Aberrant glycosylation of α-dystroglycan causes defective binding of laminin in the muscle of chicken muscular dystrophy
Aberrant glycosylation of α-dystroglycan causes defective binding of laminin in the muscle of chicken muscular dystrophy
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DOI：
10.1016/j.febslet.2005.03.033
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发表时间：
2005-04-25
期刊：
影响因子：
3.5
通讯作者：
Matsumura, K
中科院分区：
文献类型：
--
作者：
Saito, F;Blank, M;Matsumura, K
肌营养不良聚糖是肌营养不良蛋白-糖蛋白复合物的核心成分，连接骨骼肌中的细胞外基质和细胞骨架。虽然营养不良鸡已被公认为人类肌营养不良症的动物模型，但导致肌肉变性的病理机制仍不清楚。我们在这里表明，α-肌营养不良蛋白聚糖（α-DG）的糖基化和层粘连蛋白结合活性是有缺陷的营养不良鸡。广泛的聚糖结构分析表明，Gal β 1-3GalNAc和GalNAc残基在营养不良鸡的α-DG中增加，而Sia α 2-3Gal结构减少。这些结果暗示在该肌营养不良症模型动物的肌变性的发病机制中α-DG的异常糖基化。(c)2005年欧洲生物化学学会联合会。Elsevier B. V.出版，保留所有权利。
Dystroglycan is a central component of dystrophin-glycoprotein complex that links extracellular matrix and cytoskeleton in skeletal muscle. Although dystrophic chicken is well established as an animal model of human muscular dystrophy, the pathomechanism leading to muscular degeneration remains unknown. We show here that glycosylation and laminin-binding activity of alpha-dystroglycan (alpha-DG) are defective in dystrophic chicken. Extensive glycan structural Analysis reveals that Gal beta 1-3GalNAc and GalNAc residues are increased while Sia alpha 2-3Gal structure is reduced in alpha-DG of dystrophic chicken. These results implicate aberrant glycosylation of alpha-DG in the pathogenesis of muscular degeneration in this model animal of muscular dystrophy. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.