Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2002-6-14
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
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
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0026-895X
pubmed:author
pubmed:issnType
Print
pubmed:volume
62
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
173-80
pubmed:dateRevised
2009-11-19
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
pubmed:year
2002
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.
pubmed:affiliation
Laboratory of Molecular Immunology, Rega Institute for Medical Research, University of Leuven, Leuven, Belgium.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't