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- W2007504230 abstract "Abstract Cellular prion protein (PrP c ) has a pivotal role in prion diseases. PrP c is a specific receptor for laminin (LN) γ1 peptide and several lines of evidence indicate that it is also involved in neural plasticity. Here we investigated whether the interaction between PrP c and LN plays a role in rat memory formation. We found that post‐training intrahippocampal infusion of PrP c ‐derived peptides that contain the LN binding site ( and ) or of anti‐PrP c or anti‐LN antibodies that inhibit PrP c –LN interaction impaired inhibitory avoidance memory retention. The amnesic effect of anti‐PrP c antibodies and peptide was reversed by co‐infusion of a LN γ1 chain‐derived peptide containing the PrP c ‐binding site, suggesting that PrP c –LN interaction is indeed crucial for memory consolidation. In addition, peptide and anti‐PrP c or anti‐LN antibodies also inhibited the activation of hippocampal cAMP‐dependent protein kinase A (PKA) and extracellular regulated kinase (ERK1/2), two kinases that mediate the up‐regulation of signaling pathways needed for consolidation of inhibitory avoidance memory. Our findings show that, through its interaction with LN, hippocampal PrP c plays a critical role in memory processing and suggest that this role is mediated by activation of both PKA and ERK1/2 signaling pathways." @default.
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- W2007504230 date "2006-12-01" @default.
- W2007504230 modified "2023-10-18" @default.
- W2007504230 title "The interaction between prion protein and laminin modulates memory consolidation" @default.
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- W2007504230 doi "https://doi.org/10.1111/j.1460-9568.2006.05156.x" @default.
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