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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1995-8-15
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pubmed:abstractText |
We examined chemotaxis of human plasma cells (PCs) in response to extracellular matrix proteins (ECMs) in the human PC cell lines FR4ds and OPM-1ds. The FR4ds cells expressed beta 1+, beta 3-, alpha 2-, alpha 3-, alpha 4+, alpha 5+, alpha 6+, and alpha v+ integrins, whereas the OPM-1ds cells expressed beta 1+, beta 3-, alpha 2-, alpha 3+, alpha 4+, alpha 5-, alpha 6+, and alpha v+. Fibronectin (FN) and laminin (LN) promoted the chemotaxis of the PCs. An inhibitory assay with anti-integrin monoclonal antibodies (MoAbs) showed that anti-alpha 4 MoAb partially inhibited the chemotaxis of FR4ds and completely inhibited the chemotaxis of OPM-1ds. Anti-alpha 5 MoAb alone had no effect on either of these two lines. Nevertheless, anti-alpha 5 MoAb completely inhibited chemotaxis when it was added with anti-alpha 4 in FR4ds, demonstrating a novel complementary role of VLA-5 toward VLA-4 in the chemotaxis induced by FN. LN facilitated chemotaxis both in OPM-1ds expressing alpha 3 and alpha 6 integrins and in FR4ds expressing alpha 6 integrin alone. Anti-alpha 6 MoAb completely inhibited FR4ds chemotaxis, whereas anti-alpha 3 and -alpha 6 MoAb had synergistic inhibitory effects on the chemotaxis of OPM-1ds. These results indicated that the distribution of PCs in human tissue are determined by at least two factors: the concentration of the ECM proteins FN and LN and the expression of integrins.
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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/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Fibronectins,
http://linkedlifedata.com/resource/pubmed/chemical/Laminin,
http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Oligopeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Fibronectin,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Laminin,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Very Late Antigen,
http://linkedlifedata.com/resource/pubmed/chemical/arginyl-glycyl-aspartic acid,
http://linkedlifedata.com/resource/pubmed/chemical/glycyl-arginyl-glycyl-aspartyl-seryl...
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0006-4971
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
86
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
719-25
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:7606001-Antibodies, Monoclonal,
pubmed-meshheading:7606001-Cell Adhesion,
pubmed-meshheading:7606001-Cell Size,
pubmed-meshheading:7606001-Chemotaxis,
pubmed-meshheading:7606001-Fibronectins,
pubmed-meshheading:7606001-Humans,
pubmed-meshheading:7606001-Laminin,
pubmed-meshheading:7606001-Neoplasm Proteins,
pubmed-meshheading:7606001-Neoplastic Stem Cells,
pubmed-meshheading:7606001-Oligopeptides,
pubmed-meshheading:7606001-Plasma Cells,
pubmed-meshheading:7606001-Plasmacytoma,
pubmed-meshheading:7606001-Receptors, Fibronectin,
pubmed-meshheading:7606001-Receptors, Laminin,
pubmed-meshheading:7606001-Receptors, Very Late Antigen,
pubmed-meshheading:7606001-Tumor Cells, Cultured
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pubmed:year |
1995
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pubmed:articleTitle |
Laminin and fibronectin promote the chemotaxis of human malignant plasma cell lines.
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pubmed:affiliation |
Department of Hematology and Oncology, Osaka University Medical School, Japan.
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pubmed:publicationType |
Journal Article
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