| Autor: |
Gojanovich AD; Laboratorio de Integración de Señales Celulares. Instituto de Histología y Embriología de Mendoza (IHEM/CONICET-UNCuyo), School of Medicine, National University of Cuyo, Mendoza, Argentina., Bustos DM; Laboratorio de Integración de Señales Celulares. Instituto de Histología y Embriología de Mendoza (IHEM/CONICET-UNCuyo), School of Medicine, National University of Cuyo, Mendoza, Argentina., Uhart M; Laboratorio de Integración de Señales Celulares. Instituto de Histología y Embriología de Mendoza (IHEM/CONICET-UNCuyo), School of Medicine, National University of Cuyo, Mendoza, Argentina. |
| Jazyk: |
angličtina |
| Zdroj: |
Biochemistry and biophysics reports [Biochem Biophys Rep] 2016 May 30; Vol. 7, pp. 106-112. Date of Electronic Publication: 2016 May 30 (Print Publication: 2016). |
| DOI: |
10.1016/j.bbrep.2016.05.020 |
| Abstrakt: |
The 14-3-3 protein family interacts with more than 2000 different proteins in mammals, as a result of its specific phospho-serine/phospho-threonine binding activity. Seven paralogs are strictly conserved in mammalian species. Here, we show that during adipogenic differentiation of 3T3-L1 preadipocytes, the level of each 14-3-3 protein paralog is regulated independently. For instance 14-3-3β, γ, and η protein levels are increased compared to untreated cells. In contrast, 14-3-3ε protein levels decreased after differentiation while others remained constant. In silico analysis of the promoter region of each gene showed differences that explain the results obtained at mRNA and protein levels. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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