PrP-dependent cell adhesion in N2a neuroblastoma cells

被引：80

作者：

Mangé, A

Milhavet, O

Umlauf, D

Harris, D

Lehmann, S

机构：

[1] Inst Genet Humaine, CNRS UPR 1142, F-34396 Montpellier 05, France

[2] NIA, NIH, Gerontol Res Ctr, Neurosci Lab, Baltimore, MD 21224 USA

[3] Washington Univ, Sch Med, Dept Cell Biol & Physiol, St Louis, MO 63110 USA

来源：

FEBS LETTERS | 2002年 / 514卷 / 2-3期

关键词：

aggregation; intercellular adhesion; prion protein;

D O I：

10.1016/S0014-5793(02)02338-4

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The cellular isoform of prion protein (PrPC) is a ubiquitous glycoprotein expressed by most tissues and with a biological function yet to be determined. Here, we have used a neuroblastoma cell model to investigate the involvement of PrP in cell adhesion. Incubation of single cell suspension induced cell-cell adhesion and formation of cell aggregates. Interestingly, cells overexpressing PrP exhibit increased cation-independent aggregation. Aggregation was reduced after phosphatidylinositol-specific phospholipase C release of the protein and by preincubation of cells with an antibody raised against the N-terminal part of PrPC. Our paradigm allows the study of the function of PrP as an intercellular adhesion molecule and a cell surface ligand or receptor. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

引用

页码：159 / 162

页数：4

共 29 条

[1]

Aplin AE, 1998, PHARMACOL REV, V50, P197

[2] NCAM140 interacts with the focal adhesion kinase p125(fak) and the SRC-related tyrosine kinase p59(fyn) [J].