Ervasti J M, Campbell K P
Howard Hughes Medical Institute, University of Iowa College of Medicine, Iowa City 52242.
Cell. 1991 Sep 20;66(6):1121-31. doi: 10.1016/0092-8674(91)90035-w.
The stoichiometry, cellular location, glycosylation, and hydrophobic properties of the components in the dystrophin-glycoprotein complex were examined. The 156, 59, 50, 43, and 35 kd dystrophin-associated proteins each possess unique antigenic determinants, enrich quantitatively with dystrophin, and were localized to the skeletal muscle sarcolemma. The 156, 50, 43, and 35 kd dystrophin-associated proteins contained Asn-linked oligosaccharides. The 156 kd dystrophin-associated glycoprotein contained terminally sialylated Ser/Thr-linked oligosaccharides. Dystrophin, the 156 kd, and the 59 kd dystrophin-associated proteins were found to be peripheral membrane proteins, while the 50 kd, 43 kd, and 35 kd dystrophin-associated glycoproteins and the 25 kd dystrophin-associated protein were confirmed as integral membrane proteins. These results demonstrate that dystrophin and its 59 kd associated protein are cytoskeletal elements that are tightly linked to a 156 kd extracellular glycoprotein by way of a complex of transmembrane proteins.
对肌营养不良蛋白 - 糖蛋白复合物中各成分的化学计量、细胞定位、糖基化和疏水特性进行了研究。156、59、50、43和35kd的肌营养不良蛋白相关蛋白各自具有独特的抗原决定簇，与肌营养不良蛋白定量富集，并定位于骨骼肌肌膜。156、50、43和35kd的肌营养不良蛋白相关蛋白含有天冬酰胺连接的寡糖。156kd的肌营养不良蛋白相关糖蛋白含有末端唾液酸化的丝氨酸/苏氨酸连接的寡糖。发现肌营养不良蛋白、156kd和59kd的肌营养不良蛋白相关蛋白是外周膜蛋白，而50kd、43kd和35kd的肌营养不良蛋白相关糖蛋白以及25kd的肌营养不良蛋白相关蛋白被确认为整合膜蛋白。这些结果表明，肌营养不良蛋白及其59kd相关蛋白是细胞骨架成分，它们通过跨膜蛋白复合物与156kd的细胞外糖蛋白紧密相连。
