tailieunhanh - Báo cáo khoa học: Proteomic and biochemical analysis of 14-3-3-binding proteins during C2-ceramide-induced apoptosis

14-3-3 is a family of proteins comprising several isoforms that, in many cases, promote cell survival by association with proapoptotic proteins. This study was designed to obtain further understanding of the 14-3-3 role in apoptosis regulation, by analyzing apoptosis-related protein–14-3-3 interactions. | Proteomic and biochemical analysis of 14-3-3-binding proteins during C2-ceramide-induced apoptosis Mercedes Pozuelo-Rubio Centro Andaluz de Biologia Molecular y Medicina Regenerativa Consejo Superior de Investigaciones Cientificas Sevilla Spain Keywords 14-3-3 apoptosis C2-ceramide Hela cells proteomics Correspondence M. Pozuelo-Rubio CABIMER SC4 Americo Vespucio s n Sevilla 41092 Spain Fax 34 954 461664 Tel 34 600826730 E-mail merce_pozo@ Received 14 March 2010 revised 28 May 2010 accepted 3 June 2010 doi 14-3-3 is a family of proteins comprising several isoforms that in many cases promote cell survival by association with proapoptotic proteins. This study was designed to obtain further understanding of the 14-3-3 role in apoptosis regulation by analyzing apoptosis-related protein-14-3-3 interactions. Western blot analysis of an eluted fraction from the 14-3-3-affinity chromatography column identified proapoptotic proteins as receptor-interacting protein 3 and Bcl-2-antagonist killer as new phophorylation-dependent 14-3-3-binding proteins under physiological conditions. The apoptosis inducer C2-ceramide promoted decay of the 14-3-3-binding signal of protein cell extracts. Investigation of the role of 14-3-3 in C2-ceramide-induced apoptosis showed that depletion of the 14-3-3f isoform sensitized to cell death whereas overexpression of this isoform delayed cell death. A combination of tandem affinity purification and liquid chromatography-tandem MS techniques identified 15 proteins involved in cell survival processes whose 14-3-3-binding status changed during C2-ceramide-induced apoptosis. Under physiological conditions desmin was clearly identified as a new 14-3-3-interactor protein and vasodilator-stimulated phosphoprotein nucleophosmin and calmodulin whose 14-3-3 binding was suggested by others on the basis of MS analysis were confirmed here as phosphorylation-dependent 14-3-3-associated proteins. Interestingly proteins .

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