Gossrau R
Department of Molecular Anatomy and Cell Biology, University Clinic Benjamin Franklin, Free University of Berlin, Germany.
Acta Histochem. 1998 Nov;100(4):451-62. doi: 10.1016/S0065-1281(98)80042-1.
Previously, we and others have reported association of nitric oxide (NO)-generating nitric oxide synthase I (NOS I) with dystrophin in the subsarcolemmal cytoskeleton of striated muscle fibers. Since this structure shows a costameric organization the detailed distribution of NOS I and other molecules inside and outside the subsarcolemmal cytoskeleton was investigated. Using catalytic histochemistry and immunohistochemistry on rat skeletal muscle NOS I was colocalized in the costameres together with dystrophin, beta-dystroglycan, alpha-, beta- and gamma-sarcoglycan, beta 1-integrin, vinculin, paxillin and caveolin-3. Additionally, only NOS appeared in uncharacterized subsarcolemmal wave-like structures. These data show 1) a growing family of proteins assembled in the costameres including NOS I as described here for the first time, 2) expanded distribution patterns for NOS I, and 3) therefore, presumably uneven NO concentrations within the skeletal muscle fibers which may have implications for NO function.
此前，我们和其他人曾报道，生成一氧化氮（NO）的一氧化氮合酶I（NOS I）与横纹肌纤维肌膜下细胞骨架中的肌营养不良蛋白有关联。由于该结构呈现出一种肌小节附着结构组织，因此对肌膜下细胞骨架内外的NOS I和其他分子的详细分布进行了研究。利用大鼠骨骼肌的催化组织化学和免疫组织化学方法，发现NOS I与肌营养不良蛋白、β - 肌营养不良聚糖、α -、β - 和γ - 肌聚糖、β1整合素、纽蛋白、桩蛋白和小窝蛋白 - 3一起共定位于肌小节附着结构中。此外，只有NOS出现在未明确的肌膜下波浪状结构中。这些数据表明：1）首次在此处描述的一个在肌小节附着结构中组装的不断增加的蛋白质家族，包括NOS I；2）NOS I的分布模式扩大；3）因此，推测骨骼肌纤维内的NO浓度不均匀，这可能对NO的功能有影响。
