rdf:type |
|
lifeskim:mentions |
umls-concept:C0023693,
umls-concept:C0205087,
umls-concept:C0337112,
umls-concept:C0597357,
umls-concept:C0868955,
umls-concept:C0871261,
umls-concept:C1512631,
umls-concept:C1524075,
umls-concept:C1704632,
umls-concept:C1706817,
umls-concept:C1749467,
umls-concept:C2911692
|
pubmed:issue |
2
|
pubmed:dateCreated |
2003-7-8
|
pubmed:abstractText |
Receptor editing is an important mechanism to modify the Ag specificity of newly developing B cells that are reactive with self-Ags. Previous studies have suggested that late immature B cells, bearing high levels of IgM on their cell surface, are unable to initiate receptor editing and instead are deleted by apoptosis. Using the hen egg lysozyme transgenic system, we show that IgM(high) late-immature B cells are fully capable of receptor editing to soluble self-Ag. This was demonstrated by the induction of new endogenous light chain locus rearrangements and by a single-cell flow cytometric assay using a recombination-activating gene 2-green fluorescence protein reporter transgene. These studies suggest that the developmental window available for immature B cells to edit their Ig receptors, at least in response to certain soluble Ags, extends through the IgM(high) late immature B cell stage.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
AIM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Autoantigens,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin D,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin Light Chains,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin M,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Muramidase,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Antigen, B-Cell,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Fc,
http://linkedlifedata.com/resource/pubmed/chemical/hen egg lysozyme,
http://linkedlifedata.com/resource/pubmed/chemical/immunoglobulin D receptor,
http://linkedlifedata.com/resource/pubmed/chemical/immunoglobulin M receptor
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jul
|
pubmed:issn |
0022-1767
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
15
|
pubmed:volume |
171
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
678-82
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:12847233-Animals,
pubmed-meshheading:12847233-Autoantigens,
pubmed-meshheading:12847233-B-Lymphocyte Subsets,
pubmed-meshheading:12847233-Bone Marrow Cells,
pubmed-meshheading:12847233-Cell Differentiation,
pubmed-meshheading:12847233-Cells, Cultured,
pubmed-meshheading:12847233-Immunoglobulin D,
pubmed-meshheading:12847233-Immunoglobulin Light Chains,
pubmed-meshheading:12847233-Immunoglobulin M,
pubmed-meshheading:12847233-Membrane Proteins,
pubmed-meshheading:12847233-Mice,
pubmed-meshheading:12847233-Mice, Transgenic,
pubmed-meshheading:12847233-Muramidase,
pubmed-meshheading:12847233-RNA Editing,
pubmed-meshheading:12847233-Receptors, Antigen, B-Cell,
pubmed-meshheading:12847233-Receptors, Fc,
pubmed-meshheading:12847233-Solubility
|
pubmed:year |
2003
|
pubmed:articleTitle |
Late immature B cells (IgMhighIgDneg) undergo a light chain receptor editing response to soluble self-antigen.
|
pubmed:affiliation |
Center for Immunology and Department of Medicine, University of Minnesota Medical School, Minneapolis, MN 55455, USA.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|