Novel E-cadherin-mediated adhesion in peripheral nerve: Schwann cell architecture is stabilized by autotypic adherens junctions.
Novel E-cadherin-mediated adhesion in peripheral nerve: Schwann cell architecture is stabilized by autotypic adherens junctions.
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新型的E-钙粘蛋白介导的外周神经：Schwann细胞结构的粘附稳定在自动型粘附连接处。
DOI：
10.1083/jcb.129.1.189
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发表时间：
1995-04
影响因子：
7.8
通讯作者：
Colman, D R
中科院分区：
文献类型：
--
作者：
Fannon, A M;Sherman, D L;Ilyina-Gragerova, G;Brophy, P J;Friedrich, V L Jr;Colman, D R
以前的研究（布兰克，W. F.， M. B. Bunge， R. P. Bunge. 1974）。Brain Res. 67:503-518)显示雪旺细胞旁腺膜在无钙培养基中被破坏，这表明钙粘蛋白介导的机制可能维持了旁腺膜复合物的完整性。利用针对E-cadherin细胞外第五结构域的抗体，我们现在通过共聚焦激光和电子免疫显微镜显示E-cadherin是周围神经系统雪旺细胞的主要粘附糖蛋白。然而，在致密髓磷脂双层中没有发现e -钙粘蛋白。相反，它集中在偏执狂身上，在施密特-兰特曼的切口上，在内部和外部循环上。在这些位点上，e -钙粘蛋白与细胞质下的电子密度有关，这些电子密度在单个雪旺细胞的几个细胞质旋转中协调一致。F-Actin和β -catenin这两种参与细胞信号传导的蛋白也共同定位于E- cadherin阳性位点。这些复合物是由单个雪旺细胞合成的局限于质膜的自型粘附型连接；在两个雪旺细胞之间和雪旺细胞与轴突之间均未观察到e -钙粘蛋白。我们的研究结果表明，e -钙粘蛋白及其相关蛋白是雪旺细胞细胞质通道网络结构的重要组成部分，并表明该网络除了髓鞘形成所需的功能外还具有特殊功能。
Previous studies (Blank, W. F., M. B. Bunge, and R. P. Bunge. 1974. Brain Res. 67:503-518) showed that Schwann cell paranodal membranes were disrupted in calcium free medium suggesting that cadherin mediated mechanisms may operate to maintain the integrity of the paranodal membrane complex. Using antibodies against the fifth extracellular domain of E-cadherin, we now show by confocal laser and electron immunomicroscopy that E-cadherin is a major adhesive glycoprotein in peripheral nervous system Schwann cells. E-Cadherin is not found, however, in compact myelin bilayers. Rather, it is concentrated at the paranodes, in Schmidt-Lanterman incisures, and at the inner and outer loops. At these loci, E-cadherin is associated with subplasmalemmal electron densities that coordinate in register across several cytoplasmic turns of a single Schwann cell. F-Actin and beta-catenin, two proteins implicated in cellular signaling, also co-localize to E- cadherin positive sites. These complexes are autotypic adherens-type junctions that are confined to the plasma membrane synthesized by a single Schwann cell; E-cadherin was never observed between two Schwann cells, nor between Schwann cells and the axon. Our findings demonstrate that E-cadherin and its associated proteins are essential components in the architecture of the Schwann cell cytoplasmic channel network, and suggest that this network has specialized functions in addition to those required for myelinogenesis.