ArticleInfectious agents and cancer2018
Glycogene expression profiles based on microarray data from cervical carcinoma HeLa cells with partially silenced E6 and E7 HPV oncogenes.
Article in Infectious agents and cancer, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Who cites it
7 citing papers in PubMed, 15 citations in OpenAlex.
- hnRNP E1 Regulates HPV16 Oncogene Expression and Inhibits Cervical Cancerization.Frontiers in oncology · 2022Article
- Big-Data Glycomics: Tools to Connect Glycan Biosynthesis to Extracellular Communication.Trends in biochemical sciences · 2021Review
- Glycosylation in Cervical Cancer: New Insights and Clinical Implications.Frontiers in oncology · 2021Review
- Hallmarks of glycogene expression and glycosylation pathways in squamous and adenocarcinoma cervical cancer.PeerJ · 2021Article
- Glycogene expression profiles from a HaCaT cell line stably transfected with HPV16 E5 oncogene.Molecular medicine reports · 2020Article
- A lectin-based glycomic approach identifies FUT8 as a driver of radioresistance in oesophageal squamous cell carcinoma.Cellular oncology (Dordrecht, Netherlands) · 2020Article
- Recent Advances on the Molecular Mechanism of Cervical Carcinogenesis Based on Systems Biology Technologies.Computational and structural biotechnology journal · 2019Review
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundAberrant glycosylation is a characteristic of tumour cells. The expression of certain glycan structures has been associated with poor prognosis. In cervical carcinoma, changes in the expression levels of some glycogenes have been associated with lymph invasion. Human papillomavirus (HPV) infection is one of the most important factors underlying the development of cervical cancer. The HPV oncoproteins E6 and E7 have been implicated in cervical carcinogenesis and can modify the host gene expression profile. The roles of these oncoproteins in glycosylation changes have not been previously reported.
methodsTo determine the effect of the E6 and E7 oncoproteins on glycogene expression we partially silenced the E6 and E7 oncogenes in HeLa cells, we performed a microarray expression assay to identify altered glycogenes and quantified the mRNA levels of glycogenes by RT-qPCR. A protein-protein interaction network was constructed to identify potentially altered glycosylation pathways.
resultsThe microarray analysis showed 9 glycogenes that were upregulated and 7 glycogenes that were downregulated in HeLa shE6/E7 cells. Some of these genes participate in glycosylation related to Notch proteins and O-glycans antigens.
conclusionsOur results support that E6 and E7 oncoproteins could modify glycogene expression the products of which participate in the synthesis of structures implicated in proliferation, adhesion and apoptosis.
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