Reelin binds α3β1 integrin and inhibits neuronal migration
Reelin binds α3β1 integrin and inhibits neuronal migration
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DOI：
10.1016/s0896-6273(00)00007-6
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发表时间：
2000-07-01
期刊：
影响因子：
16.2
通讯作者：
Anton, ES
中科院分区：
文献类型：
--
作者：
Dulabon, L;Olson, EC;Anton, ES
瑞林（Reelin）或Dab1突变的小鼠，或者极低密度脂蛋白受体（VLDLR）和载脂蛋白E受体2（ApoER2）双突变的小鼠，都表现出大脑皮质分层紊乱。瑞林及其受体如何调节大脑皮质的层状组织尚不清楚。我们发现瑞林抑制皮质神经元的迁移，并使神经元从放射状胶质细胞上脱离。重组瑞林和天然瑞林都与α3β1整合素结合，α3β1整合素调节神经元 - 胶质细胞相互作用，并且是实现正常层状组织所必需的。瑞林在体外和体内对皮质神经元迁移的影响取决于瑞林与α3β1整合素之间的相互作用。α3β1的缺失会导致Dab1减少，Dab1是一种在瑞林下游起作用的信号蛋白。因此，瑞林可能通过结合α3β1整合素并调节整合素介导的细胞黏附来阻止神经元迁移并促进正常的皮质分层。
Mice that are mutant for Reelin or Dab1, or doubly mutant for the VLDL receptor (VLDLR) and ApoE receptor 2 (ApoER2), show disorders of cerebral cortical lamination. How Reelin and its receptors regulate laminar organization of cerebral cortex is unknown. We show that Reelin inhibits migration of cortical neurons and enables detachment of neurons from radial glia. Recombinant and native Reelin associate with alpha 3 beta 1 integrin, which regulates neuron-glia interactions and is required to achieve proper laminar organization. The effect of Reelin on cortical neuronal migration in vitro and in vivo depends on interactions between Reelin and alpha 3 alpha 1 integrin. Absence of alpha 3 beta 1 leads to a reduction of Dab1, a signaling protein acting downstream of Reelin. Thus, Reelin may arrest neuronal migration and promote normal cortical lamination by binding alpha 3 beta 1 integrin and modulating integrin-mediated cellular adhesion.