Cellular prion protein binds laminin and mediates neuritogenesis

Cellular prion protein binds laminin and mediates neuritogenesis

Author Graner, E. Google Scholar
Mercadante, A. F. Google Scholar
Zanata, S. M. Google Scholar
Forlenza, O. V. Google Scholar
Cabral, ALB Google Scholar
Veiga, S. S. Google Scholar
Juliano, M. A. Google Scholar
Roesler, R. Google Scholar
Walz, R. Google Scholar
Minetti, A. Google Scholar
Izquierdo, I Google Scholar
Martins, V. R. Google Scholar
Brentani, R. R. Google Scholar
Institution Ludwig Inst Canc Res
Universidade de São Paulo (USP)
Universidade Federal de São Paulo (UNIFESP)
Ctr Tratamento
Pesquisa Hosp Canc
Abstract 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. (C) 2000 Elsevier Science B.V. All rights reserved.
Keywords cellular prion protein
extracellular matrix
hippocampal neuron
neurite outgrowth
PC-12 cell line
Language English
Date 2000-03-10
Published in Molecular Brain Research. Amsterdam: Elsevier B.V., v. 76, n. 1, p. 85-92, 2000.
ISSN 0169-328X (Sherpa/Romeo, impact factor)
Publisher Elsevier B.V.
Extent 85-92
Origin http://dx.doi.org/10.1016/S0169-328X(99)00334-4
Access rights Closed access
Type Article
Web of Science ID WOS:000085921300010
URI http://repositorio.unifesp.br/handle/11600/26270

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