| Literature DB >> 18000956 |
Kaoru Kikuno1, Dong-Won Kang, Kazuki Tahara, Ikuko Torii, Homare M Kubagawa, Kang Jey Ho, Lucie Baudino, Naoto Nishizaki, Akira Shibuya, Hiromi Kubagawa.
Abstract
The Fc receptor for IgA and IgM (Fcalpha/muR) is of particular interest because it can bind antibodies of both IgM and IgA isotypes and thus may play a pivotal role in systemic and mucosal immunity. Using IgM and IgA ligands and newly generated Fcalpha/muR specific monoclonal antibodies we have defined biochemical features and cellular distribution of the human Fcalpha/muR. Both recombinant and native forms of human Fcalpha/muR are expressed on the cell surface as remarkably stable homodimeric transmembrane glycoproteins that can bind specifically polymeric IgM or IgA. The only human B cells to express Fcalpha/muR, albeit at very low levels, are found in the pre-germinal center subpopulation defined by the IgD+/CD38+ phenotype. Hence the expression pattern differs from that of the mouse wherein Fcalpha/muR is expressed by both circulating and resident B cell populations. Significantly, the predominant cell type expressing the Fcalpha/muR in humans is the follicular dendritic cell of germinal centers. The Fcalpha/muR may thus function in antigen presentation and B cell selection in the germinal center response.Entities:
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Year: 2007 PMID: 18000956 PMCID: PMC4160165 DOI: 10.1002/eji.200737655
Source DB: PubMed Journal: Eur J Immunol ISSN: 0014-2980 Impact factor: 5.532