Yamada H, Shimizu T, Tanaka T, Campbell K P, Matsumura K
Department of Neurology and Neuroscience, Teikyo University School of Medicine, Tokyo, Japan.
FEBS Lett. 1994 Sep 19;352(1):49-53. doi: 10.1016/0014-5793(94)00917-1.
alpha-Dystroglycan, a 156 kDa dystrophin-associated glycoprotein, binds laminin in skeletal muscle. Here we demonstrate that alpha-dystroglycan is a binding protein of laminin (A/B1/B2) and merosin (M/B1/B2) in peripheral nerve. Immunocytochemical analysis demonstrates the localization of alpha-dystroglycan and merosin surrounding myelin sheath of peripheral nerve fibers. Biochemical analysis demonstrates that the 120 kDa peripheral nerve alpha-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 of dy mice which have defects in myelination. The interaction between alpha-dystroglycan and merosin may play a role in the regulation of Schwann cell myelination and/or maintenance of myelin sheath.
α-肌营养不良蛋白聚糖是一种156 kDa的与肌营养不良蛋白相关的糖蛋白,在骨骼肌中与层粘连蛋白结合。在此我们证明,α-肌营养不良蛋白聚糖是外周神经中层粘连蛋白(A/B1/B2)和merosin(M/B1/B2)的结合蛋白。免疫细胞化学分析显示α-肌营养不良蛋白聚糖和merosin定位于外周神经纤维的髓鞘周围。生化分析表明,120 kDa的外周神经α-肌营养不良蛋白聚糖与merosin以及层粘连蛋白结合。层粘连蛋白和merosin的结合依赖于Ca2+,并受到NaCl和肝素的抑制。最近研究表明,dy小鼠的外周神经中merosin缺乏,这些小鼠存在髓鞘形成缺陷。α-肌营养不良蛋白聚糖与merosin之间的相互作用可能在雪旺细胞髓鞘形成的调节和/或髓鞘的维持中发挥作用。