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The 37-kDa/67-kDa laminin receptor acts as the cell-surface receptor for the cellular prion protein

Academic Article
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Overview

authors

  • Gauczynski, S.
  • Peyrin, J. M.
  • Haik, S.
  • Leucht, C.
  • Hundt, C.
  • Rieger, R.
  • Krasemann, S.
  • Deslys, J. P.
  • Dormont, D.
  • Lasmezas, Corinne
  • Weiss, S.

publication date

  • 2001

journal

  • EMBO Journal  Journal

abstract

  • 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 PrP(0/0) 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 degrees 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.

subject areas

  • Animals
  • Cell Line
  • Cell Membrane
  • Cricetinae
  • Flow Cytometry
  • Humans
  • Kidney
  • Mice
  • Mice, Knockout
  • Mutagenesis, Site-Directed
  • Neuroblastoma
  • Neurons
  • Oligopeptides
  • Peptides
  • Prion Diseases
  • Prions
  • Protein Binding
  • Protein Precursors
  • Protein Structure, Tertiary
  • Receptors, Laminin
  • Recombinant Fusion Proteins
  • Semliki forest virus
  • Transfection
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Research

keywords

  • 37-kDa laminin receptor precursor
  • 67-kDa high-affinity laminin receptor
  • PrP internalization
  • Semliki Forest virus
  • prion receptor
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Identity

PubMed Central ID

  • PMC125290

International Standard Serial Number (ISSN)

  • 0261-4189

Digital Object Identifier (DOI)

  • 10.1093/emboj/20.21.5863

PubMed ID

  • 11689427
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Additional Document Info

start page

  • 5863

end page

  • 5875

volume

  • 20

issue

  • 21

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