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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Sharma, Animesh Slupphaug, Geir Hagen, Lars Aas, Per Arne |
| Description | Author Affiliation: Hagen L ( Department of Cancer Research and Molecular Medicine and PROMEC Core Facility for Proteomics and Metabolomics, Norwegian University of Science and Technology, NTNU, N-7491 Trondheim, Norway.); Sharma A ( Department of Cancer Research and Molecular Medicine and PROMEC Core Facility for Proteomics and Metabolomics, Norwegian University of Science and Technology, NTNU, N-7491 Trondheim, Norway.); Aas PA ( Department of Cancer Research and Molecular Medicine and PROMEC Core Facility for Proteomics and Metabolomics, Norwegian University of Science and Technology, NTNU, N-7491 Trondheim, Norway.); Slupphaug G ( Department of Cancer Research and Molecular Medicine and PROMEC Core Facility for Proteomics and Metabolomics, Norwegian University of Science and Technology, NTNU, N-7491 Trondheim, Norway. Electronic address: geir.slupphaug@ntnu.no.) |
| Abstract | Transient transfection of mammalian cells with plasmid expression vectors and chemical transfection reagents is widely used to study protein transport and dynamics as well as phenotypic alterations mediated by the overexpressed protein. Despite the undisputed impact of this technique, surprisingly little is known about the cellular effects mediated by the transfection process per se. Conceivably, off-target effects could have implications upon proteins or processes being studied and understanding the molecular pathways affected would add value to the interpretation of experimental observations subsequent to cell transfection. Here we have used a SILAC-based proteomic approach to study differentially expressed proteins after transfection of HeLa cells with ECFP vector using a commonly employed non-liposome based transfection reagent, Fugene®HD. Whereas the transfection reagent itself mediated minimal effects upon protein expression, 11 proteins were found to be significantly upregulated after transfection, all of which were associated with an interferon type I/II response. The upregulated proteins might potentially inflict major cellular processes such as RNA splicing, chromatin remodeling, post-translational protein modification and cell cycle control. The results were validated by western analysis as well as quantitative RT-PCR and this demonstrated that an essentially identical response was induced in HeLa by transfection using an empty pUC18 vector, which does not contain a mammalian virus promoter, as well as a liposome-based transfection reagent, Lipofectamine $^{TM}$ 2000. Notably, no induction of the interferon response was observed in HEK293 cells, suggesting that these cells might be preferable to HeLa to avoid undesired off-target effects in transfection studies encompassing interferon-signaling and antiviral responses. |
| ISSN | 00063002 |
| Journal | Biochimica et Biophysica Acta (BBA) - Reviews on Cancer |
| Issue Number | 1 |
| Volume Number | 1854 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2015-01-01 |
| Publisher Place | Netherlands |
| Access Restriction | Open |
| Subject Keyword | Plasmids Genetics Proteome Metabolism Proteomics Transfection Blotting, Western Carbon Isotopes Chromatography, Liquid Gene Expression HEK293 Cells HeLa Cells Isotope Labeling Lipids Chemistry Lysine Reverse Transcriptase Polymerase Chain Reaction Tandem Mass Spectrometry Research Support, Non-U.S. Gov't Biochemistry |
| Content Type | Text |
| Resource Type | Article |
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