Functional dissection of the cytoplasmic subregions of the interleukin‐5 receptor α chain in growth and immunoglobulin G1 switch recombination of B cells

• DOI: 10.1046/j.1365-2567.2001.01196.x
• Publication Date: 2003-03-12T02:28:06Z
• Authors: B.‐G. Moon; T. Yoshida; M. Shiiba; K. Nakao; M. Katsuki; S. Takaki; K. Takatsu
• Keywords: 0301 basic medicine; Cytoplasm; Molecular Sequence Data; B-Lymphocyte Subsets; Cell Culture Techniques; Cell Differentiation; Mice, Transgenic; Receptors, Interleukin; Receptors, Interleukin-5; Immunoglobulin Class Switching; 3. Good health; Mice, Inbred C57BL; Mice; Structure-Activity Relationship; 03 medical and health sciences; 0302 clinical medicine; Immunoglobulin M; Immunoglobulin G; Mutation; Animals; Amino Acid Sequence; Interleukin-5; Cell Division

Summary The interleukin‐5 receptor α chain (IL‐5Rα) is known to regulate the development and function of B cells eosinophils. Although functions IL‐5Rα cytoplasmic domain subregions have been studied extensively using cultured cell lines, this approach has limitations when studying distinct primary B‐cell subpopulations their responsiveness IL‐5. In present study, we generated mice on an null background, each expressing a mutant form transgene ligated µ enhancer VH promoter, either lacking DC3 region or substituting two proline residues for alanine (ApvA) in membrane‐proximal ppvp motif domain. motif, which mediates activation JAK2/STAT5 Btk, also contributes c‐fos , c‐jun c‐myc expression. showed impaired B‐1‐cell development, reduced serum immunoglobulin G3 (IgG3) IgM, no IL‐5‐induced enhancement proliferation switch recombination from gene γ1 gene; these were not recovered following expression ApvA mutant. contrast, absence affected while IgM production at levels similar those wild‐type transgene. results clearly indicated that played roles differentiation. Thus, offers new insights into IL‐5Rα, particular its carboxy‐terminal region.