Laminin-induced PC-12 cell differentiation is inhibited following laser inactivation of cellular prion protein.
Prions, the etiological agents for infectious degenerative encephalopathies, act by inducing structural modifications in the cellular prion protein (PrPc). Recently, we demonstrated that PrPc binds laminin (LN) and that this interaction is important for the neuritogenesis of cultured hippocampal neurons. Here we have used the PC-12 cell model to explore the biological role of LN-PrPc interaction. Antibodies against PrPc inhibit cell adhesion to LN-coated culture plaques. Furthermore, chromophore-assisted laser inactivation of cell surface PrPc perturbs LN-induced differentiation and promotes retraction of mature neurites. These results point out to the importance of PrPc as a cell surface ligand for LN.
Graner
E
E
Ludwig Institute for Cancer Research, São Paulo, Brazil.
Mercadante
A F
AF
Zanata
S M
SM
Martins
V R
VR
Jay
D G
DG
Brentani
R R
RR
D000818:Animals; D000906:Antibodies / Q000276:immunology; D002448:Cell Adhesion / Q000502:physiology / Q000528:radiation effects; D002454:Cell Differentiation / Q000502:physiology* / Q000528:radiation effects; D007797:Laminin / Q000502:physiology*; D007834:Lasers; D016716:PC12 Cells; D011328:Prions / Q000276:immunology / Q000502:physiology* / Q000528:radiation effects; D051381:Rats
D000906:Antibodies; D007797:Laminin; D011328:Prions