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Predicate | Object |
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rdf:type | |
lifeskim:mentions |
umls-concept:C0001511,
umls-concept:C0003250,
umls-concept:C0018183,
umls-concept:C0024264,
umls-concept:C0032167,
umls-concept:C0035253,
umls-concept:C0064830,
umls-concept:C0205314,
umls-concept:C0332621,
umls-concept:C0679622,
umls-concept:C0814999,
umls-concept:C1444748,
umls-concept:C1879547,
umls-concept:C2755994
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pubmed:issue |
7
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pubmed:dateCreated |
1994-8-9
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pubmed:abstractText |
We have raised a monoclonal antibody (mAb), NG2B12, directed against rat CD18, capable of inducing lymphocyte homotypic adhesion and granulocyte adherence to plastic. NG2B12-induced aggregation is temperature sensitive and requires metabolic energy, an intact cytoskeleton and the presence of Mg2+, but is independent of protein synthesis. Ca2+ is not only dispensable but exerts a suppressive effect on the NG2B12-induced adhesion. The adhesion is readily observed in thymocytes and concanavalin A blasts of thymocytes and splenocytes but is very weak in resting spleen and lymph node cells. NG2B12 also enhances phorbol 12-myristate 13-acetate (PMA)-induced aggregation in an additive fashion. The NG2B12-induced homotypic adhesion is mediated by LFA-1. mAb against ICAM-1 completely inhibited the induced adhesion of activated cells but inhibited only partially and in a time-dependent manner the adhesion of resting thymocytes. The activation of protein phosphatases 1 and 2A (as assessed by the use of okadaic acid) is necessary for the NG2B12-induced adhesion of both resting and activated thymocytes. In contrast, H-7 (an inhibitor of protein kinase C and A), substantially suppressed the adhesion of resting thymocytes, whereas W-7 (an inhibitor of calmodulin-dependent protein kinase) inhibited the adhesion of activated thymocytes. NG2B12 induces both adherence to plastic and homotypic aggregation of granulocytes; the events being blocked by anti-CD18 (WT.3) and anti-CD11b/CD11c (OX-42) mAb, augmented by okadaic acid and not modified by H-7 and W-7. Additionally, we have demonstrated that NG2B12 and PMA employ distinct intracellular signaling pathways in inducing adhesion of both thymocytes and granulocytes.
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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, CD,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD18,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Adhesion Molecules,
http://linkedlifedata.com/resource/pubmed/chemical/Intercellular Adhesion Molecule-1,
http://linkedlifedata.com/resource/pubmed/chemical/Lymphocyte Function-Associated...
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0014-2980
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
24
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1640-8
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pubmed:dateRevised |
2003-11-14
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pubmed:meshHeading |
pubmed-meshheading:7913039-Animals,
pubmed-meshheading:7913039-Antibodies, Monoclonal,
pubmed-meshheading:7913039-Antigens, CD,
pubmed-meshheading:7913039-Antigens, CD18,
pubmed-meshheading:7913039-Cell Adhesion,
pubmed-meshheading:7913039-Cell Adhesion Molecules,
pubmed-meshheading:7913039-Cell Aggregation,
pubmed-meshheading:7913039-Cells, Cultured,
pubmed-meshheading:7913039-Colorimetry,
pubmed-meshheading:7913039-Female,
pubmed-meshheading:7913039-Granulocytes,
pubmed-meshheading:7913039-Intercellular Adhesion Molecule-1,
pubmed-meshheading:7913039-Leukocytes,
pubmed-meshheading:7913039-Lymphocyte Activation,
pubmed-meshheading:7913039-Lymphocyte Function-Associated Antigen-1,
pubmed-meshheading:7913039-Lymphocytes,
pubmed-meshheading:7913039-Rats,
pubmed-meshheading:7913039-Signal Transduction,
pubmed-meshheading:7913039-Thymus Gland
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pubmed:year |
1994
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pubmed:articleTitle |
A novel anti-rat CD18 monoclonal antibody triggers lymphocyte homotypic aggregation and granulocyte adhesion to plastic: different intracellular signaling pathways in resting versus activated thymocytes.
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pubmed:affiliation |
Institute of Medical Research, Military Medical Academy, Belgrade, Yugoslavia.
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pubmed:publicationType |
Journal Article
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