Source:http://linkedlifedata.com/resource/pubmed/id/14990582
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
19
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| pubmed:dateCreated |
2004-5-4
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| pubmed:abstractText |
It was recently shown that individuals carrying the naturally occurring mutant CX3CR1-Ile(249)-Met(280) (hereafter called CX3CR1-IM) have a lower risk of cardiovascular disease than individuals homozygous for the wild-type CX3CR1-Val(249)-Thr(280) (CX3CR1-VT). We report here that peripheral blood mononuclear cells (PBMC) from individuals with the CX3CR1-IM haplotype adhered more potently to membrane-bound CX3CL1 than did PBMC from homozygous CX3CR1-VT donors. Similar excess adhesion was observed with CX3CR1-IM-transfected human embryonic kidney (HEK) cell lines tested with two different methods: the parallel plate laminar flow chamber and the dual pipette aspiration technique. Suppression of the extra adhesion in the presence of pertussis toxin indicates that G-protein mediated the underlying transduction pathway, in contrast to the G-protein-independent adhesion previously described for CX3CR1-VT. Surprisingly, HEK and PBMC that expressed CX3CR1-IM and -VT were indistinguishable when tested with the soluble form of CX3CL1 for chemotaxis, calcium release, and binding capacity. In conclusion, only the membrane-anchored form of CX3CL1 functionally discriminated between these two allelic isoforms of CX3CR1. These results suggest that each form of this ligand may lead to a different signaling pathway. The extra adhesion of CX3CR1-IM may be related to immune defenses and to atherogenesis, both of which depend substantially on adhesive intercellular events.
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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/CX3CR1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Isoleucine,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Methionine,
http://linkedlifedata.com/resource/pubmed/chemical/Pertussis Toxin,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Chemokine
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| pubmed:status |
MEDLINE
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| pubmed:month |
May
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| pubmed:issn |
0021-9258
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
7
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| pubmed:volume |
279
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| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
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| pubmed:pagination |
19649-57
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| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:14990582-Blotting, Western,
pubmed-meshheading:14990582-Calcium,
pubmed-meshheading:14990582-Cell Adhesion,
pubmed-meshheading:14990582-Cell Line,
pubmed-meshheading:14990582-Cell Movement,
pubmed-meshheading:14990582-Chemotaxis,
pubmed-meshheading:14990582-Flow Cytometry,
pubmed-meshheading:14990582-Homozygote,
pubmed-meshheading:14990582-Humans,
pubmed-meshheading:14990582-Isoleucine,
pubmed-meshheading:14990582-Leukocytes, Mononuclear,
pubmed-meshheading:14990582-Membrane Proteins,
pubmed-meshheading:14990582-Methionine,
pubmed-meshheading:14990582-Mutation,
pubmed-meshheading:14990582-Pertussis Toxin,
pubmed-meshheading:14990582-Protein Binding,
pubmed-meshheading:14990582-Receptors, Chemokine,
pubmed-meshheading:14990582-Signal Transduction,
pubmed-meshheading:14990582-Time Factors,
pubmed-meshheading:14990582-Transfection
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| pubmed:year |
2004
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| pubmed:articleTitle |
Enhanced adhesive capacities of the naturally occurring Ile249-Met280 variant of the chemokine receptor CX3CR1.
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| pubmed:affiliation |
Laboratoire d'Immunologie Cellulaire, INSERM U543, Faculté de Médecine Pitié-Salpêtrière, 91 Boulevard de l'Hôpital, 75013 Paris, France.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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