| Human keratinocytes release high levels of inducible heat shock protein 70 that enhances peptide uptake. | |
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MedLine Citation:
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PMID: 21539621 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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Background: The stress-inducible chaperone heat shock protein (HSP) 70 is considered a 'danger signal' if released into the extracellular environment. It has been proposed to play a role in the pathogenesis of skin diseases such as psoriasis and lupus erythematosus (LE). Objectives: The aim of this study was to decipher the role of human primary keratinocytes with regard to release and reactivity to HSP70. Methods: We determined HSP70 and IFNγ in cell supernatants by ELISA. Uptake of labelled HSP70 or labelled peptide by human primary keratinocytes or macrophages was analysed by flow cytometry and fluorescent microscopy. Results: We found that living keratinocytes are an important source of HSP70 in the skin compartment. They release considerably more HSP70 than fibroblasts, macrophages or lymphocytes. Interestingly, keratinocytes also bind and internalise HSP70/HSP70-peptide complexes. TNFα, IL-27 as well as HMGB-1 enhanced the uptake of HSP70. No difference with regard to HSP70 release or uptake was observable between keratinocytes from healthy donors or patients with cutaneous LE. Keratinocytes pulsed with HSP70-peptide complexes significantly increased IFNγ production by autologous T cells. Conclusions: Production and uptake of inducible HSP70 by keratinocytes may critically influence the chronic course of inflammatory skin diseases. |
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Authors:
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Dong Wang; Britta Eiz-Vesper; Jana Zeitvogel; Ralf Dressel; Thomas Werfel; Miriam Wittmann |
Publication Detail:
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Type: JOURNAL ARTICLE Date: 2011-5-4 |
Journal Detail:
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Title: Experimental dermatology Volume: - ISSN: 1600-0625 ISO Abbreviation: - Publication Date: 2011 May |
Date Detail:
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Created Date: 2011-5-4 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 9301549 Medline TA: Exp Dermatol Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Copyright Information:
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© 2011 John Wiley & Sons A/S. |
Affiliation:
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Division of Immunodermatology and Allergy Research, Department of Dermatology and Allergy, Hannover Medical School, Hannover, Germany Institute for Transfusion Medicine, Hannover Medical School, Hannover, Germany Department of Cellular and Molecular Immunology, University of Göttingen, Göttingen, Germany Institute of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, UK. |
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