Evidence map›Paper›PMID 20716521›Full record

ArticleThe Journal of biological chemistry2010

A major fraction of glycosphingolipids in model and cellular cholesterol-containing membranes is undetectable by their binding proteins.

Radhia Mahfoud, Adam Manis, Beth Binnington, Cameron Ackerley, Clifford A Lingwood

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

42 citing papers in PubMed, 80 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Recent Advancements in Technologies to Detect EnterohaemorrhagicJournal of microbiology and biotechnology · 2023
    Review
  6. Article
  7. Role of Globotriaosylceramide in Physiology and Pathology.Frontiers in molecular biosciences · 2022
    Review
  8. Review
  9. Chemically synthesized GbEuropean biophysics journal : EBJ · 2021
    Review
  10. Article
  11. Article
  12. Verotoxin Receptor-Based Pathology and Therapies.Frontiers in cellular and infection microbiology · 2020
    Review
  13. Synthesis of GbAngewandte Chemie (International ed. in English) · 2019
    Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Impact of GMBiophysical journal · 2017
    Review
  19. Review
  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

5 authors at 2 institutions in 2 countries.

Radhia MahfoudDivision of Molecular Structure and Function, Research Institute, The Hospital for Sick Children, Ontario M5G 1X8, Canada.
Adam Manis
Beth Binnington
Cameron Ackerley
Clifford A Lingwood
Hospital for Sick Children · CAUniversity of Toronto · CA

Funding

Canadian Institutes of Health Research MT 13747
6 · The paper itself

Abstract

Glycosphingolipids (GSLs) accumulate in cholesterol-enriched cell membrane domains and provide receptors for protein ligands. Lipid-based "aglycone" interactions can influence GSL carbohydrate epitope presentation. To evaluate this relationship, Verotoxin binding its receptor GSL, globotriaosyl ceramide (Gb(3)), was analyzed in simple GSL/cholesterol, detergent-resistant membrane vesicles by equilibrium density gradient centrifugation. Vesicles separated into two Gb(3/)cholesterol-containing populations. The lighter, minor fraction (<5% total GSL), bound VT1, VT2, IgG/IgM mAb anti-Gb(3), HIVgp120 or Bandeiraea simplicifolia lectin. Only IgM anti-Gb(3), more tolerant of carbohydrate modification, bound both vesicle fractions. Post-embedding cryo-immuno-EM confirmed these results. This appears to be a general GSL-cholesterol property, because similar receptor-inactive vesicles were separated for other GSL-protein ligand systems; cholera toxin (CTx)-GM1, HIVgp120-galactosyl ceramide/sulfatide. Inclusion of galactosyl or glucosyl ceramide (GalCer and GlcCer) rendered VT1-unreactive Gb(3)/cholesterol vesicles, VT1-reactive. We found GalCer and GlcCer bind Gb(3), suggesting GSL-GSL interaction can counter cholesterol masking of Gb(3). The similar separation of Vero cell membrane-derived vesicles into minor "binding," and major "non-binding" fractions when probed with VT1, CTx, or anti-SSEA4 (a human GSL stem cell marker), demonstrates potential physiological relevance. Cell membrane GSL masking was cholesterol- and actin-dependent. Cholesterol depletion of Vero and HeLa cells enabled differential VT1B subunit labeling of "available" and "cholesterol-masked" plasma membrane Gb(3) pools by fluorescence microscopy. Thus, the model GSL/cholesterol vesicle studies predicted two distinct membrane GSL formats, which were demonstrated within the plasma membrane of cultured cells. Cholesterol masking of most cell membrane GSLs may impinge many GSL receptor functions.

Indexed as

AnimalsCell MembraneChlorocebus aethiopsCholera ToxinCholesterolCryoelectron MicroscopyGlycosphingolipidsG(M1) GangliosideHIV Envelope Protein gp120HumansImmunoblottingMicroscopy, FluorescenceMicroscopy, ImmunoelectronProtein BindingShiga ToxinsTrihexosylceramidesCholera ToxinCholesterolganglioside GM1alphaglobotriaosylceramideGlycosphingolipidsG(M1) GangliosideHIV Envelope Protein gp120Shiga ToxinsTrihexosylceramides

Identifiers

PMID20716521
PMCPMC2975227
OpenAlexW2019502270

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.