Cellular prion protein binds laminin and mediates neuritogenesis

被引：259

作者：

Graner, E

Mercadante, AF

Zanata, SM

Forlenza, OV

Cabral, ALB

Veiga, SS

Juliano, MA

Roesler, R

Walz, R

Minetti, A

Izquierdo, I

Martins, VR

Brentani, RR

机构：

[1] Ludwig Inst Canc Res, Sao Paulo Branch, BR-01509010 Sao Paulo, Brazil

[2] Univ Sao Paulo, Fac Med, Inst Psiquiatria, Lab Invest Med LIM 27, BR-09500900 Sao Paulo, Brazil

[3] Univ Fed Sao Paulo, INFAR, Sao Paulo, Brazil

[4] Univ Fed Rio Grande do Sul, Inst Ciencias Basicas Saude, Dept Bioquim, BR-90035003 Porto Alegre, RS, Brazil

[5] Ctr Tratamento, BR-01509010 Sao Paulo, Brazil

[6] Pesquisa Hosp Canc, BR-01509010 Sao Paulo, Brazil

来源：

MOLECULAR BRAIN RESEARCH | 2000年 / 76卷 / 01期

基金：

巴西圣保罗研究基金会;

关键词：

cellular prion protein; extracellular matrix; hippocampal neuron; laminin; neurite outgrowth; PC-12 cell line;

D O I：

10.1016/S0169-328X(99)00334-4

中图分类号：

Q189 [神经科学];

学科分类号：

071006 ;

摘要：

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.

引用

页码：85 / 92

页数：8

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