Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
6276
|
| pubmed:dateCreated |
1990-7-12
|
| pubmed:abstractText |
It is well known that Fc receptors for IgG (FcRII) on macrophages mediate the endocytosis of antibody-antigen complexes and signal the release of inflammatory and cytotoxic agents. FcRII are also expressed at high levels on B cells where they are less involved in endocytosis than in modulating B-cell activation by membrane immunoglobulins. Although crosslinking of membrane immunoglobulins can result in B-cell differentiation and proliferation through stimulation of phospholipase C, mobilization of intracellular Ca2+, and activation of protein kinase C, crosslinking FcR with membrane immunoglobulins confers a dominant inhibitory signal that prevents or aborts activation. This form of regulation may have a role in the induction of tolerance by IgG and in controlling the B-cell repertoire by anti-idiotypes. The different functions of FcR on B cells and macrophages may reflect the fact that these cell types express closely related but distinct FcR isoforms. We have recently found that the main lymphocyte FcR isoform, FcRII-B1, is unable to mediate endocytosis by way of coated pits and coated vesicles owing to an in-frame insertion of 47 amino acids in its cytoplasmic tail. Here we show that this insert, absent from the FcRII-B2 macrophage isoform, also contains serine phosphorylation sites that may have a role in the ability of FcR to regulate B-cell activation through membrane immunoglobulins.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Alkaloids,
http://linkedlifedata.com/resource/pubmed/chemical/Cross-Linking Reagents,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Fc,
http://linkedlifedata.com/resource/pubmed/chemical/Staurosporine,
http://linkedlifedata.com/resource/pubmed/chemical/Tetradecanoylphorbol Acetate
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jun
|
| pubmed:issn |
0028-0836
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
14
|
| pubmed:volume |
345
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
628-32
|
| pubmed:dateRevised |
2007-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:2190097-Alkaloids,
pubmed-meshheading:2190097-Amino Acid Sequence,
pubmed-meshheading:2190097-Animals,
pubmed-meshheading:2190097-B-Lymphocytes,
pubmed-meshheading:2190097-Cell Line,
pubmed-meshheading:2190097-Cell Membrane,
pubmed-meshheading:2190097-Cricetinae,
pubmed-meshheading:2190097-Cross-Linking Reagents,
pubmed-meshheading:2190097-DNA,
pubmed-meshheading:2190097-Dogs,
pubmed-meshheading:2190097-Immunoglobulins,
pubmed-meshheading:2190097-Immunosorbent Techniques,
pubmed-meshheading:2190097-Lymphocyte Activation,
pubmed-meshheading:2190097-Molecular Sequence Data,
pubmed-meshheading:2190097-Phosphorylation,
pubmed-meshheading:2190097-Protein Kinase C,
pubmed-meshheading:2190097-Receptors, Fc,
pubmed-meshheading:2190097-Signal Transduction,
pubmed-meshheading:2190097-Staurosporine,
pubmed-meshheading:2190097-Tetradecanoylphorbol Acetate,
pubmed-meshheading:2190097-Transfection
|
| pubmed:year |
1990
|
| pubmed:articleTitle |
Fc receptor phosphorylation during receptor-mediated control of B-cell activation.
|
| pubmed:affiliation |
Department of Cell Biology, Yale University School of Medicine, New Haven, Connecticut 06510.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|