EN
Recent studies indicate that MMP-9 (gelatinase B that regulates pericellular environment through the cleavage of protein components of the extracellular matrix) plays a role in synaptic plasticity. Szklarc zyk et al. (2002), Konopacki et al. (2008) and Wilczynski et al. (2008) have demonstrated the presence of mRNA and protein for MMP-9 at postsynaptic sides of rat hippocampal neurons. It was also shown by Michaluk et al. (2007) that gelatinolytic activity of MMP9 increases after stimulation of rat neuronal cultures with either glutamate or bicuculine. We observed the presence of MMP-9 protein and mRNA in synaptoneurosomes, the synaptic fraction isolated from hippocampus. To detect the activity of MMP-9 we measured the cleavage of its substrate, β-dystroglycan. By the use of this readout we showed that MMP-9 is activated 5 to 10 mintes after neuronal stimulation. We postulate here that MMP-9 is translated from dendritically-localized mRNA and the protein is produced in response to synaptic stimulation. Its rapid and local translation and secretion is a polyadenylation- and local translation-dependent process.