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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1984-7-18
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pubmed:abstractText |
One of seven monoclonal antibodies generated against mouse macrophages (M phi) was found to recognize isolated heterologous C1q. This antibody was shown to be cytotoxic and to react in a strain-independent way with mouse M phi derived from bone marrow cells as well as with M phi from the peritoneal cavity; it did not react, however, with mouse granulocytes, thymocytes, or T and B lymphocytes. The hemolytic activity of fluid phase C1q was inhibited to 50% at a 2 X 10(-4) dilution of hybridoma supernatant, whereas a 100-fold higher concentration was required to inhibit C1q bound to immune complexes ( EAC1q ) to the same extent. It was demonstrated that this antibody recognizes the isolated globular, Fc-binding portions of the C1q molecule and reacts with the A and B chains. Because M phi have been shown to synthesize C1q, the Fc-recognizing subcomponent of the first component of complement, evidence was provided that endogeneous C1q can serve as an Fc receptor on M phi during secretion. This fact was demonstrated by a dose-dependent inhibition of Fc-receptor activity for EIgG by the F(ab')2 fragment of this monoclonal antibody. These experiments further support the concept that C1q produced by M phi functions on the surface as an Fc-recognizing molecule before it is released and incorporated into the macromolecular complex of serum C1.
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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/Antigen-Antibody Complex,
http://linkedlifedata.com/resource/pubmed/chemical/Complement Activating Enzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Complement C1,
http://linkedlifedata.com/resource/pubmed/chemical/Complement C1q,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Fc
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0022-1767
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
133
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
400-4
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:6609989-Animals,
pubmed-meshheading:6609989-Antibodies, Monoclonal,
pubmed-meshheading:6609989-Antibody Specificity,
pubmed-meshheading:6609989-Antigen-Antibody Complex,
pubmed-meshheading:6609989-Antigen-Antibody Reactions,
pubmed-meshheading:6609989-Binding, Competitive,
pubmed-meshheading:6609989-Complement Activating Enzymes,
pubmed-meshheading:6609989-Complement Activation,
pubmed-meshheading:6609989-Complement C1,
pubmed-meshheading:6609989-Complement C1q,
pubmed-meshheading:6609989-Macrophages,
pubmed-meshheading:6609989-Mice,
pubmed-meshheading:6609989-Mice, Inbred C3H,
pubmed-meshheading:6609989-Rats,
pubmed-meshheading:6609989-Rats, Inbred WF,
pubmed-meshheading:6609989-Receptors, Fc
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pubmed:year |
1984
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pubmed:articleTitle |
Monoclonal anti-mouse macrophage antibodies recognize the globular portions of C1q, a subcomponent of the first component of complement.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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