptotic-like death in HeLa cells}},
  url          = {{http://doi.org/10.1016/j.fct.2021.112590}},
  volume       = {{157}},
  year         = {{2021}},
}

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