Mizuno Yuji, Guyon Jeffrey R, Watkins Simon C, Mizushima Kazuyuki, Sasaoka Toshikuni, Imamura Michihiro, Kunkel Louis M, Okamoto Koichi
Department of Neurology, Gunma University Graduate School of Medicine, 3-39-22 Showa, Maebashi, Gunma 371-8511, Japan.
Muscle Nerve. 2004 Sep;30(3):337-46. doi: 10.1002/mus.20111.
Synemin is an intermediate filament protein shown previously to interact with alpha-dystrobrevin and desmin. Immunoblot analysis detects a beta-synemin protein of 170 kDa in human skeletal muscle and an alpha-synemin protein of 225 kDa in monkey brain. Low-resolution immunohistochemical analysis localizes beta-synemin within muscle along the sarcolemma, whereas confocal microscopic analysis further refines localization to the costamere and muscle Z-lines. In addition to these locations, beta-synemin is also enriched at the neuromuscular and myotendinous junctions, other regions that undergo high stress during myofiber contraction. Based on its localization and its expression pattern, it is proposed that beta-synemin functions as a structural protein involved in maintaining muscle integrity through its interactions with alpha-dystrobrevin, desmin, and other structural proteins.
联丝蛋白是一种中间丝蛋白，先前已证明它能与α - 肌营养不良蛋白和结蛋白相互作用。免疫印迹分析在人类骨骼肌中检测到一种170 kDa的β - 联丝蛋白，在猴脑中检测到一种225 kDa的α - 联丝蛋白。低分辨率免疫组织化学分析将β - 联丝蛋白定位在肌膜沿线的肌肉内，而共聚焦显微镜分析进一步将定位细化到肌小节和肌肉Z线。除了这些位置，β - 联丝蛋白在神经肌肉接头和肌肌腱连接处也有富集，这些区域在肌纤维收缩过程中承受高应力。基于其定位和表达模式，有人提出β - 联丝蛋白作为一种结构蛋白，通过与α - 肌营养不良蛋白、结蛋白和其他结构蛋白相互作用，参与维持肌肉完整性。
