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Predicate | Object |
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rdf:type | |
lifeskim:mentions |
umls-concept:C0003250,
umls-concept:C0004561,
umls-concept:C0020861,
umls-concept:C0037083,
umls-concept:C0037791,
umls-concept:C0086418,
umls-concept:C0441655,
umls-concept:C0591833,
umls-concept:C0936012,
umls-concept:C1514562,
umls-concept:C1710082,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
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pubmed:issue |
8
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pubmed:dateCreated |
1987-11-9
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pubmed:abstractText |
The domain binding specificity of 19 murine anti-human IgM monoclonal antibodies (MoAbs) that have shown considerable heterogeneity in the transduction of stimulatory and inhibitory signals to B lymphocytes was evaluated by competition radioimmunoassays. Through the use of: (i) enzymatic fragments of IgM which each encompass more than a single CH domain, i.e. Fc5 mu and F(ab')2 mu, (ii) isolated single domains, C mu 2, C mu 3, and C mu 4, and (iii) mu heavy chain disease proteins, nine anti-IgM MoAbs were found to have C mu 1 domain specificity, five to have C mu 2 specificity, and five others to have C mu 4 specificity. Ineffective binding to isolated mu chain demonstrated that C mu 1-specific MoAbs were directed to epitopes which require light chain for expression. The lack of binding of the C mu 4-specific MoAbs to CNBr cleavage fragments of Fc5 mu suggest that the determinants recognized by these MoAbs may also be conformational in nature. Cross-inhibition analyses were used to determine the number of unique epitopes recognized by the anti-IgM MoAbs. Results from these experiments showed that: (i) eight of the nine MoAbs specific for C mu 1 likely bind to a single epitope, or very proximate epitopes, (ii) the five C mu 2-specific MoAbs recognize at least three distinct epitopes, and (iii) the five C mu 4-specific MoAbs each recognize a separate determinant. A comparison of the known B cell activating properties of these MoAbs with their specificity for the various segments of the IgM molecule indicate that mitogenicity cannot be attributed to selective binding to any one domain.
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pubmed:grant | |
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, Anti-Idiotypic,
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin Light Chains,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin M
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0161-5890
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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 |
809-20
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:2443845-Animals,
pubmed-meshheading:2443845-Antibodies, Anti-Idiotypic,
pubmed-meshheading:2443845-Antibodies, Monoclonal,
pubmed-meshheading:2443845-Antibody Specificity,
pubmed-meshheading:2443845-B-Lymphocytes,
pubmed-meshheading:2443845-Binding, Competitive,
pubmed-meshheading:2443845-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:2443845-Epitopes,
pubmed-meshheading:2443845-Humans,
pubmed-meshheading:2443845-Immunoglobulin Fragments,
pubmed-meshheading:2443845-Immunoglobulin Light Chains,
pubmed-meshheading:2443845-Immunoglobulin M,
pubmed-meshheading:2443845-Mice
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pubmed:year |
1987
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pubmed:articleTitle |
Analysis of the domain specificity of various murine anti-human IgM monoclonal antibodies differing in human B lymphocyte signaling activity.
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pubmed:affiliation |
Hospital for Joint Diseases, Mount Sinai School of Medicine, City University of New York, NY 10029.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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