PrP^CControls via Protein Kinase A the Direction of Synaptic Plasticity in the Immature Hippocampus

Abstract

The cellular form of prion protein PrP C is highly expressed in the brain, where it can be converted into its abnormally folded isoform PrP Sc to cause neurodegenerative diseases. Its predominant synaptic localization suggests a crucial role in synaptic signaling. Interestingly, PrP C is developmentally regulated and its high expression in the immature brain could be instrumental in regulating neurogenesis and cell proliferation. Here, PrP C -deficient (Prnp 0/0 ) mice were used to assess whether the prion protein is involved in synaptic plasticity processes in the neonatal hippocampus. To this aim, calcium transients associated with giant depolarizing potentials, a hallmark of developmental networks, were transiently paired with mossy fiber activation in such a way that the two events were coincident. While this procedure caused long-term potentiation (LTP) in wild-type (WT) animals, it caused long-term depression (LTD) in

Role of the Fifth Copper Binding Site in Prion Conversion

“…A wealth of studies explored the functional aspects of this interaction, suggesting that PrP C may act as a copper transporter, a sink of copper excess or a scavenger for free radicals [13,14]. These findings are consistent with current evidence proposing a PrP C neuroprotective function [15][16][17].…”

CaMKII-dependent dendrite ramification and spine generation promote spatial training-induced memory improvement in a rat model of sporadic Alzheimer's disease

“…We also measured the level and the activity-dependent phosphorylation of CaMKII, cAMP-dependent protein kinase (PKA), and extracellular signal-related kinase 1/2 (ERK1/2), which are involved in dendrite remodeling (Hudmon and Schulman, 2002;Caiati et al, 2013;Silingardi et al, 2011). The results showed that the level of phosphorylated CaMKII at Thr286 (pCaMKII) was remarkably increased in hippocampus of T-hHcy rats, whereas the levels of total CaMKII, total ERK1/2 and pERK1/2, PKAa catalytic subunit (PKAa-cat), and PKA Ib regulatory subunit (PKA Ib-reg) were not changed by training (Fig.…”

Role of amyloid β protein receptors in mediating synaptic plasticity

“…Recent research demonstrates that PrP c is involved in synaptic plasticity processes in the neonatal hippocampus (33). In addition, PrP c has been proposed as an additional possible mediator of oligomer action.…”