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Title

Glucose-regulated protein 78: A new partner of p53 in trophoblast

Authors
Shin-ya, Kasuo
Tomida, A.
Tsuruo, T.
Published in Proteomics. 2009, vol. 9, no. 23, p. 5316-5327
Abstract Although wild-type p53 protein is overexpressed in first trimester trophoblast, it is inactive towards its target genes Metalloproteinase 2 and 9. This seems to be due to a complex mechanism of inactivation and stabilization of p53 relying on the formation of protein complexes involving the N-terminus of p53. To detect the proteins associated with this sequence, we incubated biotinylated p53 N-terminal peptide in cytotrophoblastic cell medium 24 h before lysis of cells. We purified the proteins retained on biotinylated peptide using a neutravidin affinity column. Proteins were then identified by peptide mass finger printing followed or not by peptide fragmentation sequencing. Among these proteins, we identified glucose-regulated protein 78 (GRP78) and verified its interaction with p53 in trophoblastic cells by immunoprecipitation and Western blot analysis. Moreover, the decreased expression of GRP78 induced by GRP78siRNA or versipelostatin decreased the formation of high molecular weight p53 complexes and p53 monomer and increased trophoblastic invasion. These results suggest that GRP78 is involved in inactivation and stabilization of p53 and in the regulation of trophoblastic invasion.
Identifiers
PMID: 20017148
Full text
Article (Published version) (395 Kb) - document accessible for UNIGE members only Limited access to UNIGE
Other version: http://doi.wiley.com/10.1002/pmic.200800865
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Research group Laboratoire de biologie des tumeurs gynécologiques et du développement (927)
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(ISO format)
ARNAUDEAU, Serge et al. Glucose-regulated protein 78: A new partner of p53 in trophoblast. In: Proteomics, 2009, vol. 9, n° 23, p. 5316-5327. https://archive-ouverte.unige.ch/unige:46772

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Deposited on : 2015-02-18

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