The 37-kDa/67-kDa laminin receptor acts as the cell-surface receptor for the cellular prion protein
AUTOR(ES)
Gauczynski, Sabine
FONTE
Oxford University Press
RESUMO
Recently, we identified the 37-kDa laminin receptor precursor (LRP) as an interactor for the prion protein (PrP). Here, we show the presence of the 37-kDa LRP and its mature 67-kDa form termed high-affinity laminin receptor (LR) in plasma membrane fractions of N2a cells, whereas only the 37-kDa LRP was detected in baby hamster kidney (BHK) cells. PrP co-localizes with LRP/LR on the surface of N2a cells and Semliki Forest virus (SFV) RNA transfected BHK cells. Cell-binding assays reveal the LRP/LR-dependent binding of cellular PrP by neuronal and non-neuronal cells. Hyperexpression of LRP on the surface of BHK cells results in the binding of exogenous PrP. Cell binding is similar in PrP+/+ and PrP0/0 primary neurons, demonstrating that PrP does not act as a co-receptor of LRP/LR. LRP/LR-dependent internalization of PrP is blocked at 4°C. Secretion of an LRP mutant lacking the transmembrane domain (aa 86–101) from BHK cells abolishes PrP binding and internalization. Our results show that LRP/LR acts as the receptor for cellular PrP on the surface of mammalian cells.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=125290Documentos Relacionados
- Identification of interaction domains of the prion protein with its 37-kDa/67-kDa laminin receptor
- Laminin-induced retinoblastoma cell differentiation: possible involvement of a 100-kDa cell-surface laminin-binding protein.
- Cellular adherence elicits ligand-independent activation of the Met cell-surface receptor.
- Use of anti-idiotypic antibodies as cell-surface receptor probes
- Molecular weight and valence of the cell-surface receptor for immunoglobulin E.