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PrP-dependent cell adhesion in N2a neuroblastoma cells
Alain Mangé1, Ollivier Milhavet, David Umlauf
1Institut de Génétique Humaine, CNRS U.P.R. 1142, 141 rue de la Cardonille, 34396 Montpellier Cedex 5, France.
FEBS Letters
|April 12, 2002
Summary
The cellular prion protein (PrP(C)) promotes cell-cell adhesion and aggregation in neuroblastoma cells. This suggests PrP(C) functions as an intercellular adhesion molecule, a role influenced by its N-terminal region.
Area of Science:
- Neuroscience
- Cell Biology
- Biochemistry
Background:
- The cellular prion protein (PrP(C)) is a glycoprotein found in most tissues.
- Its precise biological function remains largely undetermined.
- Investigating PrP(C) function in cell adhesion is crucial for understanding its role.
Purpose of the Study:
- To explore the involvement of PrP(C) in cell adhesion using a neuroblastoma cell model.
- To determine if PrP(C) acts as an intercellular adhesion molecule.
Main Methods:
- Neuroblastoma cells were used to study cell-cell adhesion and aggregation.
- Overexpression of PrP(C) was induced.
- The effect of phosphatidylinositol-specific phospholipase C and anti-PrP(C) antibodies was assessed.
Main Results:
- Single cell suspensions spontaneously formed aggregates.
- Cells overexpressing PrP(C) showed increased cation-independent aggregation.
- Aggregation was reduced by releasing PrP(C) from the cell surface and by N-terminal PrP(C) antibody treatment.
Conclusions:
- PrP(C) plays a significant role in mediating cell-cell adhesion and aggregation.
- PrP(C) functions as an intercellular adhesion molecule.
- The N-terminal region of PrP(C) is important for its adhesive properties.