Yoshida T, Hanada H, Iwata Y, Pan Y, Sigekawa M
Department of Molecular Physiology, National Cardiovascular Center Research Institute, Osaka, Japan.
Biochem Biophys Res Commun. 1996 Aug 5;225(1):11-5. doi: 10.1006/bbrc.1996.1123.
Dystrophin and alpha- and gamma-sarcoglycans were newly expressed in BC3H1 cells during differentiation induced by serum withdrawal. These proteins formed a tight complex with other dystophin-associated proteins (DAPs), as detected by immunoprecipitation with anti-dystrophin antibody. Integrins beta 1 and beta 3, vinculin, and focal adhesion kinase were also detected in the same immunoprecipitate. In a cell adhesion assay, differentiated BC3H1 cells attached more efficiently to type I collagen-coated dishes than nondifferentiated cells and loss of alpha-sarcoglycan induced by antisense ODN in differentiated cells resulted in significant inhibition of cell adhesion. Thus dystrophin and DAPs, at least partly, form a complex with the focal adhesion proteins in differentiated BC3H1 cells and alpha-sarcoglycan seems to modulate the function of the focal adhesion complex in these cells.
在血清饥饿诱导的分化过程中,肌营养不良蛋白、α-和γ-肌聚糖在BC3H1细胞中重新表达。如用抗肌营养不良蛋白抗体进行免疫沉淀检测所示,这些蛋白质与其他肌营养不良蛋白相关蛋白(DAPs)形成紧密复合物。整合素β1和β3、纽蛋白和粘着斑激酶也在同一免疫沉淀产物中被检测到。在细胞粘附试验中,分化的BC3H1细胞比未分化细胞更有效地附着于I型胶原包被的培养皿,并且反义寡核苷酸在分化细胞中诱导的α-肌聚糖缺失导致细胞粘附受到显著抑制。因此,肌营养不良蛋白和DAPs至少部分地与分化的BC3H1细胞中的粘着斑蛋白形成复合物,并且α-肌聚糖似乎调节这些细胞中粘着斑复合物的功能。