Grozdanovic Z, Gosztonyi G, Gossrau R
Department of Anatomy, Konigin-Luise-Strasse, Berlin, Germany.
Acta Histochem. 1996 Jan;98(1):61-9. doi: 10.1016/S0065-1281(96)80051-1.
Previously, we have demonstrated the expression of the brain-type nitric oxide synthase (NOS-I) in the sarcolemmal region of somatic and visceral striated muscle fibers in a variety of mammalian species through the use of enzyme histochemical and immunochemical techniques. Here we report that NOS-I protein and its NADPH diaphorase (NADPHd) activity are co-localized in the sarcolemma of human skeletal muscles. NOS-I immunolabeling and NADPHd activity showed no significant variation between type I and II fibers. In muscle biopsy specimens from patients with Duchenne muscular dystrophy (DMD), both NOS-I protein and activity were absent or markedly reduced. We, therefore, propose that NOS-I is complexed with dystrophin and/or dystrophin-associated proteins, adding a novel member to the sarcolemmal dystrophin-glycoprotein complex (DGC). The nature of the NOS-I-DGC link, and its role in skeletal muscle physiology and pathophysiology remain to be elucidated.
此前，我们通过酶组织化学和免疫化学技术，证实了在多种哺乳动物物种的躯体和内脏横纹肌纤维的肌膜区域中存在脑型一氧化氮合酶（NOS-I）的表达。在此我们报告，NOS-I蛋白及其NADPH黄递酶（NADPHd）活性共定位于人类骨骼肌的肌膜中。I型和II型纤维之间，NOS-I免疫标记和NADPHd活性无显著差异。在杜兴氏肌营养不良症（DMD）患者的肌肉活检标本中，NOS-I蛋白和活性均缺失或显著降低。因此，我们提出NOS-I与肌营养不良蛋白和/或肌营养不良蛋白相关蛋白复合，这为肌膜肌营养不良蛋白-糖蛋白复合体（DGC）增添了一个新成员。NOS-I-DGC联系的本质及其在骨骼肌生理和病理生理中的作用仍有待阐明。
