Source:http://linkedlifedata.com/resource/pubmed/id/12065768
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2002-6-14
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pubmed:abstractText |
The recently discovered CC chemokine, regakine-1, is constitutively present in bovine serum and synergizes with the CXC chemokine interleukin-8 (IL-8) to chemoattract neutrophils. Here we show that regakine-1 cooperates with the CXC chemokine receptor 2 ligand neutrophil activating protein-2 (NAP-2) and the anaphylatoxin C5a, two other mediators of inflammation present in the circulation. Neutrophil chemotaxis was 3-fold enhanced when regakine-1 (100 ng/ml) and C5a (30 ng/ml) were combined at concentrations present in bovine or human plasma, respectively. This synergy was also observed when neutrophils were preincubated with regakine-1. Plasma chemokines such as NAP-2, beta-thromboglobulin, and hemofiltrate CC-chemokine-1 did not affect C5a chemotactic activity. The capability of regakine-1 to synergize with C5a, NAP-2, or N-formyl-methionyl-leucyl-phenylalanine (fMLP) was not observed for monocyte chemotactic protein-3 (MCP-3), another CC chemokine that weakly chemoattracts neutrophils. Regakine-1 also failed to cooperate with MCP-3 and macrophage inflammatory protein-1alpha in neutrophil chemotaxis. The receptor of regakine-1 is not known yet. Competition with labeled fMLP or C5a for binding to neutrophils or receptor transfected cell lines demonstrated that regakine-1 did not alter receptor recognition. The protein kinase inhibitors 2'-amino-3'-methoxyflavone (PD98059), wortmannin and staurosporin had no effect on the synergy between C5a and regakine-1. Although NH2-terminal truncation affects the chemotactic potency of most chemokines, it did not affect the synergistic capacity of regakine-1 with C5a on neutrophils. These findings indicate that the constitutive plasma chemokine regakine-1 is a stable enhancer of the inflammatory response and that its blockade might be beneficial in acute and systemic inflammatory disorders.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/CCL7 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Chemokine CCL4,
http://linkedlifedata.com/resource/pubmed/chemical/Chemokine CCL7,
http://linkedlifedata.com/resource/pubmed/chemical/Chemokines, CC,
http://linkedlifedata.com/resource/pubmed/chemical/Complement C5a,
http://linkedlifedata.com/resource/pubmed/chemical/Cytokines,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Macrophage Inflammatory Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Monocyte Chemoattractant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/N-Formylmethionine...,
http://linkedlifedata.com/resource/pubmed/chemical/PPBP protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/beta-Thromboglobulin,
http://linkedlifedata.com/resource/pubmed/chemical/regakine 1
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0026-895X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
62
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
173-80
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:12065768-Chemokine CCL4,
pubmed-meshheading:12065768-Chemokine CCL7,
pubmed-meshheading:12065768-Chemokines, CC,
pubmed-meshheading:12065768-Chemotaxis,
pubmed-meshheading:12065768-Complement C5a,
pubmed-meshheading:12065768-Cytokines,
pubmed-meshheading:12065768-Drug Synergism,
pubmed-meshheading:12065768-Enzyme Inhibitors,
pubmed-meshheading:12065768-Humans,
pubmed-meshheading:12065768-Macrophage Inflammatory Proteins,
pubmed-meshheading:12065768-Monocyte Chemoattractant Proteins,
pubmed-meshheading:12065768-N-Formylmethionine Leucyl-Phenylalanine,
pubmed-meshheading:12065768-Neutrophils,
pubmed-meshheading:12065768-Peptides,
pubmed-meshheading:12065768-Protein Kinase Inhibitors,
pubmed-meshheading:12065768-Protein Kinases,
pubmed-meshheading:12065768-Protein Structure, Tertiary,
pubmed-meshheading:12065768-Transfection,
pubmed-meshheading:12065768-beta-Thromboglobulin
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pubmed:year |
2002
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pubmed:articleTitle |
The unique property of the CC chemokine regakine-1 to synergize with other plasma-derived inflammatory mediators in neutrophil chemotaxis does not reside in its NH2-terminal structure.
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pubmed:affiliation |
Laboratory of Molecular Immunology, Rega Institute for Medical Research, University of Leuven, Leuven, Belgium.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
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