A myasthenia gravis plasma immunoglobulin reduces miniature endplate potentials at human endplates in vitro

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Abstract
A particular myasthenia gravis (MG) plasma Ig has previously been shown to block a single α‐bungarotoxin (α‐BuTX) binding site on embryonic rat muscle acetylcholine receptor (AChR). We have investigated its effect on embryonic/denervated and adult human AChR both in extracts and in situ. Plasma Ig blocked 125I‐α‐BuTx binding by greater than 85% to the AChR extracted from denervated muscle, but only by 55% to AChR extracted from normal human muscle. Incubation of intact human muscle fibers with the plasma Ig reduced 125I‐α‐BuTx binding to the endplate AChRs by 63%, and substantially decreased the amplitude of miniature endplate potentials. We conclude that anti‐α‐BuTx site antibodies, when present, can be important in the pathophysiology of the disease.