Synaptic remodeling induced by axotomy of superior cervical ganglion neurons: Involvement of metalloproteinase-2

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 (E-CM) 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. (c) 2005 Elsevier Ltd. All rights reserved.