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Decrease in acetylcholine‐receptor content of human myotube cultures mediated by monoclonal antibodies to α, β and γ subunits
Author(s) -
Tzartos Socrates J.,
Starzinski-Powitz Anna
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80220-4
Subject(s) - internalization , acetylcholine receptor , monoclonal antibody , receptor , antibody , myasthenia gravis , acetylcholine , myogenesis , antigen , chemistry , microbiology and biotechnology , biology , biochemistry , myocyte , immunology , endocrinology
One of the two main causes of acetylcholine‐receptor loss in myasthenia gravis is antigenic modulation, i.e. accelerated internalization and degradation rate by antibody‐crosslinking. This phenomenon has been studied only in animal tissues. Therefore, we tested antigenic modulation of the acetylcholine receptor on human embryonic myotubes in culture. Several monoclonal antibodies to the α, β and γ subunits of the receptor reduced its concentration, in some cases down to one‐third of the control. Some of these antibodies only form complexes of one antibody with two receptor molecules; consequently such small complexes are sufficient to accelerate internalization of the human acetylcholine receptor. This technique might be proved valuable for clinical screening of sera from myasthenie patients.