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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
9
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pubmed:dateCreated |
1996-6-13
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pubmed:abstractText |
The effect of ligation of CD40 on the proliferation and Ig secretion of a battery of human Ig-secreting hybridomas was examined to determine the regulatory activity of this surface molecule on B cells after initial activation. B cell hybridomas were generated by fusing activated peripheral blood B cells with SPAZ-4, a non-Ig-secreting fusion partner, and were cloned before analysis. All hybridomas expressed CD40 comparably. These hybridomas were stimulated with either recombinant baculovirus-expressed membrane-bound CD40L or a soluble murine CD40L/CD8 construct in the presence or the absence of various cytokines. Concentrations of CD40L that saturated 40 to 100% of CD40 induced initial homotypic aggregation followed by Fas (CD95)-independent apoptosis, with resultant decreases in growth and Ig secretion. Concentrations of CD40L that saturated 15 to 25% of CD40 also stimulated aggregation of all hybridomas. However, proliferation and Ig secretion of 9 of 13 IgM-secreting hybridomas, but none of 14 IgG- or IgA-secreting hybridomas, were enhanced by these concentrations of CD40L. These responses were independent of interactions mediated by the adhesion pair CD1la/CD18-CD54. These results indicate that the impact of CD40 ligation on human Ig-secreting hybridomas varies with the extent of CD40 engagement and depending on whether the hybridoma derived from an activated B cell that had previously undergone switch recombination.
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pubmed:grant | |
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, CD40,
http://linkedlifedata.com/resource/pubmed/chemical/Biological Markers,
http://linkedlifedata.com/resource/pubmed/chemical/CD40 Ligand,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulins,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0022-1767
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
156
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3118-32
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:8617932-Adult,
pubmed-meshheading:8617932-Animals,
pubmed-meshheading:8617932-Antigens, CD40,
pubmed-meshheading:8617932-Apoptosis,
pubmed-meshheading:8617932-B-Lymphocytes,
pubmed-meshheading:8617932-Base Sequence,
pubmed-meshheading:8617932-Biological Markers,
pubmed-meshheading:8617932-CD40 Ligand,
pubmed-meshheading:8617932-Cell Aggregation,
pubmed-meshheading:8617932-Humans,
pubmed-meshheading:8617932-Hybridomas,
pubmed-meshheading:8617932-Immunoglobulins,
pubmed-meshheading:8617932-Ligands,
pubmed-meshheading:8617932-Lymphocyte Activation,
pubmed-meshheading:8617932-Membrane Glycoproteins,
pubmed-meshheading:8617932-Mice,
pubmed-meshheading:8617932-Molecular Sequence Data,
pubmed-meshheading:8617932-Protein Binding
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pubmed:year |
1996
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pubmed:articleTitle |
Ligation of CD40 influences the function of human Ig-secreting B cell hybridomas both positively and negatively.
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pubmed:affiliation |
Harold C. Simmons Arthritis Research Center, University of Texas Southwestern Medical Center, Dallas 75235, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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