PDGF-A激活的ERK信号介导的FAK-Paxillin相互作用在少突胶质祖细胞迁移中的作用。,Journal of Molecular Neuroscience

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PDGF-A激活的ERK信号介导的FAK-Paxillin相互作用在少突胶质祖细胞迁移中的作用。
Journal of Molecular Neuroscience ( IF 2.8 ) Pub Date : 2019-01-16 , DOI: 10.1007/s12031-019-1260-1
Juhi Singh ₁ , Kedarlal Sharma ₁ , Emma E Frost ₂ , Prakash P Pillai ₁

Affiliation

少突胶质祖细胞（OPC）起源于发育中的脑室下脑室。它们迁移并增殖以占据中枢神经系统的白质束，并转变为有髓的少突胶质细胞。沿其迁移途径，OPC受几种生长因子和趋化因子的引导和控制。PDGF-A（血小板衍生的生长因子）是一种生长因子，在该过程中充当单基因和有丝分裂线索，并激活细胞内的细胞内信号传导途径。细胞外信号调节激酶（ERK）信号的激活是PDGF-A诱导OPC迁移的机制之一。但是，PDGF-A诱导的ERK驱动的OPC迁移的机制仍不清楚。在目前的研究中我们进一步研究了PDGF-A诱导的ERK信号在OPC迁移中的作用。首先，我们使用药理抑制剂U0126或siRNA介导的ERK表达抑制，证实了PDGF-A激活的ERK信号在OPC迁移中的作用。然后，我们证明在用MEK抑制剂U0126处理的OPC中，PDGF-A诱导的肌动蛋白重组以及粘着斑激酶（FAK），帕西林和pERK信号的相互作用受到损害。因此，我们的发现证明PDGF-A通过调节肌动蛋白重组和FAK-Paxillin相互作用以ERK依赖性机制诱导OPC迁移。我们证明在用MEK抑制剂U0126处理的OPC中，PDGF-A诱导的肌动蛋白重组和粘着斑激酶（FAK），帕西林和pERK信号的相互作用受到损害。因此，我们的发现证明PDGF-A通过调节肌动蛋白重组和FAK-Paxillin相互作用以ERK依赖性机制诱导OPC迁移。我们证明了在用MEK抑制剂U0126处理的OPC中，PDGF-A诱导的肌动蛋白重组和粘着斑激酶（FAK），Paxillin和pERK信号的相互作用受到损害。因此，我们的发现证明PDGF-A通过调节肌动蛋白重组和FAK-Paxillin相互作用以ERK依赖性机制诱导OPC迁移。

"点击查看英文标题和摘要"

Role of PDGF-A-Activated ERK Signaling Mediated FAK-Paxillin Interaction in Oligodendrocyte Progenitor Cell Migration.

Oligodendrocyte progenitor cells (OPCs) originate from the sub-ventricular zone of the developing brain. They migrate and proliferate to occupy the white matter tracts of the central nervous system and transform into myelinating oligodendrocytes. Along their route of migration, OPCs are guided and controlled by several growth factors and chemokines. PDGF-A (platelet-derived growth factor), a growth factor, serves as a monogenic and mitogenic cue during the process and activates intracellular signaling pathways inside the cell. Activation of extracellular signal regulated kinase (ERK) signaling is one of the mechanisms by which PDGF-A induces the migration of OPCs. However, the mechanisms governing the PDGF-A-induced ERK-driven OPCs migration are still unclear. In the current study, we investigated further the role of PDGF-A-induced ERK signaling in OPC migration. First, we confirmed the role of PDGF-A-activated ERK signaling in OPC migration using the pharmacological inhibitor U0126, or siRNA-mediated suppression of ERK expression. Then, we demonstrated that PDGF-A-induced actin reorganization and interaction of focal adhesion kinase (FAK), Paxillin, and pERK signals are impaired in OPCs treated with the MEK inhibitor U0126. Thus, our findings demonstrated that PDGF-A induces OPC migration in an ERK-dependent mechanism via regulation of actin reorganization and FAK-Paxillin interaction.

更新日期：2019-01-16

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