PrP-dependent cell adhesion in N2a neuroblastoma cells.
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.
Mangé
Alain
A
Institut de Génétique Humaine, CNRS U.P.R. 1142, 141 rue de la Cardonille, 34396 Montpellier Cedex 5, France.
Milhavet
Ollivier
O
Umlauf
David
D
Harris
David
D
Lehmann
Sylvain
S
D000818:Animals; D000906:Antibodies / Q000378:metabolism; D002412:Cations / Q000378:metabolism; D002448:Cell Adhesion / Q000187:drug effects / Q000502:physiology; D002449:Cell Aggregation / Q000187:drug effects / Q000502:physiology; D015151:Immunoblotting; D051379:Mice; D009447:Neuroblastoma / Q000378:metabolism* / Q000473:pathology; D043265:Phosphatidylinositol Diacylglycerol-Lyase; D054801:Phosphoinositide Phospholipase C; D018621:PrPC Proteins / Q000235:genetics / Q000378:metabolism* / Q000494:pharmacology; D014162:Transfection; D014407:Tumor Cells, Cultured; D010738:Type C Phospholipases / Q000378:metabolism
D000906:Antibodies; D002412:Cations; D018621:PrPC Proteins; D010738:Type C Phospholipases; D054801:Phosphoinositide Phospholipase C; D043265:Phosphatidylinositol Diacylglycerol-Lyase