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Retinoic Acid Treatment induces rapid phosphorylation of nuclear proteins in neuroblastoma cells.

AutorLaserna Mendieta, Emilio J.; Sanz, Libia ; Calvete, Juan J. ; Barettino, Domingo
Fecha de publicación2007
CitaciónJoint Meeting: 2nd Congress of the Spanish Proteomics Society and 1st Meeting of the European Proteomics Association. (2007)
ResumenRetinoic acid (RA), the active form of vitamin A, induces neuroblastoma cells SH-SY5Y to differentiate. In addition to its classical transcriptional actions regulating the expression of specific genes, RA acts in an extra-genomic way, modulating the activity of relevant signalling cascades. In particular, RA treatment activates PI3K/Akt signalling pathway, and this activation is an essential requirement for neural differentiation (López-Carballo G. et al., J. Biol. Chem. 277, 25297-25304, 2002). Western blots using an antibody which specifically recognizes the phosphorylation site of Akt have demonstrated that Akt activation in response to RA treatment produced a rapid phosphorylation of downstream substrates. Moreover, RA treatment resulted in rapid phosphorylation of well-known targets of Akt, such as mTOR and the ribosomal kinase p70S6, and other proteins, as CREB and histone H3, which are likely targets of RA non-genomic actions according to the scientific literature. We have carried out a proteomic approach in order to identify novel nuclear proteins whose phosphorylation state is modified by these extra-genomic actions of RA. Nuclei from control and RA-treated (1mM, 30 min) neuroblastoma cells were obtained, and nuclear phospho-proteins were purified by affinity chromatrography. The phosph-oproteins were separated by 2-D gel electrophoresis (IEF/SDS-PAGE), and comparison of 2-D protein patterns using a bioinformatic software package allowed the selection of a series of spots that have undergone changes on their phosphorylation state. These spots with differential expression could be identified by mass spectrometry analysis as the proteins nucleophosmin/B23, hnRNP-C1/C2, hnRNP-K, HMGB1, PABP and histone H1.5. All those proteins have a nuclear distribution and phosphorylation sites. Finally, the observed RA-induced phosphorylation changes in these proteins were confirmed in 2-D western blots and immunoprecipitation experiments.
DescripciónPóster original presentado Joint Meeting: 2nd Congress of the Spanish Proteomics Society and 1st Meeting of the European Proteomics Association, celebrado en Valencia (España), en 2007
URIhttp://hdl.handle.net/10261/123178
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