ArticleThe EMBO journal2001
The 37-kDa/67-kDa laminin receptor acts as the cell-surface receptor for the cellular prion protein.
Article in The EMBO journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 136 papers.
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136 citing papers in PubMed, 425 citations in OpenAlex.
- Presymptomatic pharmacological inhibition of mGluR5 improves survival in a mouse model of prion diseases.Acta neuropathologica communications · 2026Article
- PrPInternational journal of molecular sciences · 2026Article
- Article
- Exploring immunotherapeutic strategies for neurodegenerative diseases: a focus on Huntington's disease and Prion diseases.Acta pharmacologica Sinica · 2025Review
- Expression of the RPSA-Containing and 67EBP Laminin Receptors in Relation to the Debatable Nature of the 67 kDa Laminin Receptor 67LR in Colorectal Cancer.International journal of molecular sciences · 2025Article
- Reconsideration of the laminin receptor 67LR in colorectal cancer cells.Biomolecules & biomedicine · 2024Article
- The dual role of ribosomal protein SA in pathogen infection: the key role of structure and localization.Molecular biology reports · 2024Review
- PLGA nanocapsules as a delivery system for a recombinant LRP-based therapeutic.FEBS open bio · 2024Article
- The structural line between prion and "prion-like": Insights from prion protein and tau.Current opinion in neurobiology · 2024Review
- Host cell factors involved in classical swine fever virus entry.Veterinary research · 2023Review
- Emerging roles of the cellular prion protein (PrPCellular and molecular life sciences : CMLS · 2023Review
- Anchorless risk or released benefit? An updated view on the ADAM10-mediated shedding of the prion protein.Cell and tissue research · 2023Review
- Cell biology of prion strains in vivo and in vitro.Cell and tissue research · 2023Review
- Vitamin E functions by association with a novel binding site on the 67 kDa laminin receptor activating diacylglycerol kinase.The Journal of nutritional biochemistry · 2022Article
- The Role of Diacylglycerol Kinase in the Amelioration of Diabetic Nephropathy.Molecules (Basel, Switzerland) · 2022Review
- 67-kDa Laminin Receptor-Mediated Cellular Sensing System of Green Tea Polyphenol EGCG and Functional Food Pairing.Molecules (Basel, Switzerland) · 2022Review
- Glycosaminoglycan binding by arboviruses: a cautionary tale.The Journal of general virology · 2022Review
- Knock-down of LRP/LR influences signalling pathways in late-stage colorectal carcinoma cells.BMC cancer · 2021Article
- The Role of Cellular Prion Protein in Promoting Stemness and Differentiation in Cancer.Cancers · 2021Review
- Bacterial genome-wide association study of hyper-virulent pneumococcal serotype 1 identifies genetic variation associated with neurotropism.Communications biology · 2020Article
76 more citing papers are in PubMed but not listed here.
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Authors and funding
11 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
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.
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