Evidence map›Paper›PMID 25980678›Full record

ArticleImmunology2015

Transfer of the human NKG2D ligands UL16 binding proteins (ULBP) 1-3 is related to lytic granule release and leads to ligand retransfer and killing of ULBP-recipient natural killer cells.

Sheila López-Cobo, Gema Romera-Cárdenas, Eva M García-Cuesta, Hugh T Reyburn, Mar Valés-Gómez

Open access · bronzeAbstract read
In one paragraph

Article in Immunology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.7field-weighted citation impact, top 31% 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

14 citing papers in PubMed, 19 citations in OpenAlex.

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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 at 2 institutions in 1 country.

Sheila López-CoboDepartment of Immunology and Oncology, Centro Nacional de Biotecnología, Agencia Estatal Consejo Superior de Investigaciones Científicas, Madrid, Spain.
Gema Romera-CárdenasDepartment of Immunology and Oncology, Centro Nacional de Biotecnología, Agencia Estatal Consejo Superior de Investigaciones Científicas, Madrid, Spain.
Eva M García-CuestaDepartment of Immunology and Oncology, Centro Nacional de Biotecnología, Agencia Estatal Consejo Superior de Investigaciones Científicas, Madrid, Spain.
Hugh T ReyburnDepartment of Immunology and Oncology, Centro Nacional de Biotecnología, Agencia Estatal Consejo Superior de Investigaciones Científicas, Madrid, Spain.
Mar Valés-GómezDepartment of Immunology and Oncology, Centro Nacional de Biotecnología, Agencia Estatal Consejo Superior de Investigaciones Científicas, Madrid, Spain.
Centro Nacional de Biotecnología · ESConsejo Superior de Investigaciones Científicas · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

After immune interactions, membrane fragments can be transferred between cells. This fast transfer of molecules is transient and shows selectivity for certain proteins; however, the constraints underlying acquisition of a protein are unknown. To characterize the mechanism and functional consequences of this process in natural killer (NK) cells, we have compared the transfer of different NKG2D ligands. We show that human NKG2D ligands can be acquired by NK cells with different efficiencies. The main findings are that NKG2D ligand transfer is related to immune activation and receptor-ligand interaction and that NK cells acquire these proteins during interactions with target cells that lead to degranulation. Our results further demonstrate that NK cells that have acquired NKG2D ligands can stimulate activation of autologous NK cells. Surprisingly, NK cells can also re-transfer the acquired molecule to autologous effector cells during this immune recognition that leads to their death. These data demonstrate that transfer of molecules occurs as a consequence of immune recognition and imply that this process might play a role in homeostatic tuning-down of the immune response or be used as marker of interaction.

Indexed as

AnimalsCell DegranulationCell LineCHO CellsCricetinaeCricetulusCytotoxicity, ImmunologicGlycosylphosphatidylinositolsGPI-Linked ProteinsHistocompatibility Antigens Class IHumansIntercellular Signaling Peptides and ProteinsIntracellular Signaling Peptides and ProteinsKiller Cells, NaturalProtein TransportReceptors, Natural Killer CellGlycosylphosphatidylinositolsGPI-Linked ProteinsHistocompatibility Antigens Class IIntercellular Signaling Peptides and ProteinsIntracellular Signaling Peptides and ProteinsReceptors, Natural Killer CellULBP1 protein, humanULBP2 protein, humanULBP3 protein, humanglycosyl-phosphatidyl-inositol-anchored proteinshuman natural killer cellsimmune synapseNKG2Dtrogocytosis

Identifiers

PMID25980678
PMCPMC4552502
OpenAlexW1918620986

What OpenQuestion holds

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Registered trials

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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.