Slater C R, Nicholson L V
Muscular Dystrophy Group Research Laboratories, Newcastle General Hospital, Newcastle upon Tyne, U.K.
J Neurol Sci. 1991 Feb;101(2):187-92. doi: 10.1016/0022-510x(91)90044-8.
It has been reported that immunofluorescent labelling of dystrophin in muscle from patients with Becker muscular dystrophy (BMD) is invariably patchy or discontinuous. This observation has led to the suggestion that BMD dystrophin molecules, which are usually smaller than normal due to the presence of "in frame" gene deletions, cannot be assembled into a complete lattice network under the plasma membrane and instead form isolated patches. Our experience with immunoperoxidase labelling of BMD muscle indicates that complete gaps in the reaction around fibres are uncommon. We have therefore compared immunofluorescence and immunoperoxidase labelling patterns on sets of serial sections from 6 BMD patients using a monoclonal antibody to dystrophin. No difference was detected between the two types of label used: the incidence of discontinuous labelling was rare in both cases. We suggest that significantly different patterns of dystrophin labelling may be obtained using different primary antibodies, and that caution needs to be exercised in extrapolating models of structure/function relationships from observations of antibody binding patterns.
据报道，贝克型肌营养不良症（BMD）患者肌肉中肌营养不良蛋白的免疫荧光标记总是呈斑块状或不连续。这一观察结果提示，由于存在“框内”基因缺失，BMD肌营养不良蛋白分子通常比正常分子小，无法在质膜下组装成完整的晶格网络，而是形成孤立的斑块。我们对BMD肌肉进行免疫过氧化物酶标记的经验表明，纤维周围反应完全缺失的情况并不常见。因此，我们使用抗肌营养不良蛋白单克隆抗体，比较了6例BMD患者连续切片上的免疫荧光和免疫过氧化物酶标记模式。未检测到两种标记类型之间的差异：两种情况下不连续标记的发生率都很低。我们认为，使用不同的一抗可能会获得明显不同的肌营养不良蛋白标记模式，并且在从抗体结合模式的观察结果推断结构/功能关系模型时需要谨慎。
