Dystroglycan is a binding protein of laminin and merosin in peripheral nerve
Dystroglycan is a binding protein of laminin and merosin in peripheral nerve
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DOI：
10.1016/0014-5793(94)00917-1
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发表时间：
1994-09
期刊：
影响因子：
3.5
通讯作者：
H. Yamada;Teruo Shimizu;Takeshi Tanaka;K. Campbell;K. Matsumura
中科院分区：
文献类型：
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作者：
H. Yamada;Teruo Shimizu;Takeshi Tanaka;K. Campbell;K. Matsumura
α-肌营养不良聚糖是一种156 kDa的肌营养不良蛋白相关糖蛋白，与骨骼肌中的层粘连蛋白结合。本研究证明α-肌营养不良蛋白聚糖是周围神经中层粘连蛋白（A/B1/B2）和裂球蛋白（M/B1/B2）的结合蛋白。免疫细胞化学分析显示周围神经纤维髓鞘周围有α-肌营养不良蛋白聚糖和肌球蛋白。生化分析表明，120 kDa的外周神经α-肌营养不良蛋白聚糖结合merosin以及层粘连蛋白。层粘连蛋白和裂球蛋白的结合是Ca 2+依赖性的，并且被NACl和肝素抑制。最近，在有髓鞘形成缺陷的小鼠的外周神经中发现了merosin的缺陷。α-dystroglycan和merosin之间的相互作用可能在雪旺细胞髓鞘形成和/或髓鞘维持的调节中起作用。
α-Dystroglycan, a 156 kDa dystrophin-associated glycoprotein, binds laminin in skeletal muscle. Here we demonstrate that α-dystroglycan is a binding protein of laminin (A/B1/B2) and merosin (M/B1/B2) in peripheral nerve. Immunocytochemical analysis demonstrates the localization of α-dystroglycan and merosin surrounding myelin sheath of peripheral nerve fibers. Biochemical analysis demonstrates that the 120 kDa peripheral nerve α-dystroglycan binds merosin as well as laminin. The binding of laminin and merosin is Ca2+dependent and is inhibited by NACl and heparin. Recently, merosin was shown to be deficient in the peripheral nerve ofdymice which have defects in myelination. The interaction between α-dystroglycan and merosin may play a role in the regulation of Schwann cell myelination and/or maintenance of myelin sheath.