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. 2014 Nov 3;14:801. doi: 10.1186/1471-2407-14-801

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© Grosset et al.; licensee BioMed Central Ltd. 2014

This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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Decreased of p53 nuclear translocation through proteasomal degradation induced by cytoplasmic gal-7. (A) Cytosolic and nuclear fractions were purified from control (srα) cells and MCF-7 cells expressing wild type or mutated gal-7 after doxorubicin treatment. Expression of p53, p21 and gal-7 was measured in both fractions by Western blotting. β-tubulin and lamin A/C are shown as positive cytoplasmic and nuclear expression controls, respectively. (B) Cells were treated with 10 μM MG-132 for 0, 2, and 6 hrs. Total cellular extracts were subjected to Western blot analysis for p53, gal-7 and β-actin. Immunoprecipitation (IP) experiments showing p53 interaction with (C) wild type and (D) R74S mutant of gal-7 in MCF-7 cells. Whole-cell lysates were made from MCF-7 cells transfected with a construct expressing p53. Lysates were immunoprecipitated with anti-p53 or a control IgG antibody, and immunoblot analysis was performed with anti-gal-7.