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首页> 外文期刊>The European Journal of Neuroscience >Cbln1 binds to specific postsynaptic sites at parallel fiber-Purkinje cell synapses in the cerebellum.
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Cbln1 binds to specific postsynaptic sites at parallel fiber-Purkinje cell synapses in the cerebellum.

机译：Cbln1绑定到小脑中平行纤维-Purkinje细胞突触的特定突触后位点。

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摘要

Cbln1, which belongs to the C1q/tumor necrosis factor superfamily, is a unique molecule that is not only required for maintaining normal parallel fiber (PF)-Purkinje cell synapses, but is also capable of inducing new PF synapses in adult cerebellum. Although Cbln1 is reportedly released from granule cells, where and how Cbln1 binds in the cerebellum has remained largely unclear, partly because Cbln1 undergoes proteolysis to yield various fragments that are differentially detected by different antibodies. To circumvent this problem, we characterized the Cbln1-binding site using recombinant Cbln1. An immunohistochemical analysis revealed that recombinant Cbln1 preferentially bound to PF-Purkinje cell synapses in primary cultures and acute slice preparations in a saturable and replaceable manner. Specific binding was observed for intact Cbln1 that had formed a hexamer, but not for the N-terminal or C-terminal fragments of Cbln1 fused to other proteins. Similarly, mutant Cbln1 that had formed a trimer did not bind to the Purkinje cells. Immunoreactivity for the recombinant Cbln1 was observed in weaver cerebellum (which lacks granule cells) but was absent in pcd cerebellum (which lacks Purkinje cells), suggesting that the binding site was located on the postsynaptic sites of PF-Purkinje cell synapses. Finally, a subcellular fractionation analysis revealed that recombinant Cbln1 bound to the synaptosomal and postsynaptic density fractions. These results indicate that Cbln1, released from granule cells as hexamers, specifically binds to a putative receptor located at the postsynaptic sites of PF-Purkinje cell synapses, where it induces synaptogenesis.
机译：Cbln1，属于C1q /肿瘤坏死因子超家族，是一个独特的分子，不仅是维持正常平行纤维（PF）-Purkinje细胞突触所必需的，而且还能够在成年小脑中诱导新的PF突触。尽管据报道Cbln1是从颗粒细胞中释放出来的，但是在小脑中Cbln1的结合位置和结合方式尚不清楚，部分原因是Cbln1经历了蛋白水解作用，产生了各种片段，这些片段被不同的抗体差异检测。为了解决这个问题，我们使用重组Cbln1表征了Cbln1结合位点。免疫组织化学分析显示，重组Cbln1以可饱和和可替换的方式优先结合至原代培养物和急性切片制品中的PF-Purkinje细胞突触。观察到已形成六聚体的完整Cbln1的特异性结合，但未观察到与其他蛋白质融合的Cbln1的N端或C端片段。同样，已形成三聚体的突变体Cbln1不与Purkinje细胞结合。重组Cbln1的免疫反应性在韦弗小脑（缺乏颗粒细胞）中观察到，但在pcd小脑（缺乏普肯野细胞）中不存在，这表明结合位点位于PF-普肯果细胞突触的突触后位点。最后，亚细胞分级分析显示重组Cbln1绑定到突触和突触后密度分数。这些结果表明，以六聚体形式从颗粒细胞释放的Cbln1特异性结合位于PF-Purkinje细胞突触后突触位点的假定受体，在该处诱导突触形成。

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