Source:http://linkedlifedata.com/resource/pubmed/id/10570306
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
11
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| pubmed:dateCreated |
1999-12-20
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| pubmed:abstractText |
Chemokines are important mediators of leukocyte migration during the inflammatory response. Post-translational modifications affect the biological potency of chemokines. In addition to previously identified NH2-terminally truncated forms, COOH-terminally truncated forms of the CXC chemokine murine granulocyte chemotactic protein-2 (GCP-2) were purified from conditioned medium of stimulated fibroblasts. The truncations generated 28 natural murine GCP-2 isoforms containing 69-92 residues, including most intermediate forms. Both NH2- and COOH-terminal truncations of GCP-2 resulted in enhanced chemotactic potency for human and murine neutrophils in vitro. The truncated isoform GCP-2(9-78) was 30-fold more potent than intact GCP-2(1-92)/LPS-induced CXC chemokine (LIX) at inducing an intracellular calcium increase in human neutrophils. After intradermal injection in mice, GCP-2(9-78) was also more effective than GCP-2(1-92)/LIX at inducing neutrophil infiltration. Similar to human IL-8 and GCP-2, murine GCP-2(9-78) and macrophage inflammatory protein-2 (MIP-2) induced calcium increases in both CXCR1 and CXCR2 transfectants. Murine GCP-2(9-78) could desensitize the calcium response induced by MIP-2 in human neutrophils and vice versa. Furthermore, MIP-2 and truncated GCP-2(9-78), but not intact GCP-2(1-92)/LIX, partially desensitized the calcium response to human IL-8 in human neutrophils. Taken together, these findings point to an important role of post-translationally modified GCP-2 to replace IL-8 in the mouse.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
AIM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD,
http://linkedlifedata.com/resource/pubmed/chemical/CXCL6 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Chemokine CXCL2,
http://linkedlifedata.com/resource/pubmed/chemical/Chemokine CXCL6,
http://linkedlifedata.com/resource/pubmed/chemical/Chemokines, CXC,
http://linkedlifedata.com/resource/pubmed/chemical/Monokines,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Isoforms,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Chemokine,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Interleukin,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Interleukin-8A,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Interleukin-8B
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| pubmed:status |
MEDLINE
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| pubmed:month |
Dec
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| pubmed:issn |
0022-1767
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
1
|
| pubmed:volume |
163
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| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
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| pubmed:pagination |
6155-63
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| pubmed:dateRevised |
2007-11-15
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| pubmed:meshHeading |
pubmed-meshheading:10570306-Amino Acid Sequence,
pubmed-meshheading:10570306-Animals,
pubmed-meshheading:10570306-Antigens, CD,
pubmed-meshheading:10570306-Calcium Signaling,
pubmed-meshheading:10570306-Chemokine CXCL2,
pubmed-meshheading:10570306-Chemokine CXCL6,
pubmed-meshheading:10570306-Chemokines, CXC,
pubmed-meshheading:10570306-Chemotaxis, Leukocyte,
pubmed-meshheading:10570306-Humans,
pubmed-meshheading:10570306-Mice,
pubmed-meshheading:10570306-Molecular Sequence Data,
pubmed-meshheading:10570306-Monokines,
pubmed-meshheading:10570306-Neutrophil Infiltration,
pubmed-meshheading:10570306-Neutrophils,
pubmed-meshheading:10570306-Peptide Fragments,
pubmed-meshheading:10570306-Protein Isoforms,
pubmed-meshheading:10570306-Receptors, Chemokine,
pubmed-meshheading:10570306-Receptors, Interleukin,
pubmed-meshheading:10570306-Receptors, Interleukin-8A,
pubmed-meshheading:10570306-Receptors, Interleukin-8B,
pubmed-meshheading:10570306-Sequence Alignment,
pubmed-meshheading:10570306-Sequence Deletion,
pubmed-meshheading:10570306-Species Specificity
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| pubmed:year |
1999
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| pubmed:articleTitle |
NH2- and COOH-terminal truncations of murine granulocyte chemotactic protein-2 augment the in vitro and in vivo neutrophil chemotactic potency.
|
| pubmed:affiliation |
Laboratories ofMolecular Immunology and Immunobiology, Rega Institute for Medical Research, and Laboratory for Developmental Physiology and Molecular Biology, Zoological Institute, University of Leuven, Leuven, Belgium. anja.wuyts@rega.kuleuven.ac.be
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| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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