Cellular prion protein binds laminin and mediates neuritogenesis

Laminin (LN) plays a major role in neuronal differentiation, migration and survival. Here, we show that the cellular prion protein (PrPc) is a saturab le, specific, high-affinity receptor for LN. The PrPc-LN interaction is inv olved in the neuritogenesis induced by NGF plus LN in the PC-12 cell line a nd the binding site resides in a carboxy-terminal decapeptide from the gamm a-1 LN chain. Neuritogenesis induced by LN or its gamma-1-derived peptide i n primary cultures from rat or either wild type or PrP null mice hippocampa l neurons, indicated that PrPc is the main cellular receptor for that parti cular LN domain. These results point out to the importance of the PrPc-LN i nteraction for the neuronal plasticity mechanism. (C) 2000 Elsevier Science B.V. All rights reserved.