Heat shock proteins form part of a danger signal cascade in response to lipopolysaccharide and GroEL

Hdl Handle:
http://hdl.handle.net/10034/95141
Title:
Heat shock proteins form part of a danger signal cascade in response to lipopolysaccharide and GroEL
Authors:
Davies, Emma L.; Bacelar, Maria M. F. V. G.; Marshall, Michael J.; Johnson, E.; Wardle, T. D.; Andrew, Sarah M.; Williams, John H. H.
Abstract:
An increasing number of cell types, including peripheral blood mononuclear cells (PBMCs), have been demonstrated to release heat shock proteins (Hsps). This paper investigates further the hypothesis that Hsps are danger signals. PBMCs and Jurkat cells released Hsp70 (0·22 and 0·7 ng/106 cells, respectively) into medium over 24 h at 37°C. Release of Hsp70 was stimulated 10-fold by GroEL (P < 0·001) and more than threefold by lipopolysaccharide (LPS) (P < 0·001). Although Hsp60 could be detected in the medium of cells cultured at 37°C for 24 h, the low rates of release were due probably to cell damage. Significant release of Hsp60 was observed when Jurkat cells were exposed to GroEL (2·88 ng/106 cells) or LPS (1·40 ng/106 cells). The data are consistent with the hypothesis that Hsp70 and Hsp60 are part of a danger signalling cascade in response to bacterial infection.
Affiliation:
University of Chester ; University of Chester ; Charles Salt Centre, The Robert Jones and Agnes Hunt Orthopaedic Hospital, Oswestry ; Spinal Studies, The Robert Jones and Agnes Hunt Orthopaedic Hospital, Oswestry ; Countess of Chester Hospital ; University of Chester ; University of Chester
Citation:
Clinical and Experimental Immunology, 451(1), 2006, pp. 183-189
Publisher:
Wiley
Journal:
Clinical and Experimental Immunology
Publication Date:
Apr-2006
URI:
http://hdl.handle.net/10034/95141
DOI:
10.1111/j.1365-2249.2006.03109.x
Additional Links:
http://www3.interscience.wiley.com/journal/117996139
Type:
Article
Language:
en
Description:
This article is not available through ChesterRep.
ISSN:
0009-9104; 1365-2249
Sponsors:
This article was submitted to the RAE2008 for the University of Chester - Allied Health Professions and Studies.
Appears in Collections:
Biological Sciences

Full metadata record

DC FieldValue Language
dc.contributor.authorDavies, Emma L.en
dc.contributor.authorBacelar, Maria M. F. V. G.en
dc.contributor.authorMarshall, Michael J.en
dc.contributor.authorJohnson, E.en
dc.contributor.authorWardle, T. D.en
dc.contributor.authorAndrew, Sarah M.en
dc.contributor.authorWilliams, John H. H.en
dc.date.accessioned2010-03-29T11:10:14Zen
dc.date.available2010-03-29T11:10:14Zen
dc.date.issued2006-04en
dc.identifier.citationClinical and Experimental Immunology, 451(1), 2006, pp. 183-189en
dc.identifier.issn0009-9104en
dc.identifier.issn1365-2249en
dc.identifier.doi10.1111/j.1365-2249.2006.03109.xen
dc.identifier.urihttp://hdl.handle.net/10034/95141en
dc.descriptionThis article is not available through ChesterRep.en
dc.description.abstractAn increasing number of cell types, including peripheral blood mononuclear cells (PBMCs), have been demonstrated to release heat shock proteins (Hsps). This paper investigates further the hypothesis that Hsps are danger signals. PBMCs and Jurkat cells released Hsp70 (0·22 and 0·7 ng/106 cells, respectively) into medium over 24 h at 37°C. Release of Hsp70 was stimulated 10-fold by GroEL (P < 0·001) and more than threefold by lipopolysaccharide (LPS) (P < 0·001). Although Hsp60 could be detected in the medium of cells cultured at 37°C for 24 h, the low rates of release were due probably to cell damage. Significant release of Hsp60 was observed when Jurkat cells were exposed to GroEL (2·88 ng/106 cells) or LPS (1·40 ng/106 cells). The data are consistent with the hypothesis that Hsp70 and Hsp60 are part of a danger signalling cascade in response to bacterial infection.en
dc.description.sponsorshipThis article was submitted to the RAE2008 for the University of Chester - Allied Health Professions and Studies.en
dc.language.isoenen
dc.publisherWileyen
dc.relation.urlhttp://www3.interscience.wiley.com/journal/117996139en
dc.subjectdanger signalsen
dc.subjectGroELen
dc.subjectHsp60 releaseen
dc.subjectHsp70 releaseen
dc.subjectLPSen
dc.subjectlymphocytesen
dc.subjectperipheral blood mononuclear cellsen
dc.titleHeat shock proteins form part of a danger signal cascade in response to lipopolysaccharide and GroELen
dc.typeArticleen
dc.contributor.departmentUniversity of Chester ; University of Chester ; Charles Salt Centre, The Robert Jones and Agnes Hunt Orthopaedic Hospital, Oswestry ; Spinal Studies, The Robert Jones and Agnes Hunt Orthopaedic Hospital, Oswestry ; Countess of Chester Hospital ; University of Chester ; University of Chesteren
dc.identifier.journalClinical and Experimental Immunologyen
All Items in ChesterRep are protected by copyright, with all rights reserved, unless otherwise indicated.