| Chemerin activation by serine proteases of the coagulation, fibrinolytic, and inflammatory cascades. | |
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MedLine Citation:
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PMID: 16096270 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Proteases function at every level in host defense, from regulating vascular hemostasis and inflammation to mobilizing the "rapid responder" leukocytes of the immune system by regulating the activities of various chemoattractants. Recent studies implicate proteolysis in the activation of a ubiquitous plasma chemoattractant, chemerin, a ligand for the G-protein-coupled receptor CMKLR1 present on plasmacytoid dendritic cells and macrophages. To define the pathophysiologic triggers of chemerin activity, we evaluated the ability of serum- and inflammation-associated proteases to cleave chemerin and stimulate CMKLR1-mediated chemotaxis. We showed that serine proteases factor XIIa and plasmin of the coagulation and fibrinolytic cascades, elastase and cathepsin G released from activated neutrophil granules and mast cell tryptase are all potent activators of chemerin. Activation results from cleavage of the labile carboxyl terminus of the chemoattractant at any of several different sites. Activation of chemerin by the serine protease cascades that trigger rapid defenses in the body may direct CMKLR1-positive plasmacytoid dendritic cell and tissue macrophage recruitment to sterile sites of tissue damage, as well as trafficking to sites of infectious and allergic inflammation. |
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Authors:
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Brian A Zabel; Samantha J Allen; Paulina Kulig; Jessica A Allen; Joanna Cichy; Tracy M Handel; Eugene C Butcher |
Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S. Date: 2005-08-11 |
Journal Detail:
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Title: The Journal of biological chemistry Volume: 280 ISSN: 0021-9258 ISO Abbreviation: J. Biol. Chem. Publication Date: 2005 Oct |
Date Detail:
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Created Date: 2005-10-10 Completed Date: 2005-12-13 Revised Date: 2009-11-19 |
Medline Journal Info:
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Nlm Unique ID: 2985121R Medline TA: J Biol Chem Country: United States |
Other Details:
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Languages: eng Pagination: 34661-6 Citation Subset: IM |
Affiliation:
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Laboratory of Immunology and Vascular Biology, Department of Pathology, Stanford University School of Medicine, Stanford, California 94305, USA. bazabel@alum.mit.edu |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Sequence Baculoviridae / genetics Binding Sites Cathepsin G Cathepsins / chemistry, pharmacology Chemokines / chemistry* Chemotaxis Culture Media, Conditioned / pharmacology Culture Media, Serum-Free / pharmacology Dendritic Cells / cytology Escherichia coli / metabolism Factor XIIa / chemistry Fibrinolysin / chemistry, metabolism Humans Inflammation Ligands Macrophages / cytology, metabolism Mass Spectrometry Mast Cells / cytology Models, Biological Molecular Sequence Data Neutrophils / metabolism Pancreatic Elastase / chemistry, metabolism Plasmacytoma / metabolism Protein Structure, Tertiary Recombinant Fusion Proteins / chemistry Serine Endopeptidases / chemistry*, pharmacology Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Time Factors Transfection Trypsin / chemistry Tryptases |
| Grant Support | |
ID/Acronym/Agency:
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AI-37832/AI/NIAID NIH HHS; AI-47822/AI/NIAID NIH HHS; AI-59635/AI/NIAID NIH HHS; AI37113-09/AI/NIAID NIH HHS; DK56339/DK/NIDDK NIH HHS; GM-37734/GM/NIGMS NIH HHS; HL-67674/HL/NHLBI NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Chemokines; 0/Culture Media, Conditioned; 0/Culture Media, Serum-Free; 0/Ligands; 0/Recombinant Fusion Proteins; 0/chemerin, human; EC 3.4.-/Cathepsins; EC 3.4.21.-/Serine Endopeptidases; EC 3.4.21.20/CTSG protein, human; EC 3.4.21.20/Cathepsin G; EC 3.4.21.36/Pancreatic Elastase; EC 3.4.21.38/Factor XIIa; EC 3.4.21.4/Trypsin; EC 3.4.21.59/Tryptases; EC 3.4.21.7/Fibrinolysin |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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