Evidence map›Paper›PMID 15322032›Full record

ArticleInfection and immunity2004

Involvement of raft-like plasma membrane domains of Entamoeba histolytica in pinocytosis and adhesion.

Richard C Laughlin, Glen C McGugan, Rhonda R Powell, Brenda H Welter, Lesly A Temesvari

Open access · greenAbstract read
In one paragraph

Article in Infection and immunity, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.5field-weighted citation impact, top 12% 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

33 citing papers in PubMed, 66 citations in OpenAlex.

  1. Review
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  4. Identification of Multiple Domains ofInternational journal of molecular sciences · 2022
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  6. Molecular interplays of theFrontiers in cellular and infection microbiology · 2022
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  7. Revisiting Drug Development Against the Neglected Tropical Disease, Amebiasis.Frontiers in cellular and infection microbiology · 2020
    Review
  8. Lipids inFrontiers in cellular and infection microbiology · 2020
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  13. Flow shear stress differentially regulates endothelial uptake of nanocarriers targeted to distinct epitopes of PECAM-1.Journal of controlled release : official journal of the Controlled Release Society · 2015
    Article
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  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

5 authors at 1 institution in 1 country.

Richard C LaughlinDepartment of Biological Sciences, Clemson University, 132 Long Hall, Clemson, SC 29634, USA.
Glen C McGugan
Rhonda R Powell
Brenda H Welter
Lesly A Temesvari
Clemson University · US

Funding

Role of lipid rafts and phosphoinositides in E. histolytica virulenceR01AI046414 · NIAID · CLEMSON UNIVERSITY · PI TEMESVARI, LESLY A · 2001 to 2010
$1.7M
NIAID NIH HHS R01 AI046414
6 · The paper itself

Abstract

Lipid rafts are highly ordered, cholesterol-rich, and detergent-resistant microdomains found in the plasma membrane of many eukaryotic cells. These domains play important roles in endocytosis, secretion, and adhesion in a variety of cell types. The parasitic protozoan Entamoeba histolytica, the causative agent of amoebic dysentery, was determined to have raft-like plasma membrane domains by use of fluorescent lipid analogs that specifically partition into raft and nonraft regions of the membrane. Disruption of raft-like membrane domains in Entamoeba with the cholesterol-binding agents filipin and methyl-beta-cyclodextrin resulted in the inhibition of several important virulence functions, fluid-phase pinocytosis, and adhesion to host cell monolayers. However, disruption of raft-like domains did not inhibit constitutive secretion of cysteine proteases, another important virulence function of Entamoeba. Flotation of the cold Triton X-100-insoluble portion of membranes on sucrose gradients revealed that the heavy, intermediate, and light subunits of the galactose-N-acetylgalactosamine-inhibitible lectin, an important cell surface adhesion molecule of Entamoeba, were enriched in cholesterol-rich (raft-like) fractions, whereas EhCP5, another cell surface molecule, was not enriched in these fractions. The subunits of the lectin were also observed in high-density, actin-rich fractions of the sucrose gradient. Together, these data suggest that pinocytosis and adhesion are raft-dependent functions in this pathogen. This is the first report describing the existence and physiological relevance of raft-like membrane domains in E. histolytica.

Indexed as

Cell AdhesionPinocytosisAnimalsCell MembraneCHO CellsCricetinaeEntamoeba histolyticaHumansMembrane Microdomains

Identifiers

PMID15322032
PMCPMC517461
OpenAlexW2122797441

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.