agin n端一半的神经元抑制区域。

J. Bixby, Kristine Baerwald-de la Torre, Cong Wang, F. Rathjen, M. Rüegg
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引用次数: 46

摘要

在神经肌肉连接的突触前和突触后分化中,agin是必需的。虽然agrin协调突触后分化的能力已被充分证明,但最近的实验表明,agrin也是突触前神经元的“停止信号”,并且agrin对中枢神经系统中的神经元有作用。为了阐明agrin的神经元活性并确定负责这些功能的受体,我们在体外研究了神经元的粘附及其对纯化agrin的神经突生长反应。研究发现,鸡纤毛神经节(CG)和前脑神经元与全长agrin和足以诱导突触后分化的agrin c -末端95 kDa (agrin c95)均具有黏附性。与之前的研究结果一致,我们的研究结果表明N-CAM与全长agrin结合,并表明α -异糖甘聚糖是agrin c95的神经元受体。在神经突生长实验中,全长agrin抑制层粘连蛋白和n-钙粘蛋白诱导的CG神经元神经突生长。agin的n端150 kDa片段抑制了神经突的生长,而不是agin c95,这表明agin n端部分的结构域足以实现这一功能。使用蛋白包被珠和表达agrin的细胞进行的粘附试验揭示了agrin与细胞粘附分子免疫球蛋白超家族成员的不同相互作用。然而,这些,包括N-CAM,似乎都不是神经元粘附的关键。总之,我们的研究结果表明,agin的n端一半参与了agin抑制神经突生长的能力。我们的研究结果进一步表明,α -三磷酸甘氨酸和N-CAM这两种已知的agrin结合蛋白都没有介导这种作用。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
A neuronal inhibitory domain in the N-terminal half of agrin.
Agrin is required for appropriate pre- and postsynaptic differentiation of neuromuscular junctions. While agrin's ability to orchestrate postsynaptic differentiation is well documented, more recent experiments have suggested that agrin is also a "stop signal" for the presynaptic neuron, and that agrin has actions on neurons in the CNS. To elucidate the neuronal activities of agrin and to define the receptor(s) responsible for these functions, we have examined adhesions of neurons and their neurite-outgrowth responses to purified agrin in vitro. We find that both full-length agrin and the C-terminal 95 kDa of agrin (agrin c95), which is sufficient to induce postsynaptic differentiation, are adhesive for chick ciliary ganglion (CG) and forebrain neurons. Consistent with previous findings, our results show that N-CAM binds to full-length agrin, and suggest that alpha-dystroglycan is a neuronal receptor for agrin c95. In neurite outgrowth assays, full-length agrin inhibited both laminin- and N-cadherin-induced neurite growth from CG neurons. The N-terminal 150 kDa fragment of agrin, but not agrin c95, inhibited neurite outgrowth, indicating that domains in the N-terminal portion of agrin are sufficient for this function. Adhesion assays using protein-coated beads and agrin-expressing cells revealed differential interactions of agrin with members of the immunoglobulin superfamily of cell adhesion molecules. However, none of these, including N-CAM, appeared to be critical for neuronal adhesion. In summary, our results suggest that the N-terminal half of agrin is involved in agrin's ability to inhibit neurite outgrowth. Our results further suggest that neither alpha-dystroglycan nor N-CAM, two known binding proteins for agrin, mediate this effect.
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