NR AHTK
AU Mange,A.; Milhavet,O.; Umlauf,D.; Harris,D.; Lehmann,S.
TI PrP-dependent cell adhesion in N2a neuroblastoma cells
QU FEBS Letters 2002 Mar 13; 514(2-3): 159-62
PT journal article
AB 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 pre-incubation 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.
MH Animal; Antibodies/metabolism; Cations/metabolism; Cell Adhesion/drug effects/physiology; Cell Aggregation/drug effects/physiology; Immunoblotting; Mice; Neuroblastoma/*metabolism/pathology; Phospholipase C/metabolism; PrPc Proteins/genetics/*metabolism/pharmacology; Support, Non-U.S. Gov't; Transfection; Tumor Cells, Cultured
AD Institut de Genetique Humaine, CNRS U.P.R. 1142, 141 rue de la Cardonille, 34396 Montpellier Cedex 5, France.
SP englisch
PO Niederlande