von Bernhardi R, Inestrosa N C
Department of Cell and Molecular Biology, Faculty of Biological Sciences and Medicine, Catholic University of Chile, Santiago.
Brain Res. 1990 Oct 8;529(1-2):91-5. doi: 10.1016/0006-8993(90)90814-r.
We are interested in the study of the interactions involved in the attachment of collagen-tailed acetylcholinesterase (AChE) to the synaptic basal lamina. The fact that AChE occupies less than 0.1% of the muscle basal lamina, suggests that there is a very high specificity in the interaction that defines its distribution. We have previously found that asymmetric AChE is bound to the neuromuscular junction via heparan sulfate proteoglycans. Sulfated glycosaminoglycans as heparan sulfate and heparin extracted the asymmetric AChE from the synaptic basal lamina. Here we show that dermatan sulfate as well as de-sulfated heparin, are also able to extract collagen-tailed AChE. Taking into account that the solubilization of the asymmetric AChE is concomitant with the liberation of a dermatan sulfate proteoglycan from the rat neuromuscular junction, the present results open the possibility that the collagen-tailed AChE is also anchored to dermatan sulfate proteoglycans at the synaptic basal lamina.
我们对参与胶原尾型乙酰胆碱酯酶（AChE）附着于突触基底膜的相互作用研究感兴趣。AChE在肌肉基底膜中所占比例不到0.1%，这一事实表明，在决定其分布的相互作用中存在非常高的特异性。我们之前发现，不对称AChE通过硫酸乙酰肝素蛋白聚糖与神经肌肉接头结合。硫酸化糖胺聚糖如硫酸乙酰肝素和肝素可从突触基底膜中提取不对称AChE。在此我们表明，硫酸皮肤素以及去硫酸化肝素也能够提取胶原尾型AChE。鉴于不对称AChE的溶解与大鼠神经肌肉接头处硫酸皮肤素蛋白聚糖的释放同时发生，目前的结果表明胶原尾型AChE也可能锚定在突触基底膜的硫酸皮肤素蛋白聚糖上。
