| Legionella pneumophila heat-shock protein-induced increase of interleukin-1 beta mRNA involves protein kinase C signalling in macrophages. | |
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MedLine Citation:
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PMID: 8943727 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Heat-shock proteins (hsp) are chaperon molecules important in protein folding and assembly. Furthermore, they may have functions in immunoregulatory processes, like T-cell stimulation and antigen presentation, which are not yet fully understood. It has been shown that several hsp of various species and family derivations modulate functions in macrophage immunity by directly increasing cytokine production. In the present study we showed that the 60,000 MW hsp of Legionella pneumophila (Lp-hsp 60) increased cellular steady-state levels of interleukin-1 beta (IL-1 beta) mRNA measured by quantitative reverse transcription-polymerase chain reaction and Northern blotting as well as IL-1 secretion, when added to cultures of thioglycollate-elicited mouse peritoneal macrophages in vitro. The level of mRNA increased in a dose-dependent manner with a minimum effective concentration of 0.5 microgram/ml and peaked 3 hr after stimulation. Lp-hsp 60-coated latex beads also increased IL-1 beta mRNA levels in the presence of cytochalasin D, which inhibits bead uptake but permits binding, indicating that binding to the macrophage surface was sufficient for induction. Accumulation of IL-1 beta mRNA was completely blocked by pretreatment with the protein kinase C (PKC) inhibitor, H7, but not decreased by prior treatment with cycloheximide. The cell lysates of macrophages stimulated with Lp-hsp 60 showed an increased PKC activity measured by phosphorylation of PKC pseudosubstrate. The IL-1 bioactivity in culture supernatants after 24 hr of stimulation with Lp-hsp 60 was increased in a dose-dependent manner but at hsp concentrations in excess of those needed to increase mRNA. Thus, the present study demonstrates that Lp-hsp 60 rapidly increases the steady-state level of IL-1 beta mRNA, possibly through a cell surface receptor system involving a PKC-dependent signalling pathway. |
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Authors:
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C Retzlaff; Y Yamamoto; S Okubo; P S Hoffman; H Friedman; T W Klein |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: Immunology Volume: 89 ISSN: 0019-2805 ISO Abbreviation: Immunology Publication Date: 1996 Oct |
Date Detail:
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Created Date: 1996-12-23 Completed Date: 1996-12-23 Revised Date: 2009-11-18 |
Medline Journal Info:
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Nlm Unique ID: 0374672 Medline TA: Immunology Country: ENGLAND |
Other Details:
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Languages: eng Pagination: 281-8 Citation Subset: IM |
Affiliation:
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Department of Medical Microbiology and Immunology, University of South Florida College of Medicine, Tampa 4799, USA. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine
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pharmacology Animals Bacterial Proteins / pharmacology* Blotting, Northern Cells, Cultured Chaperonin 60 / pharmacology* Dose-Response Relationship, Drug Female Interleukin-1 / genetics, metabolism* Legionella pneumophila* Macrophages / drug effects, enzymology, immunology* Mice Mice, Inbred BALB C Polymerase Chain Reaction Protein Kinase C / antagonists & inhibitors, metabolism* RNA, Messenger / analysis Signal Transduction / physiology |
| Grant Support | |
ID/Acronym/Agency:
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AI 16618/AI/NIAID NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Bacterial Proteins; 0/Chaperonin 60; 0/Interleukin-1; 0/RNA, Messenger; 84477-87-2/1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine; EC 2.7.11.13/Protein Kinase C |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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