Mygland A, Tysnes O B, Matre R, Aarli J A, Gilhus N E
Department of Neurology, Gade Institute, University of Bergen, Norway.
Autoimmunity. 1994;17(4):327-31. doi: 10.3109/08916939409010673.
Sera from myasthenia gravis (MG) patients with thymoma were examined in Western blot for the presence of antibodies to proteins in the sarcoplasmic reticulum (SR) of cardiac muscle. Fourteen of 30 MG thymoma sera had IgG antibodies to a protein with the same electrophoretic mobility as cardiac muscle ryanodine receptor (RyR). Anti-cardiac RyR antibodies were not detected in any of the 45 sera from MG patients without thymoma. The same 14 MG thymoma sera, but none of the others, bound to RyR from skeletal muscle as well. Neutralization experiments showed that the anti-RyR antibodies in MG patient cross-reacted with cardiac and skeletal muscle RyR. Since skeletal and cardiac muscle RyRs are antigenically different, our findings may indicate that autoantibodies to RyR in MG originate by sensitization to a peptide shared by cardiac and skeletal muscle RyR, rather than to the complete native RyR.
采用蛋白质印迹法检测了伴胸腺瘤的重症肌无力(MG)患者血清中针对心肌肌浆网(SR)蛋白的抗体。30份MG胸腺瘤患者血清中,有14份含有与心肌兰尼碱受体(RyR)电泳迁移率相同的蛋白的IgG抗体。45份无胸腺瘤的MG患者血清中均未检测到抗心肌RyR抗体。同样是这14份MG胸腺瘤患者血清,而非其他血清,也能与骨骼肌RyR结合。中和实验表明,MG患者体内的抗RyR抗体可与心肌和骨骼肌RyR发生交叉反应。由于骨骼肌和心肌RyR在抗原性上存在差异,我们的研究结果可能表明,MG患者体内针对RyR的自身抗体是通过对心肌和骨骼肌RyR共有的一种肽致敏产生的,而非对完整的天然RyR致敏。