EN
Matrix metalloproteinases have been implicated in physiological and pathological functions of neuronal networks. To get an insight into the specific role of protease MMP-9 in the plasticity of the mossy fiber-CA3 pathway (mf-CA3), we used field recordings to measure LTP in slices from wild type, MMP-9 KO and overexpressing (OVX) animals. Both lack of protease (KO) and its overexpression impaired the early and maintenance phase of mf-CA3 LTP (128% vs. 181% of respective baseline in KO and WT mice; and 136% vs. 189% in OVX and WT rats respectively, P<0.05). Importantly, impaired LTP in transgenic rodents could be rescued by administration of recombinant MMP-9 to the KO slices (152% of respective baseline). Moreover, autoactive MMP-9 protein application induced a stable autopotentiation of synaptic response in KO and WT mice. β-dystroglycan is a synaptic membrane protein and its MMP-mediated cleavage has been described during pathological, epileptic activity. In mf-CA3 pathway we observed a MMP-dependent significant decrease in 30 kDa β-dystroglycan digestion product as early as 5 minutes after LTP induction. Altogether, these results suggest that in mfCA3 pathway during first minutes after tetanus fine-tuned level of MMP-9 activity acts as a permissive factor for LTP establishment. Supported by Polish Ministry for Science and Higher Education grant N N401 541540.