Evidence map›Paper›PMID 15229281›Full record

ArticleMolecular biology of the cell2004

PrP(C) association with lipid rafts in the early secretory pathway stabilizes its cellular conformation.

Daniela Sarnataro, Vincenza Campana, Simona Paladino, Mariano Stornaiuolo, Lucio Nitsch, Chiara Zurzolo

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
3.6field-weighted citation impact, top 6% 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

45 citing papers in PubMed, 130 citations in OpenAlex.

  1. Review
  2. Review
  3. Emerging roles of the cellular prion protein (PrPCellular and molecular life sciences : CMLS · 2023
    Review
  4. Article
  5. Article
  6. One Raft to Guide Them All, and in Axon Regeneration Inhibit Them.International journal of molecular sciences · 2021
    Review
  7. The Cellular Prion Protein: A Promising Therapeutic Target for Cancer.International journal of molecular sciences · 2020
    Review
  8. A New Take on Prion Protein Dynamics in Cellular Trafficking.International journal of molecular sciences · 2020
    Review
  9. Article
  10. Review
  11. Prion protein-Semisynthetic prion protein (PrP) variants with posttranslational modifications.Journal of peptide science : an official publication of the European Peptide Society · 2019
    Review
  12. Review
  13. Inflammatory mediators reduce surface PrPLaboratory investigation; a journal of technical methods and pathology · 2018
    Article
  14. Cholesterol-enriched membrane microdomains are needed for insulin signaling and proliferation in hepatic cells.American journal of physiology. Gastrointestinal and liver physiology · 2018
    Article
  15. Article
  16. Article
  17. Cytochrome P450 Organization and Function Are Modulated by Endoplasmic Reticulum Phospholipid Heterogeneity.Drug metabolism and disposition: the biological fate of chemicals · 2016
    Review
  18. Article
  19. The plasma membrane as a capacitor for energy and metabolism.American journal of physiology. Cell physiology · 2016
    Review
  20. Aggregation of MBP in chronic demyelination.Annals of clinical and translational neurology · 2015
    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

6 authors at 3 institutions in 2 countries.

Daniela SarnataroDipartimento di Biologia e Patologia Cellulare e Molecolare, Centro di Endocrinologia ed Oncologia Sperimentale del Consiglio Nazionale delle Ricerche, Università degli Studi di Napoli Federico II, 80131 Napoli, Italy.
Vincenza Campana
Simona Paladino
Mariano Stornaiuolo
Lucio Nitsch
Chiara Zurzolo
Institut Pasteur · FRInstitute for Experimental Endocrinology and Oncology · ITUniversity of Naples Federico II · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The pathological conversion of cellular prion protein (PrP(C)) into the scrapie prion protein (PrP(Sc)) isoform appears to have a central role in the pathogenesis of transmissible spongiform encephalopathies. However, the identity of the intracellular compartment where this conversion occurs is unknown. Several lines of evidence indicate that detergent-resistant membrane domains (DRMs or rafts) could be involved in this process. We have characterized the association of PrP(C) to rafts during its biosynthesis. We found that PrP(C) associates with rafts already as an immature precursor in the endoplasmic reticulum. Interestingly, compared with the mature protein, the immature diglycosylated form has a different susceptibility to cholesterol depletion vs. sphingolipid depletion, suggesting that the two forms associate with different lipid domains. We also found that cholesterol depletion, which affects raft-association of the immature protein, slows down protein maturation and leads to protein misfolding. On the contrary, sphingolipid depletion does not have any effect on the kinetics of protein maturation or on the conformation of the protein. These data indicate that the early association of PrP(C) with cholesterol-enriched rafts facilitates its correct folding and reinforce the hypothesis that cholesterol and sphingolipids have different roles in PrP metabolism.

Indexed as

AnimalsCells, CulturedCholesterolDrug StabilityEndoplasmic ReticulumMembrane MicrodomainsProtein ConformationProtein FoldingProtein Processing, Post-TranslationalPrPC ProteinsRatsSphingolipidsSubcellular FractionsCholesterolPrPC ProteinsSphingolipids

Identifiers

PMID15229281
PMCPMC515338
OpenAlexW2128872171

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.