Paggi Paola, De Stefano Maria Egle, Petrucci Tamara Corinna
Dipartimento di Biologia Cellulare e dello Sviluppo, Università La Sapienza, Piazzale A. Moro 5, 00185 Roma, Italy.
J Physiol Paris. 2006 Mar-May;99(2-3):119-24. doi: 10.1016/j.jphysparis.2005.12.004. Epub 2006 Jan 25.
We previously demonstrated the involvement of the dystrophin-dystroglycan (Dys-DG) complex in the stabilization of intraganglionic synapses in rodent superior cervical ganglion (SCG) by investigating changes in the organization of their post-synaptic apparatus induced either by ganglionic neuron axotomy or by the lack of Dys in genetically dystrophic mdx mice, or by the combination of the two. A role of the matrix metalloproteinases (MMPs) MMP-2 and MMP-9 in the degradation of DG and, hence, in disrupting the connection between the extracellular matrix (ECM) and the cortical cytoskeleton, has recently been proposed. We hypothesized that the degradation by MMPs of ECM proteins and DG in ganglionic neurons may be involved in injury-induced synaptic detachment observed in rodent SCG. In this review, we report changes in MMP-2 and in the proteins involved in one of the enzymatic cascades of activation induced by axotomy of rat SCG neurons. This will be preceded by a description of our previous observations that led to investigate the role of MMP-2 in this experimental model.
我们先前通过研究以下因素引起的突触后装置组织变化，证明了肌营养不良蛋白-肌营养不良聚糖（Dys-DG）复合物参与啮齿动物颈上神经节（SCG）内神经节突触的稳定：神经节神经元轴突切断术、基因性肌营养不良mdx小鼠中Dys的缺失或两者的组合。最近有人提出基质金属蛋白酶（MMP）MMP-2和MMP-9在DG降解中发挥作用，进而破坏细胞外基质（ECM）与皮质细胞骨架之间的连接。我们假设，MMP对神经节神经元中ECM蛋白和DG的降解可能与啮齿动物SCG中观察到的损伤诱导的突触脱离有关。在这篇综述中，我们报告了MMP-2以及大鼠SCG神经元轴突切断术诱导的激活酶级联反应中涉及的蛋白质的变化。在此之前，我们将描述先前的观察结果，这些观察结果促使我们研究MMP-2在该实验模型中的作用。
