Topic: chemical LTP

Learning and memory formation require activity-dependent rearrangements of neuronal networks driven by structural plasticity. The brain's perineuronal extracellular matrix (ECM), composed mainly of chondroitin sulfate proteoglycans from the lectican family, suppresses structural plasticity in the mature brain. Several members of this family, such as aggrecan and brevican, undergo proteolytic cleavage by proteases from the ADAMTS family, which may loosen the ECM structure. Therefore, we hypothesize that activity-dependent extracellular proteolysis weakens the ECM, supporting neuronal plasticity

The anti-N-methyl-D-aspartate receptor (NMDAR) encephalitis is an autoimmune disorder characterized by specific autoantibodies targeting the GluN1 subunit of postsynaptic NMDARs. Here, we investigated the effects of patient monoclonal anti-GluN1 antibodies on the synaptic signalling and plasticity molecules CaMKII and DAPK1 and their related pathways.We incubated primary hippocampal cell cultures (div 14-21) with patient-derived monoclonal anti-GluN1 or control antibodies. Thereafter, we induced chemical LTP and/or treated cells with the DAPK1 inhibitor TC-DAPK6. We then analysed NMDARs GluN1