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Proteomic identification of glucocorticoid receptor interacting proteins
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2006 (English)In: Proteomics, ISSN 1615-9853, Vol. 6, no 10, p. 3114-26Article in journal (Refereed) Published
Abstract [en]

The glucocorticoid receptor (GR) acts as a ligand dependent transcription factor but can also cross talk with other signaling pathways via protein-protein interactions. In this paper we describe methods to study novel cytosolic GR interacting proteins, using mAb based immunoaffinity chromatography of GR from rat liver cytosol. Co-purifying proteins were identified by 2-DE in combination with MALDI-TOF-MS. Non-liganded/non-activated and in vitro liganded/activated GR, respectively, co-purifies with specific sets of proteins. Of these 34 were conclusively identified, seven have previously been reported to be part of the GR-complex, revealing 27 new possible interacting candidates for the GR-complex. Of the novel GR interacting proteins the major vault protein, TATA binding interacting protein 49a and glycoprotein PP63 were of special interest. Furthermore, using 2-D DIGE we show that the set of proteins interacting with non-liganded GR is distinctly different in protein amount compared to the proteins found with liganded/activated GR. This suggests the presence of different GR complexes in the cell, which was further substantiated by the finding of several separate GR native protein complexes, "GR-receptosomes", using blue native gel electrophoresis. Our findings suggest the existence of several new mechanisms for GR signaling and regulation.

Place, publisher, year, edition, pages
2006. Vol. 6, no 10, p. 3114-26
Keyword [en]
Animals, Antibodies; Monoclonal, Cell Line; Tumor, Chromatography; Affinity, Cytosol/metabolism, Electrophoresis; Gel; Two-Dimensional, Electrophoresis; Polyacrylamide Gel, Immunoblotting, Ligands, Liver/metabolism, Protein Interaction Mapping, Proteome/*metabolism, Rats, Receptors; Glucocorticoid/agonists/*metabolism, Spectrometry; Mass; Matrix-Assisted Laser Desorption-Ionization
Identifiers
URN: urn:nbn:se:umu:diva-11756PubMedID: 16619302OAI: oai:DiVA.org:umu-11756DiVA, id: diva2:151427
Available from: 2007-03-08 Created: 2007-03-08 Last updated: 2011-01-11Bibliographically approved

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CiteExportLink to record
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Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
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  • de-DE
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