NR AEUR
AU Graner,E.; Mercadante,A.F.; Zanata,S.M.; Forlenza,O.V.; Cabral,A.L.B.; Veiga,S.S.; Juliano,M.A.; Roesler,R.; Walz,R.; Minetti,A.; Izquierdo,I.; Martins,V.R.; Brentani,R.R.
TI Cellular prion protein binds laminin and mediates neuritogenesis
QU Brain Research. Molecular Brain Research 2000 Mar 10; 76(1): 85-92
PT journal article
AB 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.
MH Animal; Cells, Cultured; Hippocampus/cytology/metabolism/ultrastructure; Laminin/*metabolism; Mice; Neurites/*physiology; Neurons/metabolism/ultrastructure; Peptide Fragments/metabolism; PrPc Proteins/*metabolism; PrPsc Proteins/genetics; Protein Binding; Rats; Support, Non-U.S. Gov't; Tumor Cells, Cultured
AD Ludwig Institute for Cancer Research, Sao Paulo Branch, Rua Prof. Antonio Prudente 109/4A, 01509-010, Sao Paulo, Brazil.
SP englisch
PO Niederlande