ArticleOncotarget2017
The cytosolic 5'-nucleotidase cN-II lowers the adaptability to glucose deprivation in human breast cancer cells.
Article in Oncotarget, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Extracting Knowledge from Machine Learning Models to Diagnose Breast Cancer.Life (Basel, Switzerland) · 2025Article
- Transcriptional and Metabolic Investigation in 5'-Nucleotidase Deficient Cancer Cell Lines.Cells · 2021Article
- Cytosolic 5'-Nucleotidase II Silencing in Lung Tumor Cells Regulates Metabolism through Activation of the p53/AMPK Signaling Pathway.International journal of molecular sciences · 2021Article
- Enhanced migration of breast and lung cancer cells deficient for cN-II and CD73 via COX-2/PGE2/AKT axis regulation.Cellular oncology (Dordrecht, Netherlands) · 2021Article
- A screening approach for the evaluation of tobacco-free 'modern oral' nicotine products using Real Time Cell Analysis.Toxicology reports · 2021Article
- Purine-Metabolising Enzymes and Apoptosis in Cancer.Cancers · 2019Review
- Expanding the clinical relevance of the 5'-nucleotidase cN-II/NT5C2.Purinergic signalling · 2018Review
- Emerging Role of Purine Metabolizing Enzymes in Brain Function and Tumors.International journal of molecular sciences · 2018Review
- Cytosolic 5'-Nucleotidase II Silencing in a Human Lung Carcinoma Cell Line Opposes Cancer Phenotype with a Concomitant Increase in p53 Phosphorylation.International journal of molecular sciences · 2018Article
- Relapsed acute lymphoblastic leukemia-specific mutations in NT5C2 cluster into hotspots driving intersubunit stimulation.Leukemia · 2018Article
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Authors and funding
10 authors.
Funding
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Abstract
The cytosolic 5'-nucleotidase cN-II is a highly conserved enzyme implicated in nucleotide metabolism. Based on recent observations suggesting additional roles not directly associated to its enzymatic activity, we studied human cancer cell models with basal or decreased cN-II expression. We developed cancer cells with stable inhibition of cN-II expression by transfection of shRNA-coding plasmids, and studied their biology. We show that human breast cancer cells MDA-MB-231 with decreased cN-II expression better adapt to the disappearance of glucose in growth medium under normoxic conditions than cells with a baseline expression level. This is associated with enhanced
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