Glycogene expression profiles based on microarray data from cervical carcinoma HeLa cells with partially silenced E6 and E7 HPV oncogenes

Aberrant 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 i...

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Bibliographic Details
Published in:Infectious agents and cancer 2018-07, Vol.13 (1), p.25-12, Article 25
Main Authors: Aco-Tlachi, Miguel, Carreño-López, Ricardo, Martínez-Morales, Patricia L, Maycotte, Paola, Aguilar-Lemarroy, Adriana, Jave-Suárez, Luis Felipe, Santos-López, Gerardo, Reyes-Leyva, Julio, Vallejo-Ruiz, Verónica
Format: Article
Language:English
Subjects:
Antigens
Apoptosis
Bladder cancer
Cervical cancer
Cervical carcinoma
Cervix
Cloning
Diagnosis
E6 oncoprotein
Gene expression
Genetic aspects
Genomes
Glycogene
Glycosylation
HeLa cells
Human papillomavirus
Laboratories
Metastasis
Microarrays
Notch1 protein
Oncogenes
Signal transduction
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Summary:Aberrant 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. To 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. The 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. Our 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.
ISSN:1750-9378
1750-9378
DOI:10.1186/s13027-018-0197-2