Evidence map›Paper›PMID 3745271›Full record

ArticleThe Journal of cell biology1986

Schistosomula of Schistosoma mansoni use lysophosphatidylcholine to lyse adherent human red blood cells and immobilize red cell membrane components.

D E Golan, C S Brown, C M Cianci, S T Furlong, J P Caulfield

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1986. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

39 citing papers in PubMed, 94 citations in OpenAlex.

  1. Article
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  12. Erythrocyte membrane vesiculation: model for the molecular mechanism of protein sorting.Proceedings of the National Academy of Sciences of the United States of America · 1997
    Article
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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.

D E Golan
C S Brown
C M Cianci
S T Furlong
J P Caulfield

Funding

Molecular Interactions in Erythroid Cell MembranesR37HL032854 · NHLBI · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI GOLAN, DAVID E. · 1997 to 2006
$3.0M
Molecular Regulation of Adhesive Integrin Interactions in Erythroblastic IslandsR01HL032854 · NHLBI · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI GOLAN, DAVID E. · 1985 to 2011
$2.0M
NHLBI NIH HHS HL-32854NIAID NIH HHS AI-15311NIAID NIH HHS AI-19581
6 · The paper itself

Abstract

Human red blood cells (RBCs) adhere to and are lysed by schistosomula of Schistosoma mansoni. We have investigated the mechanism of RBC lysis by comparing the dynamic properties of transmembrane protein and lipid probes in adherent ghost membranes with those in control RBCs and in RBCs treated with various membrane perturbants. Fluorescence photobleaching recovery was used to measure the lateral mobility of two integral membrane proteins, glycophorin and band 3, and two lipid analogues, fluorescein phosphatidylethanolamine (Fl-PE) and carbocyanine dyes, in RBCs and ghosts adherent to schistosomula. Adherent ghosts manifested 95-100% immobilization of both membrane proteins and 45-55% immobilization of both lipid probes. In separate experiments, diamide-induced cross-linking of RBC cytoskeletal proteins slowed transmembrane protein diffusion by 30-40%, without affecting either transmembrane protein fractional mobility or lipid probe lateral mobility. Wheat germ agglutinin- and polylysine-induced cross-linking of glycophorin at the extracellular surface caused 80-95% immobilization of the transmembrane proteins, without affecting the fractional mobility of the lipid probe. Egg lysophosphatidylcholine (lysoPC) induced both lysis of RBCs and a concentration-dependent decrease in the lateral mobility of glycophorin, band 3, and Fl-PE in ghost membranes. At a concentration of 8.4 micrograms/ml, lysoPC caused a pattern of protein and lipid immobilization in RBC ghosts identical to that in ghosts adherent to schistosomula. Schistosomula incubated with labeled palmitate released lysoPC into the culture medium at a rate of 1.5 fmol/h per 10(3) organisms. These data suggest that lysoPC is transferred from schistosomula to adherent RBCs, causing their lysis.

Indexed as

HemolysisAnimalsCarbocyaninesCell AdhesionCross-Linking ReagentsErythrocyte MembraneHumansLysophosphatidylcholinesMembrane FluidityMembrane LipidsMembrane ProteinsSchistosoma mansoniCarbocyaninesCross-Linking ReagentsLysophosphatidylcholinesMembrane LipidsMembrane Proteins

Identifiers

PMID3745271
PMCPMC2114313
OpenAlexW2095416824

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.