Decrease in acetylcholine‐receptor content of human myotube cultures mediated by monoclonal antibodies to α, β and γ subunits

FEBS Letters

Starzinski-Powitz, Anna²  Tzartos, Socrates J.¹ 

[1] Laboratory of Biochemistry, Hellenic Pasteur Institute, 127, Ave. Vas. Sofias, Athens 115 21, Greece;Institut für Genetik der Universität zu Köln, 5000 Köln 41, FRG

关键词: Acetylcholine receptor;    Antigenic modulation;    Monoclonal antibody;    (Human myotube) Antibody specificity;    Receptor internalization;    AChR;    nicotinic acetylcholine receptor;    MIR;    main immunogenic region;    mAb;    monoclonal antibody;    125I-toxin;    125I-labeled α-bungarotoxin;    fusion medium;    Dulbecco's modified Eagles medium plus 4% heat-inactivated normal human serum;   

DOI  :  10.1016/0014-5793(86)80220-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown