Regulation of NF-kB Signalling Through the PR55β-RelA Interaction in Osteoblasts
| Autor: | Goro Sugiyama, Yukiko Ohyama, Tomohiro Yamada, Wataru Kumamaru, Azusa Suzuki, Yoshihide Mori |
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| Rok vydání: | 2020 |
| Předmět: |
Cancer Research
Immunoprecipitation Protein subunit Immunocytochemistry Stimulation Fibroblast growth factor Models Biological General Biochemistry Genetics and Molecular Biology Cell Line Dephosphorylation Mice 03 medical and health sciences 0302 clinical medicine medicine Animals Humans Protein Phosphatase 2 Phosphorylation Pharmacology Osteoblasts Chemistry NF-kappa B Transcription Factor RelA Osteoblast Protein phosphatase 2 Cell biology medicine.anatomical_structure 030220 oncology & carcinogenesis Fibroblast Growth Factor 2 Protein Binding Signal Transduction Research Article |
| Zdroj: | In Vivo. 34:601-608 |
| ISSN: | 1791-7549 0258-851X |
| DOI: | 10.21873/invivo.11813 |
| Popis: | Background/aim Nuclear factor kappa B (NF-kB) signalling including the RelA subunit is activated upon fibroblast growth factor (FGF) stimulation. A clear understanding of the mechanisms underlying this action will provide insights into molecular targeting therapy. Furthermore, protein phosphatase 2A (PP2A) is involved in RelA dephosphorylation, but little is known about the underlying mechanism. Materials and methods Because the regulatory subunits of PP2A drive NF-kB signalling via RelA, we used qRT-PCR and immunoblot analysis to investigate the expression of these subunits in MC3T3-E1 cells. We examined weather FGF2 interacts with NF-kB using immunocytochemistry (IC), immunoprecipitation (IP), and pull-down assay (PD) using recombinant proteins. Results PR55β expression was increased, whereas activated RelA was dephosphorylated upon FGF2 stimulation. Further, the interaction of PR55β with RelA was confirmed by IC, IP, and PD. Conclusion FGF2-induced PR55β directly interacts with RelA and regulates NF-kB signalling. |
| Databáze: | OpenAIRE |
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