| Oxidative Modifications of DAMPs Suppress Inflammation: The Case for S100A8 and S100A9. | |
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MedLine Citation:
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PMID: 20919939 Owner: NLM Status: In-Data-Review |
Abstract/OtherAbstract:
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Abstract Several S100 Ca(2+)-binding proteins are considered damage-associated molecular pattern molecules (DAMPs). They are actively secreted or released from necrotic cells in response to tissue injury or stress and have various functions important in innate immunity. Here, we review several DAMPs, with particular focus on S100A8 and S100A9, which are susceptible to oxidative modifications by various forms of reactive oxygen species. We discuss the unique posttranslational modifications generated in S100A8 by hypochlorite and the likely structural consequences that alter function. We propose that some reversible modifications act as regulatory switches, representing a mechanism to arrest their novel antiinflammatory activities. These may be important in dampening mast cell activation and altering properties of the activated microcirculation to limit leukocyte adhesion, transmigration, and accumulation. S-nitrosylation of S100A8 in the vasculature could regulate nitric oxide transport and contribute to vessel reflow during resolution of inflammation. Antioxid. Redox Signal. 15, 2235-2248. |
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Authors:
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Su Yin Lim; Mark J Raftery; Carolyn L Geczy |
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Publication Detail:
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Type: Journal Article Date: 2011-04-11 |
Journal Detail:
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Title: Antioxidants & redox signaling Volume: 15 ISSN: 1557-7716 ISO Abbreviation: Antioxid. Redox Signal. Publication Date: 2011 Oct |
Date Detail:
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Created Date: 2011-09-02 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 100888899 Medline TA: Antioxid Redox Signal Country: United States |
Other Details:
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Languages: eng Pagination: 2235-48 Citation Subset: IM |
Affiliation:
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1 Centre for Infection and Inflammation Research, School of Medical Sciences, University of New South Wales , Sydney, Australia . |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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