ArticlePloS one2008
Barnase as a new therapeutic agent triggering apoptosis in human cancer cells.
Article in PloS one, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
38 citing papers in PubMed, 82 citations in OpenAlex.
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- Novel Organomineral Complex with Prolonged Antitumor Action.International journal of molecular sciences · 2025Article
- Fusion of SARS-CoV-2 neutralizing LCB1 peptide with Bacillus amyloliquefaciens RNase improves antiviral efficacy.Scientific reports · 2025Article
- Development of Synthetic mRNAs Encoding Split Cytotoxic Proteins for Selective Cell Elimination Based on Specific Protein Detection.Pharmaceutics · 2023Article
- Magnetic Platelets as a Platform for Drug Delivery and Cell Trapping.Pharmaceutics · 2023Article
- Enhancing response of a protein conformational switch by using two disordered ligand binding domains.Frontiers in molecular biosciences · 2023Article
- Spatio-Temporal Photoactivation of Cytotoxic Proteins.Chembiochem : a European journal of chemical biology · 2022Article
- Tetracycline-controlled (TetON) gene expression system for the smut fungusFrontiers in fungal biology · 2022Article
- Barnase-Barstar Pair: Contemporary Application in Cancer Research and Nanotechnology.Molecules (Basel, Switzerland) · 2021Review
- Recombinant immunotoxins development for HER2-based targeted cancer therapies.Cancer cell international · 2021Review
- Recombinant expression of Barnase in Escherichia coli and its application in plasmid purification.Microbial cell factories · 2021Article
- Diverse protein manipulations with genetically encoded glutamic acid benzyl ester.Chemical science · 2021Article
- Natural and Designed Toxins for Precise Therapy: Modern Approaches in Experimental Oncology.International journal of molecular sciences · 2021Review
- Article
- Antibody-Mediated Enzyme Therapeutics and Applications in Glycogen Storage Diseases.Trends in molecular medicine · 2019Review
- Modulating Protein Stability to Switch Toxic Protein Function On and Off in Living Cells.Plant physiology · 2019Article
- Biological Activities of Secretory RNases: Focus on Their Oligomerization to Design Antitumor Drugs.Frontiers in immunology · 2019Review
- Surveillance of Tumour Development: The Relationship Between Tumour-Associated RNAs and Ribonucleases.Frontiers in pharmacology · 2019Review
- Updates in the Development of ImmunoRNases for the Selective Killing of Tumor Cells.Biomedicines · 2018Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundRNases are currently studied as non-mutagenic alternatives to the harmful DNA-damaging anticancer drugs commonly used in clinical practice. Many mammalian RNases are not potent toxins due to the strong inhibition by ribonuclease inhibitor (RI) presented in the cytoplasm of mammalian cells. METHODOLOGY/PRINCIPAL
findingsIn search of new effective anticancer RNases we studied the effects of barnase, a ribonuclease from Bacillus amyloliquefaciens, on human cancer cells. We found that barnase is resistant to RI. In MTT cell viability assay, barnase was cytotoxic to human carcinoma cell lines with half-inhibitory concentrations (IC(50)) ranging from 0.2 to 13 microM and to leukemia cell lines with IC(50) values ranging from 2.4 to 82 microM. Also, we characterized the cytotoxic effects of barnase-based immunoRNase scFv 4D5-dibarnase, which consists of two barnase molecules serially fused to the single-chain variable fragment (scFv) of humanized antibody 4D5 that recognizes the extracellular domain of cancer marker HER2. The scFv 4D5-dibarnase specifically bound to HER2-positive cells and was internalized via receptor-mediated endocytosis. The intracellular localization of internalized scFv 4D5-dibarnase was determined by electronic microscopy. The cytotoxic effect of scFv 4D5-dibarnase on HER2-positive human ovarian carcinoma SKOV-3 cells (IC(50) = 1.8 nM) was three orders of magnitude greater than that of barnase alone. Both barnase and scFv 4D5-dibarnase induced apoptosis in SKOV-3 cells accompanied by internucleosomal chromatin fragmentation, membrane blebbing, the appearance of phosphatidylserine on the outer leaflet of the plasma membrane, and the activation of caspase-3. CONCLUSIONS/SIGNIFICANCE: These results demonstrate that barnase is a potent toxic agent for targeting to cancer cells.
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