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 saturable, specific, high-affinity receptor for
LN. The PrPc–LN interaction is involved in the neuritogenesis induced by NGF plus LN in
the PC-12 cell line and the binding site resides in a carboxy-terminal decapeptide from the γ-
1 LN chain. Neuritogenesis induced by LN or its γ-1-derived peptide in primary cultures from
rat or either wild type or PrP null mice hippocampal neurons, indicated that PrPc is the main …
show that the cellular prion protein (PrPc) is a saturable, specific, high-affinity receptor for
LN. The PrPc–LN interaction is involved in the neuritogenesis induced by NGF plus LN in
the PC-12 cell line and the binding site resides in a carboxy-terminal decapeptide from the γ-
1 LN chain. Neuritogenesis induced by LN or its γ-1-derived peptide in primary cultures from
rat or either wild type or PrP null mice hippocampal neurons, indicated that PrPc is the main …