EN
Matrix metalloproteinase-9 (MMP-9) is an extracelularly operating protein, capable to cleave several components of extracellular matrix (ECM). It is expressed in neurons in many brain structures. It has been shown to be important for maintenance of LTP in hipoocampal CA3 to CA1 pathway (Nagy et al. 2006) as well as in the prefrontal cortex (Okulski et al. 2007). Amygdaloid body is a small heteromeric structure, important for regulation of memory and autonomic as well as endocrine responses. In the present study, we have examined if LTP is MMP-9-dependent in the pathway from basolateral to central amygdala. The basolateral nucleus of amygdala (BLA) was theta burst-stimulated using a bipolar electrode, and EPSPs were collected from CE. We have found that in slices from MMP-9 knock out mice the late phase of LTP is abolished. The same effect was obtained when inhibitor of MMP-9 was used in rat amygdala slices where LTP lasted for only 30 min after its induction. Finally, we have checked LTP in slices from the transgenic rats with neuron-specifi c MMP-9 overexpression, driven by Synapsin I promoter. LTP in these rats was lower than in control but stable. The present observation suggests that the proper level of MMP-9 expresion and activity is essential for synaptic plasticity in the BLA-CE pathway, whereas MMP-9 overexpresion may cause destabilization of neuronal environment and decreased activity-dependent strengthening of synaptic transmission.