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Rapid Communication| Volume 163, ISSUE 1, P44-46, February 01, 1999

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The 301 to 314 amino acid residue of β-tubulin is not a target epitope for serum IgM antibodies in chronic inflammatory demyelinating polyneuropathy

  • Yumi Tagawa
    Affiliations
    Department of Neurology, Dokkyo University School of Medicine, Kitakobayashi 880, Mibu, Shimotsuga, Tochigi 321-0293, Japan

    Third Department of Internal Medicine, Kagawa Medical University, Kagawa, Japan
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  • Nobuhiro Yuki
    Correspondence
    Corresponding author. Tel.: +81-282-861111, ext. 2578; fax: +81-282-865884
    Affiliations
    Department of Neurology, Dokkyo University School of Medicine, Kitakobayashi 880, Mibu, Shimotsuga, Tochigi 321-0293, Japan
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  • Koichi Hirata
    Affiliations
    Department of Neurology, Dokkyo University School of Medicine, Kitakobayashi 880, Mibu, Shimotsuga, Tochigi 321-0293, Japan
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      Abstract

      Connolly et al. [Neurology 48 (1997) 243] reported that IgM M-proteins from three patients selectively binds to an epitope on β-tubulin that consists of amino acids 301 to 314. We therefore investigated whether these 14 amino acid residues β301–314 are the target epitope for serum IgMs in sera from 67 patients with chronic inflammatory demyelinating polyneuropathy (CIDP), 50 with Guillain-Barré syndrome, 50 with motor neuron diseases, and 50 normal controls. IgM anti-β301–314 antibodies were not restricted to nor were selectively associated with CIDP. We conclude that β301–314 is not a target epitope for serum IgMs in CIDP.

      Keywords

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