Analysis of IgA binding to FcαR+ T cells and characterization of anti-FcαR antiserum

Autor: T F Meyer, T Taguchi, Wilhelm K. Aicher, Hiroshi Kiyono, M. L. McGHEE, J. Xu, Jerry R. McGhee, Kenneth W. Beagley
Rok vydání: 1990
Předmět:
Zdroj: Advances in Mucosal Immunology ISBN: 9789401073233
DOI: 10.1007/978-94-009-1848-1_46
Popis: Subpopulations of CD4 positive (CD4+) T cells from murine Peyer’s Patches (PP) express an Fc receptor for IgA (FcαR). A high frequency of FcαR+, CD8+ T cells were also found in spleens of mice bearing an IgA myeloma. We have established FcαR+ T cell lines to study the isotype specific regulatory role of this receptor in IgA responses. We have tested the expression of interleukins (IL) by FcαR+ T cells both at the level of mRNA and secreted proteins. These T cells secrete IL-5, a major cytokine for regulation of IgA responses. To better understand the precise regulatory role of FcαR+ T cells in IgA synthesis, we have analyzed the FcαR in more detail. Immunoprecipitation of membrane proteins from FcαR+ T cells with IgA resulted in a 38 kD protein as a major receptor component and antisera were raised against this 38 kD protein. The anti-FcαR antibodies blocked IgA binding to FcαR+ T cell hybridomas and to splenic CD8+ FcαR+ T cells of IgA myeloma-bearing mice, but did not interfere with the staining of CD3 and other surface markers. Furthermore, the anti-FcαR antibodies specifically stained FcαR+T cells. Thus, our results indicate that FcαR on T cell lines derived from PP is a 38 kD protein. Further, an antiserum has been produced which is either specific for this FcαR or else recognize determinants which are in close proximity to this receptor and should be useful for cloning the FcαR.
Databáze: OpenAIRE