Generation and Characterization of Monoclonal Antibodies That Specifically Recognize p65/L-Plastin Isoform but Not T-Plastin Isoform

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  • TOYOOKA Kiminori
    International Medical Center of Japan
  • LIU Fenzhi
    Department of Immunology and Host Defenses, Ehime University School of Medicine
  • ISHII Motoshi
    Department of Immunology and Host Defenses, Ehime University School of Medicine
  • SAITO Shouichiro
    Department of Anatomy and Embryology, Ehime University School of Medicine
  • KIRIKAE Teruo
    International Medical Center of Japan
  • ASANO Yoshihiro
    Department of Immunology and Host Defenses, Ehime University School of Medicine
  • SHINOMIYA Hiroto
    Department of Immunology and Host Defenses, Ehime University School of Medicine

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The 65-kDa protein (p65) was previously identified as a phosphorylated protein in activated macrophages, and has turned out to be a member of a plastin protein family characterized by a series of Ca2+-, calmodulin-, and β-actin-binding domains. In mice, two isoforms, p65/L-plastin and T-plastin, have so far been identified; p65/L-plastin is expressed in hemopoietic cells and cancer cells, and T-plastin in solid tissue cells. We generated monoclonal antibodies to p65/L-plastin, examined the isoform-specificity by using recombinant (r) T-plastin, and found that the antibodies were specific for rp65/L-plastin, whereas immune sera to rp65/L-plastin showed cross-reactions to rT-plastin. One of the antibodies, p65-7B5, was demonstrated to react to native p65/L-plastin by Western blot, flow cytometric, and immunohistochemical analysis. Furthermore, p65-7B5 has made it possible to detect p65/L-plastin-expressing cells in tissues where T-plastin is abundantly expressed. These reagents and procedures should provide specific tools to investigate the role of p65/L-plastin in leukocytes.

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