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Publication : Deletion of the α immunoglobulin chain membrane-anchoring region reduces but does not abolish IgA secretion.

First Author  Amin R Year  2012
Journal  Immunology Volume  136
Issue  1 Pages  54-63
PubMed ID  22250990 Mgi Jnum  J:184094
Mgi Id  MGI:5320248 Doi  10.1111/j.1365-2567.2012.03557.x
Citation  Amin R, et al. (2012) Deletion of the alpha immunoglobulin chain membrane-anchoring region reduces but does not abolish IgA secretion. Immunology 136(1):54-63
abstractText  Class switching and plasma cell differentiation occur at a high level within all mucosa-associated lymphoid tissues. The different classes of membrane immunoglobulin heavy chains are associated with the Igalpha/Igbeta heterodimer within the B-cell receptor (BCR). Whether BCR isotypes convey specific signals adapted to the corresponding differentiation stages remains debated but IgG and IgA membranes have been suggested to promote plasma cell differentiation. We investigated the impact of blocking expression of the IgA-class BCR through a 'alphaDeltatail' targeted mutation, deleting the Calpha immunoglobulin gene membrane exon. This allowed us to evaluate to what extent class switching and plasma cell differentiation can be concurrent processes, allowing some alphaDeltatail(+/+) B cells with an IgM BCR to directly differentiate into IgA plasma cells and yield serum secreted IgA in spite of the absence of membrane IgA(+) B lymphocytes. By contrast, in secretions the secretory IgA was very low, indicating that J-chain-positive plasma cells producing secretory IgA overwhelmingly differentiate from previously class-switched membrane IgA(+) memory B cells. In addition, although mucosa-associated lymphoid tissues are a major site for plasma cell accumulation, alphaDeltatail(+/+) mice showed that the gut B-cell lineage homeostasis is not polarized toward plasma cell differentiation through a specific influence of the membrane IgA BCR.
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