A mouse T cell product that preferentially enhances IgA production. II. Physicochemical characterization.

  • M W Bond
    DNAX Research Institute of Molecular and Cellular Biology , Palo Alto, CA 94304
  • B Shrader
    DNAX Research Institute of Molecular and Cellular Biology , Palo Alto, CA 94304
  • T R Mosmann
    DNAX Research Institute of Molecular and Cellular Biology , Palo Alto, CA 94304
  • R L Coffman
    DNAX Research Institute of Molecular and Cellular Biology , Palo Alto, CA 94304

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<jats:title>Abstract</jats:title> <jats:p>Certain subsets of helper T cells, following stimulation with concanavalin A, secrete factors that specifically enhance the production of IgG1, IgE, and IgA by lipopolysaccharide-stimulated B cells. In the previous report, we describe a factor from the helper T cell line MB2-1 which enhances IgA production. IgA-enhancing factor has been purified from serum-free supernatants of this cell line. The purified lymphokine is a family of microheterogeneous polypeptides presumably modified post-translationally. IgA-enhancing factor has a native m.w. of 45,000 to 60,000 with subunits of between 24,000 and 28,000 under reducing conditions. Upon Edman degradation, a single amino-terminal sequence is detected which is identical to that of the lymphokine interleukin 5. IgA-enhancing factor activity is thus mediated by the same polypeptide that has been characterized as type II B cell growth factor, T cell-replacing factor, and eosinophil-differentiation factor.</jats:p>

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