| 70-kDa-heat shock protein presents an adjustable lectinic activity towards O-linked N-acetylglucosamine. | |
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MedLine Citation:
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PMID: 15158436 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Numerous works demonstrated that the dynamic O-GlcNAc glycosylation could protect against the proteasomal degradation by modifying the target proteins and the proteasome itself. Considering that Hsp70 is a crucial component in the quality control of protein conformation in the proteasomal pathway, we investigated the possibility that Hsp70 physically interacts with O-GlcNAc proteins through a lectinic activity. First, we demonstrate that in HepG2 cells, Hsp70 can specifically bind to O-GlcNAc residues but also is itself modified by O-GlcNAc. Second, when cells were deprived of glucose (nutrient stress), Hsp70 lectinic activity markedly increased whereas its glycosylation dramatically decreased. On the other hand, a 42 degrees C thermic stress did not affect any of these features. Lastly, the nature of O-GlcNAc modified proteins co-immunoprecipitating with Hsp70 was similar for cells submitted to the thermic and to nutrient stress. These results strongly suggest that O-GlcNAc influences protein stability through specific interaction with 70-kDa-heat shock protein members. |
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Authors:
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Céline Guinez; Jérôme Lemoine; Jean-Claude Michalski; Tony Lefebvre |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Biochemical and biophysical research communications Volume: 319 ISSN: 0006-291X ISO Abbreviation: Biochem. Biophys. Res. Commun. Publication Date: 2004 Jun |
Date Detail:
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Created Date: 2004-05-25 Completed Date: 2004-07-12 Revised Date: 2008-11-21 |
Medline Journal Info:
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Nlm Unique ID: 0372516 Medline TA: Biochem Biophys Res Commun Country: United States |
Other Details:
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Languages: eng Pagination: 21-6 Citation Subset: IM |
Affiliation:
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UMR 8576 du CNRS, IFR 118, Unité de Glycobiologie Structurale et Fonctionnelle, Bâtiment C9, Cité Scientifique, 59655 Villeneuve d'Ascq cedex, France. |
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| MeSH Terms | |
Descriptor/Qualifier:
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Acetylglucosamine
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chemistry* Blotting, Western Cell Line Cell Line, Tumor Electrophoresis, Polyacrylamide Gel Glucose / chemistry Glycosylation HSP70 Heat-Shock Proteins / metabolism* Humans Lectins / chemistry* Models, Chemical Precipitin Tests Protein Binding Protein Conformation Protein Structure, Tertiary Stress, Physiological |
| Chemical | |
Reg. No./Substance:
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0/HSP70 Heat-Shock Proteins; 0/Lectins; 50-99-7/Glucose; 7512-17-6/Acetylglucosamine |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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