Evidence map›Paper›PMID 15601934›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2004

Protease-resistant human prion protein and ferritin are cotransported across Caco-2 epithelial cells: implications for species barrier in prion uptake from the intestine.

Ravi Shankar Mishra, Subhabrata Basu, Yaping Gu, Xiu Luo, Wen-Quan Zou, Richa Mishra, Ruliang Li, Shu G Chen, Pierluigi Gambetti, Hisashi Fujioka and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

34 citing papers in PubMed, 100 citations in OpenAlex.

  1. Article
  2. Article
  3. How do PrPPathogens (Basel, Switzerland) · 2017
    Review
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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

11 authors at 1 institution in 1 country.

Ravi Shankar MishraInstitute of Pathology, Case Western Reserve University, Cleveland, Ohio 44106, USA.
Subhabrata Basu
Yaping Gu
Xiu Luo
Wen-Quan Zou
Richa Mishra
Ruliang Li
Shu G Chen
Pierluigi Gambetti
Hisashi Fujioka
Neena Singh
Case Western Reserve University · US

Funding

PrP-scrapie transport across intestinal &BBBR01NS044209 · NINDS · CASE WESTERN RESERVE UNIVERSITY · PI SINGH, NEENA · 2004 to 2007
$1.1M
MECHANISM OF CELL DEATH BY PRIONSR01NS039089 · NINDS · CASE WESTERN RESERVE UNIVERSITY · PI SINGH, NEENA · 2000 to 2004
$952k
NINDS NIH HHS NS39089NINDS NIH HHS NS44209NINDS NIH HHS R01 NS039089NINDS NIH HHS R01 NS044209
6 · The paper itself

Abstract

Foodborne transmission of bovine spongiform encephalopathy (BSE) to humans as variant Creutzfeldt-Jakob disease (CJD) has affected over 100 individuals, and probably millions of others have been exposed to BSE-contaminated food substances. Despite these obvious public health concerns, surprisingly little is known about the mechanism by which PrP-scrapie (PrP(Sc)), the most reliable surrogate marker of infection in BSE-contaminated food, crosses the human intestinal epithelial cell barrier. Here we show that digestive enzyme (DE) treatment of sporadic CJD brain homogenate generates a C-terminal fragment similar to the proteinase K-resistant PrP(Sc) core of 27-30 kDa implicated in prion disease transmission and pathogenesis. Notably, DE treatment results in a PrP(Sc)-protein complex that is avidly transcytosed in vesicular structures across an in vitro model of the human intestinal epithelial cell barrier, regardless of the amount of endogenous PrP(C) expression. Unexpectedly, PrP(Sc) is cotransported with ferritin, a prominent component of the DE-treated PrP(Sc)-protein complex. The transport of PrP(Sc)-ferritin is sensitive to low temperature, brefeldin-A, and nocodazole treatment and is inhibited by excess free ferritin, implicating a receptor- or transporter-mediated pathway. Because ferritin shares considerable homology across species, these data suggest that PrP(Sc)-associated proteins, in particular ferritin, may facilitate PrP(Sc) uptake in the intestine from distant species, leading to a carrier state in humans.

Indexed as

Intestinal AbsorptionAgedBrainCaco-2 CellsCreutzfeldt-Jakob SyndromeFemaleFerritinsHumansIntestinal MucosaMaleMiddle AgedMultiprotein ComplexesPepsin APeptide FragmentsPeptide HydrolasesProtein BindingFerritinsMultiprotein ComplexesPepsin APeptide FragmentsPeptide HydrolasesPrPC ProteinsPrPSc Proteins

Identifiers

PMID15601934
PMCPMC6730364
OpenAlexW1972644169

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.