Source:http://linkedlifedata.com/resource/pubmed/id/11058579
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
11
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pubmed:dateCreated |
2000-11-28
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pubmed:abstractText |
The myeloid-related proteins MRP8 (S100A8) and MRP14 (S100A9), two members of the S100 family of calcium-binding proteins, are co-expressed and form a cell-surface and cytoskeleton-associated heterodimer upon calcium mobilization which is recognized by the mAb 27E10. The heterodimer is abundantly expressed in the cytoplasm of granulocytes and a subpopulation of blood monocytes. Previously, we and others demonstrated endothelium-associated MRP8/14 in inflamed tissues in the vicinity of transmigrating leukocytes, suggesting a function of the proteins in this process. Here, we demonstrate that 27E10(+) cells represent a fast-migrating monocyte subpopulation which preferentially utilizes an ICAM-1-dependent mechanism. The following observations imply a function of MRP8/14 in the transmigration process: (i) higher secretion of MRP8/14 from 27E10(+) monocytes compared to 27E10(-) monocytes after interaction with activated endothelium, (ii) higher expression of CD11b on 27E10(+) compared to 27E10(-) monocytes, (iii) up-regulation of CD11b on 27E10(-) monocytes in the presence of MRP14 or MRP8/14 heterodimers but not MRP8 and (iv) active participation of MRP14 but not of MRP8 in transmigration as shown by blocking with respective antibodies. We show that the interaction of 27E10(+) monocytes with activated endothelium leads to MRP8/14 release which may account for the high MRP8/14 concentrations in body fluids of patients with acute or chronic inflammatory diseases. Released MRP8/14 may serve a function by enhancing CD11b expression and/or affinity in human monocytes and by participating in the transendothelial migration mechanism. Thus, MRP8/14 substantially contributes to the recruitment of monocytes to an inflammatory site.
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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/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Differentiation,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Calgranulin A,
http://linkedlifedata.com/resource/pubmed/chemical/Calgranulin B,
http://linkedlifedata.com/resource/pubmed/chemical/Intercellular Adhesion Molecule-1,
http://linkedlifedata.com/resource/pubmed/chemical/S100 Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0953-8178
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
12
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1593-604
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11058579-Antibodies, Monoclonal,
pubmed-meshheading:11058579-Antigens, Differentiation,
pubmed-meshheading:11058579-Calcium-Binding Proteins,
pubmed-meshheading:11058579-Calgranulin A,
pubmed-meshheading:11058579-Calgranulin B,
pubmed-meshheading:11058579-Cell Line,
pubmed-meshheading:11058579-Cell Movement,
pubmed-meshheading:11058579-Cells, Cultured,
pubmed-meshheading:11058579-Dimerization,
pubmed-meshheading:11058579-Endothelium, Vascular,
pubmed-meshheading:11058579-Humans,
pubmed-meshheading:11058579-Immunophenotyping,
pubmed-meshheading:11058579-Intercellular Adhesion Molecule-1,
pubmed-meshheading:11058579-Monocytes,
pubmed-meshheading:11058579-S100 Proteins
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pubmed:year |
2000
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pubmed:articleTitle |
Transendothelial migration of 27E10+ human monocytes.
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pubmed:affiliation |
Institute of Experimental Dermatology, University of Münster, von-Esmarch-Strasse 56, 48149 Münster, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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