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Cbln1 accumulates and colocalizes with Cbln3 and GluRδ2 at parallel fiber-Purkinje cell synapses in the mouse cerebellum

机译:Cbln1在小鼠小脑中的平行纤维-Purkinje细胞突触处积累并与Cbln3和GluRδ2共定位

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摘要

Cbln1 (a.k.a. precerebellin) is secreted from cerebellar granule cells as homohexamer or in heteromeric complexes with Cbln3. Cbln1 plays crucial roles in regulating morphological integrity of parallel fiber (PF)-Purkinje cell (PC) synapses and synaptic plasticity; Cbln1-knockout mice display severe cerebellar phenotypes that are essentially indistinguishable from those in glutamate receptor GluRδ2-null mice and include, severe reduction in the number of PF-PC synapses and loss of long-term depression of synaptic transmission. To understand better the relationship between Cbln1, Cbln3 and GluRδ2, we performed light and electron microscopic immunohistochemical analyses using highly specific antibodies and antigen-exposing methods, i.e., pepsin pretreatment for light microscopy and postembedding immunogold for electron microscopy. In conventional immunohistochemistry, Cbln1 was preferentially associated with non-terminal portions of PF axons in the molecular layer but rarely overlapped with Cbln3. In contrast, antigen-exposing methods not only greatly intensified Cbln1 immunoreactivity in the molecular layer, but also revealed its high accumulation in the synaptic cleft of PF-PC synapses. No such synaptic accumulation was evident at other PC synapses. Furthermore, Cbln1 now came to overlap almost completely with Cbln3 and GluRδ2 at PF-PC synapses. Therefore, the convergence of all three molecules provides the anatomical basis for a common signaling pathway regulating circuit development and synaptic plasticity in the cerebellum.
机译:Cbln1(又称小脑素)从小脑颗粒细胞中以同六聚体或与Cbln3的异源复合物形式分泌。 Cbln1在调节平行纤维(PF)-Purkinje细胞(PC)突触的形态完整性和突触可塑性中起着至关重要的作用。 Cbln1基因敲除小鼠表现出严重的小脑表型,基本上与谷氨酸受体GluRδ2无小鼠中的表型没有区别,包括严重减少PF-PC突触的数量和长期抑制突触传递。为了更好地了解Cbln1,Cbln3和GluRδ2之间的关系,我们使用高度特异性的抗体和抗原暴露方法进行了光和电子显微镜免疫组织化学分析,即胃蛋白酶预处理用于光学显微镜检查和包埋后免疫金用于电子显微镜检查。在常规的免疫组织化学中,Cbln1优先与分子层中PF轴突的非末端部分相关,但很少与Cbln3重叠。相比之下,抗原暴露方法不仅大大增强了分子层中的Cbln1免疫反应性,而且还揭示了其在PF-PC突触的突触间隙中的高积累。在其他PC突触中没有明显的这种突触积累。此外,Cbln1现在在PF-PC突触中几乎与Cbln3和GluRδ2完全重叠。因此,所有三个分子的会聚为共同的信号通路提供了解剖学基础,该信号通路可调节小脑的电路发育和突触可塑性。

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