Evidence map›Paper›PMID 11309501›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2001

Selective binding of perfringolysin O derivative to cholesterol-rich membrane microdomains (rafts).

A A Waheed, Y Shimada, H F Heijnen, M Nakamura, M Inomata, M Hayashi, S Iwashita, J W Slot, Y Ohno-Iwashita

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
5.2field-weighted citation impact, top 4% 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

58 citing papers in PubMed, 214 citations in OpenAlex.

  1. Article
  2. Article
  3. Bisphosphonate inhibitors of squalene synthase protect cells against cholesterol-dependent cytolysins.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021
    Article
  4. Function of Platelet Glycosphingolipid Microdomains/Lipid Rafts.International journal of molecular sciences · 2020
    Review
  5. Review
  6. Article
  7. Article
  8. Review
  9. Pneumolysin-damaged cells benefit from non-homogeneous toxin binding to cholesterol-rich membrane domains.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2018
    Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. GsdmD p30 elicited by caspase-11 during pyroptosis forms pores in membranes.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. 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

9 authors at 2 institutions in 1 country.

A A WaheedDepartment of Protein Biochemistry, Tokyo Metropolitan Institute of Gerontology, 35-2 Sakae-cho, Itabashi-ku, Tokyo 173-0015, Japan. awaheed@tmig.or.jp
Y Shimada
H F Heijnen
M Nakamura
M Inomata
M Hayashi
S Iwashita
J W Slot
Y Ohno-Iwashita
Tokyo Metropolitan Institute of Gerontology · JPMitsubishi Group (Japan) · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

There is increasing evidence that sphingolipid- and cholesterol-rich microdomains (rafts) exist in the plasma membrane. Specific proteins assemble in these membrane domains and play a role in signal transduction and many other cellular events. Cholesterol depletion causes disassembly of the raft-associated proteins, suggesting an essential role of cholesterol in the structural maintenance and function of rafts. However, no tool has been available for the detection and monitoring of raft cholesterol in living cells. Here we show that a protease-nicked and biotinylated derivative (BCtheta) of perfringolysin O (theta-toxin) binds selectively to cholesterol-rich microdomains of intact cells, the domains that fulfill the criteria of rafts. We fractionated the homogenates of nontreated and Triton X-100-treated platelets after incubation with BCtheta on a sucrose gradient. BCtheta was predominantly localized in the floating low-density fractions (FLDF) where cholesterol, sphingomyelin, and Src family kinases are enriched. Immunoelectron microscopy demonstrated that BCtheta binds to a subpopulation of vesicles in FLDF. Depletion of 35% cholesterol from platelets with cyclodextrin, which accompanied 76% reduction in cholesterol from FLDF, almost completely abolished BCtheta binding to FLDF. The staining patterns of BCtheta and filipin in human epidermoid carcinoma A431 cells with and without cholesterol depletion suggest that BCtheta binds to specific membrane domains on the cell surface, whereas filipin binding is indiscriminate to cell cholesterol. Furthermore, BCtheta binding does not cause any damage to cell membranes, indicating that BCtheta is a useful probe for the detection of membrane rafts in living cells.

Indexed as

beta-CyclodextrinsBacterial ToxinsBiotinylationBlood PlateletsCells, CulturedCentrifugation, Density GradientCholesterolCyclodextrinsEndopeptidasesErythrocytesFilipinHemolysin ProteinsHumansMembrane MicrodomainsMicroscopy, ImmunoelectronMolecular ProbesBacterial Toxinsbeta-CyclodextrinsbetadexCholesterolClostridium perfringens theta-toxinCyclodextrinsEndopeptidasesFilipinHemolysin ProteinsMolecular ProbesOctoxynolSphingomyelins

Identifiers

PMID11309501
PMCPMC33140
OpenAlexW2065968830

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.