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首页> 外文期刊>Cell biology international. >In vitro developmental expression of dystroglycan and laminin-alpha2 in human skeletal muscle.
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In vitro developmental expression of dystroglycan and laminin-alpha2 in human skeletal muscle.

机译:dystroglycan和层粘连蛋白-α2在人体骨骼肌中的体外发育表达。

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摘要

The alpha-subunit of dystroglycan, a member of the dystrophin associated protein complex, binds to extracellular laminin-alpha2, while its beta-subunit interacts with cytoskeletal dystrophin. The exact biological role of dystroglycan, especially during human skeletal muscle development, has not been fully explored. Here, we analysed the distribution and expression characteristics of both dystroglycan subunits and laminin-alpha2 in primary human skeletal muscle cells. During development, expression levels of all three proteins increased with differentiation. The proteins were relocated from the sarcoplasm to the sarcolemma. The size of alpha-dystroglycan decreased from 150-220 kDa at the proliferation stage to 100-120 kDa at the late developmental stage. Both alpha- and beta-dystroglycan were involved in forming a complex with their respective partners laminin-alpha2 and dystrophin/utrophin. Our data show that, during development, cells may employ tightly regulated post-translational species-specific modification to produce different isoforms of alpha-dystroglycan to participate in appropriate functions.
机译:肌营养不良蛋白相关蛋白复合物成员dystroglycan的α亚基与细胞外层粘连蛋白α2结合,而其β亚基则与细胞骨架肌营养不良蛋白相互作用。 dystroglycan的确切生物学作用,特别是在人体骨骼肌发育过程中,尚未得到充分研究。在这里,我们分析了dystroglycan亚单位和层粘连蛋白-alpha2在原代人骨骼肌细胞中的分布和表达特征。在发育过程中,所有三种蛋白质的表达水平随着分化而增加。蛋白质从肌浆移至肌膜。 α-dystroglycan的大小从增殖阶段的150-220 kDa减少到发育后期的100-120 kDa。 α-和β-dystroglycan都参与与其各自的伴侣laminin-alpha2和dystrophin / utrophin形成复合物。我们的数据显示,在发育过程中,细胞可能会采用严格调节的翻译后物种特异性修饰,以产生不同的α-dystroglycan同种型,以发挥适当的功能。

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