Evidence map›Paper›PMID 26183779›Full record

ArticleThe Journal of biological chemistry2015

Tag7 (PGLYRP1) in Complex with Hsp70 Induces Alternative Cytotoxic Processes in Tumor Cells via TNFR1 Receptor.

Denis V Yashin, Olga K Ivanova, Natalia V Soshnikova, Anton A Sheludchenkov, Elena A Romanova, Elena A Dukhanina, Alexander G Tonevitsky, Nikolai V Gnuchev, Alexander G Gabibov, Georgii P Georgiev and 1 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. 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
3.5field-weighted citation impact, top 7% 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, 60 citations in OpenAlex.

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  16. N-Terminal Peptide of PGLYRP1/Tag7 Is a Novel Ligand for TREM-1 Receptor.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 1 institution in 1 country.

Denis V YashinFrom the Institute of Gene Biology, Russian Academy of Sciences (RAS), Vavilova 34/5, Moscow 119334.
Olga K IvanovaFrom the Institute of Gene Biology, Russian Academy of Sciences (RAS), Vavilova 34/5, Moscow 119334.
Natalia V SoshnikovaFrom the Institute of Gene Biology, Russian Academy of Sciences (RAS), Vavilova 34/5, Moscow 119334.
Anton A SheludchenkovFrom the Institute of Gene Biology, Russian Academy of Sciences (RAS), Vavilova 34/5, Moscow 119334.
Elena A RomanovaFrom the Institute of Gene Biology, Russian Academy of Sciences (RAS), Vavilova 34/5, Moscow 119334.
Elena A DukhaninaFrom the Institute of Gene Biology, Russian Academy of Sciences (RAS), Vavilova 34/5, Moscow 119334, the Engelhardt Institute of Molecular Biology, RAS, Moscow 119334.
Alexander G Tonevitskythe P.A. Hertsen Moscow Research Oncology Institute, 2nd Botkinskii p. 3, Moscow 125284, and.
Nikolai V GnuchevFrom the Institute of Gene Biology, Russian Academy of Sciences (RAS), Vavilova 34/5, Moscow 119334.
Alexander G GabibovFrom the Institute of Gene Biology, Russian Academy of Sciences (RAS), Vavilova 34/5, Moscow 119334, the Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, RAS, Mikluho-Maklaya 16/10, Moscow 117997, Russia.
Georgii P GeorgievFrom the Institute of Gene Biology, Russian Academy of Sciences (RAS), Vavilova 34/5, Moscow 119334.
Lidia P SashchenkoFrom the Institute of Gene Biology, Russian Academy of Sciences (RAS), Vavilova 34/5, Moscow 119334, sashchenko@genebiology.ru.
Institute of Gene Biology · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tag7 (also known as peptidoglycan recognition protein PGRP-S, PGLYRP1), an innate immunity protein, interacts with Hsp70 to form a stable Tag7-Hsp70 complex with cytotoxic activity against some tumor cell lines. In this study, we have analyzed the programmed cell death mechanisms that are induced when cells interact with the Tag7-Hsp70 complex, which was previously shown to be released by human lymphocytes and is cytotoxic to cancer cells. We show that this complex induces both apoptotic and necroptotic processes in the cells. Apoptosis follows the classic caspase-8 and caspase-3 activation pathway. Inhibition of apoptosis leads to a switch to the RIP1-dependent necroptosis. Both of these cytotoxic processes are initiated by the involvement of TNFR1, a receptor for TNF-α. Our results suggest that the Tag7-Hsp70 complex is a novel ligand for this receptor. One of its components, the innate immunity protein Tag7, can bind to the TNFR1 receptor, thereby inhibiting the cytotoxic actions of the Tag7-Hsp70 complex and TNF-α, an acquired immunity cytokine.

Indexed as

ApoptosisAnimalsCaspasesCell LineClone CellsCytokinesHEK293 CellsHSP70 Heat-Shock ProteinsHumansMiceNecrosisProtein BindingReceptors, Tumor Necrosis Factor, Type ITumor Necrosis Factor-alphaCaspasesCytokinesHSP70 Heat-Shock ProteinsPGLYRP1 protein, humanReceptors, Tumor Necrosis Factor, Type ITumor Necrosis Factor-alphaapoptosiscell deathcytotoxicityheat shock protein (HSP)Hsp70necroptosisRNA interference (RNAi)Tag7Tag7-Hsp70 complexTNFR1tumor necrosis factor (TNF)

Identifiers

PMID26183779
PMCPMC4571894
OpenAlexW1920587523

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.