PrP‐dependent cell adhesion in N2a neuroblastoma cells

FEBS Letters

Mangé, Alain³  Lehmann, Sylvain³  Umlauf, David³  Harris, David¹  Milhavet, Ollivier² 

[1] Department of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, MO 63110-1093, USA;National Institutes of Health, National Institute on Aging, Gerontology Research Center, Laboratory of Neurosciences, 5600 Nathan Shock Drive, Baltimore, MD 21224, USA;Institut de Génétique Humaine, CNRS U.P.R. 1142, 141, rue de la Cardonille, 34396 Montpellier Cedex 5, France

关键词: Aggregation;    Intercellular adhesion;    Prion protein;    PrP;    prion protein;    PrPC;    cellular isoform of PrP;    PrPSc;    scrapie isoform of PrP;    PIPLC;    phosphatidylinositol-specific phospholipase C;    LR;    laminin receptor;    LRP;    laminin receptor precursor;    N-CAM;    neural cell adhesion molecule;   

DOI  :  10.1016/S0014-5793(02)02338-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The cellular isoform of prion protein (PrP^C) 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 pre-incubation of cells with an antibody raised against the N-terminal part of PrP^C. Our paradigm allows the study of the function of PrP as an intercellular adhesion molecule and a cell surface ligand or receptor.

【 授权许可】

Unknown