Evidence map›Paper›PMID 16192638›Full record

ArticleThe American journal of pathology2005

Bovine prion is endocytosed by human enterocytes via the 37 kDa/67 kDa laminin receptor.

Etienne Morel, Thibault Andrieu, Fabrice Casagrande, Sabine Gauczynski, Stefan Weiss, Jacques Grassi, Monique Rousset, Dominique Dormont, Jean Chambaz

Open access · greenAbstract read
In one paragraph

Article in The American journal of pathology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
4.2field-weighted citation impact, top 5% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

39 citing papers in PubMed, 106 citations in OpenAlex.

  1. Review
  2. Post-translational modifications in prion diseases.Frontiers in molecular neuroscience · 2024
    Review
  3. Emerging roles of the cellular prion protein (PrPCellular and molecular life sciences : CMLS · 2023
    Review
  4. Review
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. MEK1 transduces the prion protein N2 fragment antioxidant effects.Cellular and molecular life sciences : CMLS · 2015
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 5 institutions in 2 countries.

Etienne MorelUMR505 INSERM/UPMC, 15 rue de l'école de Médecine, 75006 Paris, France.
Thibault Andrieu
Fabrice Casagrande
Sabine Gauczynski
Stefan Weiss
Jacques Grassi
Monique Rousset
Dominique Dormont
Jean Chambaz
Sorbonne Université · FRCommissariat à l'Énergie Atomique et aux Énergies Alternatives · FRLudwig-Maximilians-Universität München · DECEA Paris-Saclay · FRCEA Paris-Saclay - Etablissement de Fontenay-aux-roses · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Some forms of transmissible spongiform encephalopathies result from oral infection. We have thus analyzed the early mechanisms that could account for an uptake of infectious prion particles by enterocytes, the major cell population of the intestinal epithelium. Human Caco-2/TC7 enterocytes cultured on microporous filters were incubated with different prion strains and contaminated brain homogenates in the apical compartment. Internalization of infectious particles was analyzed by Western blotting and immunofluorescence. We observed internalization by enterocytes of prion particles from bovine spongiform encephalopathy brain homogenates but not from mouse-adapted scrapie-strain brain homogenates or purified bovine spongiform encephalopathy scrapie-associated fibrils. Bovine prion particles were internalized via endocytosis within minutes of infection and were associated with subapical vesicular structures related to early endosomes. The endocytosis of the infectious bovine PrP(Sc) was reduced by preincubating the cells with an anti-LRP/LR blocking antibody, identifying the 37 kDa/67 kDa laminin receptor (LRP/LR), which is apically expressed in Caco-2/TC7 cells, as the receptor for the infectious prion protein. Altogether, our results underscore a potential role of enterocytes in the absorption of bovine prions during oral infection through specific LRP/LR-dependent endocytosis.

Indexed as

EndocytosisAnimalsAntibodies, MonoclonalBlotting, WesternCaco-2 CellsCattleElectric ImpedanceEncephalopathy, Bovine SpongiformEnterocytesFluorescent Antibody Technique, DirectHumansL-Lactate DehydrogenaseMembranes, ArtificialMicroscopy, ConfocalMolecular WeightPrionsAntibodies, MonoclonalL-Lactate DehydrogenaseMembranes, ArtificialPrionsPrPC ProteinsPrPSc ProteinsReceptors, Laminin

Identifiers

PMID16192638
PMCPMC1603663
OpenAlexW2090202861

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.