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 gamma-1 LN chain. Neuritogenesis induced by LN or its gamma-1-derived peptide in primary cultures from rat or either wild type or PrP null mice hippocampal neurons, indicated that PrPc is the main cellular receptor for that particular LN domain. These results point out to the importance of the PrPc-LN interaction for the neuronal plasticity mechanism.
Graner
E
E
Ludwig Institute for Cancer Research, São Paulo Branch, Rua Prof. Antônio Prudente 109/4A, 01509-010, São Paulo, Brazil.
Mercadante
A F
AF
Zanata
S M
SM
Forlenza
O V
OV
Cabral
A L
AL
Veiga
S S
SS
Juliano
M A
MA
Roesler
R
R
Walz
R
R
Minetti
A
A
Izquierdo
I
I
Martins
V R
VR
Brentani
R R
RR
D000818:Animals; D002478:Cells, Cultured; D006624:Hippocampus / Q000166:cytology / Q000378:metabolism / Q000648:ultrastructure; D007797:Laminin / Q000378:metabolism*; D051379:Mice; D016501:Neurites / Q000502:physiology*; D009474:Neurons / Q000378:metabolism / Q000648:ultrastructure; D010446:Peptide Fragments / Q000378:metabolism; D018621:PrPC Proteins / Q000378:metabolism*; D018620:PrPSc Proteins / Q000235:genetics; D011485:Protein Binding; D051381:Rats; D014407:Tumor Cells, Cultured
D007797:Laminin; D010446:Peptide Fragments; D018621:PrPC Proteins; D018620:PrPSc Proteins