Open AccessRelease of IgD-binding factor by T cells under the influence of interleukin 2, interleukin 4, or cross-linked IgD.
Author(s) -
Ashok R. Amin,
Richard Coico,
Fred D. Finkelman,
Gregory W. Siskind,
G. J. Thorbecke
Publication year - 1988
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.85.23.9179
Subject(s) - immunoglobulin d , lymphokine , microbiology and biotechnology , interleukin 4 , receptor , polyclonal antibodies , biology , recombinant dna , antigen , chemistry , antibody , biochemistry , immunology , b cell , cytokine , gene
Helper T cells with receptors specific for IgD have immunoaugmenting properties. We have now detected soluble IgD-binding factor in cell supernatants immobilized on nitrocellulose paper by their ability to bind 125I-labeled IgD. IgD-binding factor is released by normal splenic T cells stimulated with recombinant interleukin 2, recombinant interleukin 4, or crosslinked IgD in amounts paralleling the induction of IgD receptors on the cells. IgD receptors are constitutively produced by antigen-specific helper T-cell hybridomas 2H10 and A3.4C6. Incubation of these hybridoma cells with recombinant interleukin 2 increases release of IgD-binding factor while reducing expression of IgD receptors. Specificity of the binding factor for IgD is established by (i) competitive inhibition; (ii) the ability of the binding factor to bind radiolabeled IgD and not monoclonal IgE, IgG2a, or polyclonal IgG; and (iii) the removal of the binding factor on passage through an IgD-Sepharose column and recovery in a subsequent acid eluate.