Vybiral T, Deitiker P R, Roberts R, Epstein H F
Department of Neurology, Baylor College of Medicine, Houston, Tex. 77030.
Circ Res. 1992 Dec;71(6):1404-9. doi: 10.1161/01.res.71.6.1404.
The sarcomeric proteins and organization of cardiac myofibrils appeared intact in multiple unrelated patients with hypertrophic cardiomyopathy. In two subjects demonstrating the missense mutation at position 403 (Arg to Gln) in the beta-myosin heavy chain gene, total myosin and immunoreactive beta-myosin heavy chain levels were similar to those found in other patients with hypertrophic cardiomyopathy and various disease control subjects. No alteration in expression of the cardiac alpha-myosin heavy chain gene was observed. These results are consistent with the examined myosin heavy chain mutation, permitting proper accumulation and assembly of myosin while primarily impairing contractile function. The characteristic myocyte disarray would appear likely to be a secondary consequence of the mutations.
在多个不相关的肥厚型心肌病患者中，肌节蛋白和心肌肌原纤维的组织结构看起来完好无损。在两名显示β-肌球蛋白重链基因第403位（精氨酸突变为谷氨酰胺）错义突变的受试者中，总肌球蛋白和免疫反应性β-肌球蛋白重链水平与其他肥厚型心肌病患者及各种疾病对照受试者中的水平相似。未观察到心脏α-肌球蛋白重链基因表达的改变。这些结果与所检测的肌球蛋白重链突变一致，允许肌球蛋白正常积累和组装，同时主要损害收缩功能。特征性的心肌细胞排列紊乱似乎可能是这些突变的次要后果。
