Karpati G, Charuk J, Carpenter S, Jablecki C, Holland P
Ann Neurol. 1986 Jul;20(1):38-49. doi: 10.1002/ana.410200108.
Four male patients from two families were first seen with impaired skeletal muscle relaxation that rapidly worsened during exercise. Muscle biopsies from 2 patients were examined by appropriate biochemical and microscopic immunocytochemical techniques. The adenosine triphosphate (ATP)-dependent Ca2+ transport rate was extremely low in a particulate membrane fraction of skeletal muscle, and there was also a marked reduction of the concentration of 100-kD phosphoprotein, corresponding to Ca2+-ATPase of sarcoplasmic reticulum, in muscle microsomes. The concentration of immunoreactive Ca2+-ATPase of sarcoplasmic reticulum was markedly reduced on immunoblots. Evaluation by microscopic immunocytochemical techniques, using one polyclonal and two monoclonal antibodies against sarcoplasmic reticulum Ca2+ transport protein, revealed that the severe reduction of immunoreactive Ca2+-ATPase was limited to the histochemical type 2 fibers. The deficiency of the Ca2+ transport protein in the sarcoplasmic reticulum of type 2 fibers, which may be the primary expression of a presumed gene defect, can explain the impaired muscle relaxation of the patients. This disease appears to be a clinically, electromyographically, and biochemically distinct metabolic myopathy.
来自两个家族的4名男性患者初诊时表现为骨骼肌松弛受损，且在运动过程中迅速恶化。对2名患者的肌肉活检标本采用适当的生化及显微镜免疫细胞化学技术进行检查。骨骼肌微粒体膜部分中依赖三磷酸腺苷（ATP）的Ca2+转运速率极低，并且在肌肉微粒体中，与肌浆网Ca2+-ATP酶相对应的100-kD磷蛋白浓度也显著降低。免疫印迹显示肌浆网免疫反应性Ca2+-ATP酶的浓度明显降低。使用一种抗肌浆网Ca2+转运蛋白的多克隆抗体和两种单克隆抗体，通过显微镜免疫细胞化学技术评估发现，免疫反应性Ca2+-ATP酶的严重降低仅限于组织化学2型纤维。2型纤维肌浆网中Ca2+转运蛋白的缺乏可能是推测的基因缺陷的主要表现，这可以解释患者肌肉松弛受损的原因。这种疾病似乎是一种在临床、肌电图和生化方面都有明显特征的代谢性肌病。
