ents of skeletal muscle from the patients with myasthenia gravisREN Huimin, ZHOU Zhigang, CHEN Xiangjun, et al.
nstitute of Neurology, Medical Center of Fudan University, Shanghai 200040, China
【Abstract】 Objective To explore whether the components of protein associated with muscle contraction appear decreased in the muscles of myasthenia gravis (MG).Methods The proteins were extracted from 10 normal cases and 17 cases of MG skeletal muscles with Gubstraub solution, and the components of the protein were analyzed by SDS-PAGE in common and micro me
thods in double blind. Composition of the differential protein band was observed by two-dimensional electrophoresis.Results SDS-PAGE patterns showed that the density of the protein band with a mass of about 25 kD in MG muscles was much lower than that in normal muscles. The value of density for 2
5 kD protein band in common analysis was 4.14±1.33 and 2.02±1.08 in the normal and MG muscles, respectively (P＜0.001), while in micro analysis the density of the protein band was 4.26±2.58 in normal and 1.34±0.79 in MG muscles, respectively (P＜0.001).The pattern of two-dimensional electrophoresis demonstrated that the differential 25 kD protein band was composed of more than two components appearing in the adjacent isoelectric point on the alkaline side of the gel, and they were proved to be not related to the components of myosin light chains. Conclusion It was suggested that pathogenically the development of MG should be associated with the involvement of 25 kD protein of the skeletal muscles. 【Key words】 Myasthenia gravis； Muscle, skeletal； Proteins
重症肌无力（MG）被认为是一种由乙酰胆碱受体（AChR）抗体引起神经肌肉接头突触膜AChR功能丧失的自身免疫疾病。但近年已发现，一系列的非AChR骨骼肌抗体［1］、Ryanodine 受体抗体及补体C9等均与MG的发病有关［2］。最近，我们不仅从肌肉组织中筛选到5个在正常人和MG患者肌肉中表达有明显不同的新的基因片段［3］，而且发现在以PBS提取的MG患者肌肉蛋白成分中，1个相对分子质量约25 000的蛋白的水平明显低于正常人肌肉。由于AChR 抗体阳性和阴性的MG患者临床表现相似，均为骨骼肌极易疲劳，并且已经知道Duchenne和强直性等肌营养不良的肌病患者骨骼肌肌球蛋白轻链组成发生了改变［4］，那么，是否MG患者肌肉极易疲劳的唯一原因为AC
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