Evidence map›Paper›PMID 24826836›Full record

ArticleJournal of lipid research2014

Endogenous sphingomyelin segregates into submicrometric domains in the living erythrocyte membrane.

Mélanie Carquin, Hélène Pollet, Maria Veiga-da-Cunha, Antoine Cominelli, Patrick Van Der Smissen, Francisca N'kuli, Hervé Emonard, Patrick Henriet, Hideaki Mizuno, Pierre J Courtoy and 1 more

Open access · hybridAbstract read
In one paragraph

Article in Journal of lipid research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

23 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
  2. Article
  3. Non-viral Gene Therapy for Melanoma Using Lysenin from Eisenia Foetida.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Article
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  7. Erythrocyte Membrane Nanomechanical Rigidity Is Decreased in Obese Patients.International journal of molecular sciences · 2022
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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

11 authors at 3 institutions in 2 countries.

Mélanie CarquinCELL Unit, de Duve Institute and Université catholique de Louvain, 1200 Brussels, Belgium.
Hélène PolletCELL Unit, de Duve Institute and Université catholique de Louvain, 1200 Brussels, Belgium.
Maria Veiga-da-CunhaLaboratory of Physiological Chemistry, de Duve Institute and Université catholique de Louvain, 1200 Brussels, Belgium.
Antoine CominelliCELL Unit, de Duve Institute and Université catholique de Louvain, 1200 Brussels, Belgium.
Patrick Van Der SmissenCELL Unit, de Duve Institute and Université catholique de Louvain, 1200 Brussels, Belgium.
Francisca N'kuliCELL Unit, de Duve Institute and Université catholique de Louvain, 1200 Brussels, Belgium.
Hervé Emonard"Matrice Extracellulaire et Dynamique Cellulaire" Unit (MEDyC), CNRS UMR 7369, Université de Reims Champagne-Ardenne, Laboratoire SiRMa, 51 100 Reims, France.
Patrick HenrietCELL Unit, de Duve Institute and Université catholique de Louvain, 1200 Brussels, Belgium.
Hideaki MizunoDepartment of Chemistry, Katholieke Universiteit Leuven, 3001 Heverlee, Belgium.
Pierre J CourtoyCELL Unit, de Duve Institute and Université catholique de Louvain, 1200 Brussels, Belgium.
Donatienne TytecaCELL Unit, de Duve Institute and Université catholique de Louvain, 1200 Brussels, Belgium.
de Duve Institute · BEKU Leuven · BEUniversité de Reims Champagne-Ardenne · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We recently reported that trace insertion of exogenous fluorescent (green BODIPY) analogs of sphingomyelin (SM) into living red blood cells (RBCs), partially spread onto coverslips, labels submicrometric domains, visible by confocal microscopy. We here extend this feature to endogenous SM, upon binding of a SM-specific nontoxic (NT) fragment of the earthworm toxin, lysenin, fused to the red monomeric fluorescent protein, mCherry [construct named His-mCherry-NT-lysenin (lysenin*)]. Specificity of lysenin* binding was verified with composition-defined liposomes and by loss of (125)I-lysenin* binding to erythrocytes upon SM depletion by SMase. The (125)I-lysenin* binding isotherm indicated saturation at 3.5 × 10(6) molecules/RBC, i.e., ∼3% of SM coverage. Nonsaturating lysenin* concentration also labeled sub-micrometric domains on the plasma membrane of partially spread erythrocytes, colocalizing with inserted green BODIPY-SM, and abrogated by SMase. Lysenin*-labeled domains were stable in time and space and were regulated by temperature and cholesterol. The abundance, size, positioning, and segregation of lysenin*-labeled domains from other lipids (BODIPY-phosphatidylcholine or -glycosphingolipids) depended on membrane tension. Similar lysenin*-labeled domains were evidenced in RBCs gently suspended in 3D-gel. Taken together, these data demonstrate submicrometric compartmentation of endogenous SM at the membrane of a living cell in vitro, and suggest it may be a genuine feature of erythrocytes in vivo.

Indexed as

Erythrocyte MembraneHumansMembrane MicrodomainsSphingomyelinsToxins, BiologicallyseninSphingomyelinsToxins, BiologicalcholesterolHis-mCherry-NT-lyseninlateral membrane heterogeneitymembrane tensiontemperaturetoxinvital confocal imaging

Identifiers

PMID24826836
PMCPMC4076090
OpenAlexW2165166898

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.