Evidence map›Paper›PMID 21763679›Full record

ArticleThe American journal of pathology2011

Orally administered prion protein is incorporated by m cells and spreads into lymphoid tissues with macrophages in prion protein knockout mice.

Ikuro Takakura, Kohtaro Miyazawa, Takashi Kanaya, Wataru Itani, Kouichi Watanabe, Shyuichi Ohwada, Hitoshi Watanabe, Tetsuya Hondo, Michael T Rose, Tsuyoshi Mori and 5 more

Open access · bronzeAbstract read
In one paragraph

Article in The American journal of pathology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

26 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Cellular and Molecular Mechanisms of Prion Disease.Annual review of pathology · 2019
    Review
  8. Article
  9. Article
  10. Cellular mechanisms responsible for cell-to-cell spreading of prions.Cellular and molecular life sciences : CMLS · 2018
    Review
  11. Review
  12. How do PrPPathogens (Basel, Switzerland) · 2017
    Review
  13. Article
  14. Sialylation Controls Prion FateThe Journal of biological chemistry · 2017
    Article
  15. Review
  16. Article
  17. Article
  18. Review
  19. Post-conversion sialylation of prions in lymphoid tissues.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  20. Article
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

15 authors at 4 institutions in 2 countries.

Ikuro TakakuraCellular Biology Laboratory, Graduate School of Agricultural Science, Tohoku University, Sendai, Japan.
Kohtaro Miyazawa
Takashi Kanaya
Wataru Itani
Kouichi Watanabe
Shyuichi Ohwada
Hitoshi Watanabe
Tetsuya Hondo
Michael T Rose
Tsuyoshi Mori
Suehiro Sakaguchi
Noriyuki Nishida
Shigeru Katamine
Takahiro Yamaguchi
Hisashi Aso
Tohoku University · JPNagasaki University · JPTokushima University · JPAberystwyth University · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Transmissible spongiform encephalopathies are fatal neurodegenerative diseases. Infection by the oral route is assumed to be important, although its pathogenesis is not understood. Using prion protein (PrP) knockout mice, we investigated the sequence of events during the invasion of orally administered PrPs through the intestinal mucosa and the spread into lymphoid tissues and the peripheral nervous system. Orally administered PrPs were incorporated by intestinal epitheliocytes in the follicle-associated epithelium and villi within 1 hour. PrP-positive cells accumulated in the subfollicle region of Peyer's patches a few hours thereafter. PrP-positive cells spread toward the mesenteric lymph nodes and spleen after the accumulation of PrPs in the Peyer's patches. The number of PrP molecules in the mesenteric lymph nodes and spleen peaked at 2 days and 6 days after inoculation, respectively. The epitheliocytes in the follicle-associated epithelium incorporating PrPs were annexin V-positive microfold cells and PrP-positive cells in Peyer's patches and spleen were CD11b-positive and CD14-positive macrophages. Additionally, PrP-positive cells in Peyer's patches and spleen were detected in the vicinity of peripheral nerve fibers in the early stages of infection. These results indicate that orally delivered PrPs were incorporated by microfold cells promptly after challenge and that macrophages might act as a transporter of incorporated PrPs from the Peyer's patches to other lymphoid tissues and the peripheral nervous system.

Indexed as

Administration, OralAnimalsBrainImmunohistochemistryIntestinal MucosaIntestine, SmallLymph NodesMacrophagesMaleMesenteryMiceMice, KnockoutPeyer's PatchesPrion DiseasesPrionsSpleenPrions

Identifiers

PMID21763679
PMCPMC3157171
OpenAlexW2110554208

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.