Evidence map›Paper›PMID 19806026›Full record

ArticlePrion

Quantitative and qualitative analysis of cellular prion protein (PrP(C)) expression in bovine somatic tissues.

Oscar A Peralta, Willard H Eyestone

Open access · bronzeAbstract read
In one paragraph

Article in Prion. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

35 citing papers in PubMed, 55 citations in OpenAlex.

  1. Article
  2. Review
  3. PrPEnvironmental science & technology · 2026
    Article
  4. Review
  5. Review
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Prion Protein at the Leading Edge: Its Role in Cell Motility.International journal of molecular sciences · 2020
    Review
  12. Review
  13. Intrinsic toxicity of the cellular prion protein is regulated by its conserved central region.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020
    Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Physiological Functions of the Cellular Prion Protein.Frontiers in molecular biosciences · 2017
    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

2 authors at 1 institution in 1 country.

Oscar A PeraltaDepartment of Large Animal Clinical Sciences, Virginia Polytechnic Institute and State University, Blacksburg, USA.
Willard H Eyestone
Virginia Tech · US

Funding

Generation of Prion Knockout CattleR21NS045908 · NINDS · VIRGINIA POLYTECHNIC INST AND ST UNIV · PI EYESTONE, WILLARD H · 2003 to 2004
$299k
NINDS NIH HHS R21 NS045908NINDS NIH HHS R21-NS045908
6 · The paper itself

Abstract

The host encoded cellular prion protein (PrP(C)) is an N-linked glycoprotein tethered to the cell membrane by a glycophosphatidylinositol (GPI) anchor. Under certain conditions, PrP(C) can undergo conversion into a conformationally-altered isoform (PrP(Sc)) widely believed to be the pathogenic agent of transmissible spongiform encephalopathies (TSEs). Understanding the tissue-specific expression of PrP(C) is crucial considering that cells expressing high levels of PrP(C) bear a risk for conversion and accumulation of PrP(Sc). In the present study, fifteen bovine somatic tissues were analyzed for PrP(C) expression by quantitative western blot and immunohistochemistry. Quantitative western blot analysis revealed highest expression of PrP(C) in cerebellum, obex and spinal cord. Intermediate levels were detected in thymus, intestine, nerve, heart and spleen, and lower levels in lung, muscle, kidney, lymph node, skin, pancreas and liver. Immunohistochemical analysis detected intense cellular-specific PrP(C) staining in neurons, thymocytes and lymphocytes. PrP(C) was also detected in the enteric wall, pancreatic islets of langerhans, myocardium, pulmonary alveolar sacs, renal glomeruli and dermal epithelial cells. This study demonstrated the quantitatively varied, wide-spread, tissue- and cell-specific expression pattern of PrP(C) in bovine somatic tissues. The importance of this study is to lay the foundation for understanding the tissue-specific expression of PrP(C) and to consider the potential participation of more bovine tissues in the transmission of BSE infection.

Indexed as

Gene Expression RegulationAnimalsCattleEpithelial CellsGlycoproteinsImmunohistochemistryMaleNeuronsPrion DiseasesProtein ConformationProtein IsoformsPrPC ProteinsSkinTissue DistributionGlycoproteinsProtein IsoformsPrPC Proteins

Identifiers

PMID19806026
PMCPMC2802781
OpenAlexW2024351041

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.