Evidence map›Paper›PMID 25418321›Full record

ArticleJournal of lipid research2015

Direct interaction, instrumental for signaling processes, between LacCer and Lyn in the lipid rafts of neutrophil-like cells.

Elena Chiricozzi, Maria Grazia Ciampa, Giuseppina Brasile, Federica Compostella, Alessandro Prinetti, Hitoshi Nakayama, Roudy C Ekyalongo, Kazuhisa Iwabuchi, Sandro Sonnino, Laura Mauri

Open access · hybridAbstract read
In one paragraph

Article in Journal of lipid research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.7field-weighted citation impact, top 18% 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

26 citing papers in PubMed, 54 citations in OpenAlex.

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  13. Glycosphingolipids.Advances in experimental medicine and biology · 2021
    Article
  14. Review
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  19. Review
  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

10 authors at 2 institutions in 2 countries.

Elena ChiricozziDepartment of Medical Biotechnology and Translational Medicine, University of Milan, Milano, Italy.
Maria Grazia CiampaDepartment of Medical Biotechnology and Translational Medicine, University of Milan, Milano, Italy.
Giuseppina BrasileDepartment of Medical Biotechnology and Translational Medicine, University of Milan, Milano, Italy.
Federica CompostellaDepartment of Medical Biotechnology and Translational Medicine, University of Milan, Milano, Italy.
Alessandro PrinettiDepartment of Medical Biotechnology and Translational Medicine, University of Milan, Milano, Italy.
Hitoshi NakayamaInstitute for Environmental Gender-Specific Medicine, Juntendo University Graduate School of Medicine, Chiba, Japan.
Roudy C EkyalongoInstitute for Environmental Gender-Specific Medicine, Juntendo University Graduate School of Medicine, Chiba, Japan.
Kazuhisa IwabuchiInstitute for Environmental Gender-Specific Medicine, Juntendo University Graduate School of Medicine, Chiba, Japan.
Sandro SonninoDepartment of Medical Biotechnology and Translational Medicine, University of Milan, Milano, Italy.
Laura MauriDepartment of Medical Biotechnology and Translational Medicine, University of Milan, Milano, Italy.
University of Milan · ITJuntendo University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lactosylceramide [LacCer; β-Gal-(1-4)-β-Glc-(1-1)-Cer] has been shown to contain very long fatty acids that specifically modulate neutrophil properties. The interactions between LacCer and proteins and their role in cell signaling processes were assessed by synthesizing two molecular species of azide-photoactivable tritium-labeled LacCer having acyl chains of different lengths. The lengths of the two acyl chains corresponded to those of a short/medium and very long fatty acid, comparable to the lengths of stearic and lignoceric acids, respectively. These derivatives, designated C18-[(3)H]LacCer-(N3) and C24-[(3)H]LacCer-(N3), were incorporated into the lipid rafts of plasma membranes of neutrophilic differentiated HL-60 (D-HL-60) cells. C24-[(3)H]LacCer-(N3), but not C18-[(3)H]LacCer-(N3), induced the phosphorylation of Lyn and promoted phagocytosis. Incorporation of C24-[(3)H]LacCer-(N3) into plasma membranes, followed by illumination, resulted in the formation of several tritium-labeled LacCer-protein complexes, including the LacCer-Lyn complex, into plasma membrane lipid rafts. Administration of C18-[(3)H]LacCer-(N3) to cells, however, did not result in the formation of the LacCer-Lyn complex. These results suggest that LacCer derivatives mimic the biological properties of natural LacCer species and can be utilized as tools to study LacCer-protein interactions, and confirm a specific direct interaction between LacCer species containing very long fatty acids, and Lyn protein, associated with the cytoplasmic layer via myristic/palmitic chains.

Indexed as

Signal TransductionAnimalsAntigens, CDAzidesCell SurvivalHL-60 CellsHumansLactosylceramidesMembrane MicrodomainsNeutrophilsPhagocytosisPhosphorylationProtein Bindingsrc-Family KinasesAntigens, CDAzidesCDw17 antigenLactosylceramideslyn protein-tyrosine kinasesrc-Family KinasesC24 fatty acid chaininterdigitationlactosylceramidephotoactivable sphingolipids

Identifiers

PMID25418321
PMCPMC4274061
OpenAlexW2159487459

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.