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dc.contributor.authorDavies, Emma L.*
dc.contributor.authorBacelar, Maria M. F. V. G.*
dc.contributor.authorMarshall, Michael J.*
dc.contributor.authorJohnson, E.*
dc.contributor.authorWardle, T. D.*
dc.contributor.authorAndrew, Sarah M.*
dc.contributor.authorWilliams, John H. H.*
dc.date.accessioned2010-03-29T11:10:14Z
dc.date.available2010-03-29T11:10:14Z
dc.date.issued2006-05-26
dc.identifier.citationClinical and Experimental Immunology, 451(1), 2006, pp. 183-189
dc.identifier.issn0009-9104en
dc.identifier.issn1365-2249en
dc.identifier.doi10.1111/j.1365-2249.2006.03109.x
dc.identifier.urihttp://hdl.handle.net/10034/95141
dc.descriptionThis article is not available through ChesterRep.
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.
dc.description.sponsorshipThis article was submitted to the RAE2008 for the University of Chester - Allied Health Professions and Studies.
dc.language.isoenen
dc.publisherWiley
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.typeArticle
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 Chester
dc.identifier.journalClinical and Experimental Immunologyen
html.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.


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