| Protease-activated receptors: novel PARtners in innate immunity. | |
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MedLine Citation:
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PMID: 17977790 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Protease-activated receptors (PARs) belong to a family of G protein-coupled receptors activated by serine proteases via proteolytic cleavage. PARs are expressed on epithelial cells, endothelial cells, and leukocytes, indicating a role in controlling barrier function against external danger. During inflammation, microorganisms as well as host immune cells release various proteases activating PARs. Thus, PARs can be viewed as an integral component of the host antimicrobial alarm system. When stimulated, PARs regulate various functions of leukocytes in vivo and in vitro, revealing a novel pathway by which proteases affect innate immune responses. Understanding protease-immune interactions could lead to novel strategies for the treatment of infectious and immune-related diseases. |
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Authors:
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V Shpacovitch; M Feld; N W Bunnett; M Steinhoff |
Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't; Review Date: 2007-10-30 |
Journal Detail:
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Title: Trends in immunology Volume: 28 ISSN: 1471-4906 ISO Abbreviation: Trends Immunol. Publication Date: 2007 Dec |
Date Detail:
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Created Date: 2007-11-20 Completed Date: 2008-02-15 Revised Date: 2009-11-19 |
Medline Journal Info:
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Nlm Unique ID: 100966032 Medline TA: Trends Immunol Country: England |
Other Details:
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Languages: eng Pagination: 541-50 Citation Subset: IM |
Affiliation:
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Department of Dermatology and Ludwig Boltzmann Institute for Cell Biology of the Skin, University of Münster, D-48149 Münster, Germany. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Animals Cathepsin G Cathepsins / physiology Dendritic Cells / physiology Granzymes / physiology Humans Immunity, Innate* Macrophages / physiology Mast Cells / physiology Monocytes / physiology Neutrophils / physiology Receptors, Proteinase-Activated / physiology* Serine Endopeptidases / physiology Tryptases / physiology |
| Chemical | |
Reg. No./Substance:
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0/Receptors, Proteinase-Activated; EC 3.4.-/Cathepsins; EC 3.4.21.-/Granzymes; EC 3.4.21.-/Serine Endopeptidases; EC 3.4.21.20/CTSG protein, human; EC 3.4.21.20/Cathepsin G; EC 3.4.21.59/Tryptases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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