Document Detail


Heat shock proteins form part of a danger signal cascade in response to lipopolysaccharide and GroEL.
MedLine Citation:
PMID:  16792689     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
An increasing number of cell types, including peripheral blood mononuclear cells (PBMCs), have been demonstrated to release heat shock proteins (Hsps). In this paper we investigate further the hypothesis that Hsps are danger signals. PBMCs and Jurkat cells released Hsp70 (0.22 and 0.7 ng/10(6) cells, respectively) into medium over 24 h at 37 degrees 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 degrees 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/10(6) cells) or LPS (1.40 ng/10(6) cells). The data are consistent with the hypothesis that Hsp70 and Hsp60 are part of a danger signalling cascade in response to bacterial infection.
Authors:
E L Davies; M M F V G Bacelar; M J Marshall; E Johnson; T D Wardle; S M Andrew; J H H Williams
Related Documents :
16204379 - Heat-shock protein 60 is required for blastema formation and maintenance during regener...
14724189 - Roles of compatible osmolytes and heat shock protein 70 in the induction of tolerance t...
7974879 - In vitro effects of high energy shock wave alone and combined with anticancer drugs on ...
14703799 - Sensitization of u937 cells to heat shock by oxalomalate, a competitive inhibitor of na...
11451409 - Expression of 25 kda heat shock protein by synovial type b cells of the mouse temporoma...
16676349 - Effects of sequential exposure to lipopolysaccharide and heat stress on dental pulp cells.
8110499 - Acute effects of growth factors on t-47d breast cancer cell cycle progression.
19230649 - Use of electric cell-substrate impedance sensing to assess in vitro cytotoxicity.
21964769 - The akt/foxo1/p27 pathway mediates the proliferative action of liraglutide in β cells.
Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Clinical and experimental immunology     Volume:  145     ISSN:  0009-9104     ISO Abbreviation:  Clin. Exp. Immunol.     Publication Date:  2006 Jul 
Date Detail:
Created Date:  2006-06-23     Completed Date:  2006-08-07     Revised Date:  2013-06-07    
Medline Journal Info:
Nlm Unique ID:  0057202     Medline TA:  Clin Exp Immunol     Country:  England    
Other Details:
Languages:  eng     Pagination:  183-9     Citation Subset:  IM    
Affiliation:
Chester Centre for Stress Research, Biological Sciences, University of Chester, Chester, UK.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Antigens, Bacterial / pharmacology*
Blotting, Western / methods
Cell Line
Cells, Cultured
Chaperonin 60 / analysis,  pharmacology,  secretion
HSP70 Heat-Shock Proteins / analysis,  secretion
Heat-Shock Proteins / analysis,  secretion*
Humans
Jurkat Cells
L-Lactate Dehydrogenase / analysis
Leukocytes, Mononuclear / drug effects,  secretion*
Lipopolysaccharides / pharmacology
Signal Transduction / drug effects*
Stromal Cells / drug effects,  secretion
T-Lymphocytes / drug effects,  secretion
Time Factors
Chemical
Reg. No./Substance:
0/Antigens, Bacterial; 0/Chaperonin 60; 0/HSP70 Heat-Shock Proteins; 0/Heat-Shock Proteins; 0/Lipopolysaccharides; EC 1.1.1.27/L-Lactate Dehydrogenase
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Hormonal regulation of mannan-binding lectin synthesis in hepatocytes.
Next Document:  Monocyte chemoattractant protein-1 (MCP-1) inhibits the intestinal-like differentiation of monocytes...