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Myasthenogenicity of a human acetylcholine receptor α‐subunit peptide: Morphology and immunology
Author(s) -
Matsuo Hidenori,
Tsujihata Mitsuhiro,
Satoh Akira,
Takeo Gou,
Yoshimura Toshiro,
Nagataki Shigenobu
Publication year - 1992
Publication title -
muscle and nerve
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.025
H-Index - 145
eISSN - 1097-4598
pISSN - 0148-639X
DOI - 10.1002/mus.880150305
Subject(s) - acetylcholine receptor , peptide , antibody , immune system , protein subunit , receptor , disulfide bond , immunization , acetylcholine , myasthenia gravis , chemistry , microbiology and biotechnology , immunology , biology , endocrinology , medicine , biochemistry , gene
Each of 10 rats inoculated with a synthetic peptide comprising residues 125–147 (without a disulfide bond) of human acetylcholine receptor (AChR) α‐subunit (Hα) had deposits of IgG and C3 (immune complexes) and showed morphological changes in the fine structure at the motor end‐plates 5 weeks after a single immunization. Antibody to the Hα peptides was elevated 1 week after immunization, but, antibody levels to solubilized human or rat AChR were very low in 8 of the 10 rats. These results suggest that the immune response to peptide Hα is the myasthenogenic site, which induces morphological change at the end‐plates.