Evidence map›Paper›PMID 24797019›Full record

ArticleOncotarget2014

Exogenously delivered heat shock protein 70 displaces its endogenous analogue and sensitizes cancer cells to lymphocytes-mediated cytotoxicity.

Maxim A Shevtsov, Elena Y Komarova, Darya A Meshalkina, Natalia V Bychkova, Nikolai D Aksenov, Sergey V Abkin, Boris A Margulis, Irina V Guzhova

Open access · diamondAbstract read
In one paragraph

Article in Oncotarget, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.8field-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

28 citing papers in PubMed, 50 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Autocrine regulation of tumor cell repopulation by Hsp70-HMGB1 alarmin complex.Journal of experimental & clinical cancer research : CR · 2023
    Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Review
  12. Review
  13. Article
  14. Article
  15. Membrane heat shock protein 70: a theranostic target for cancer therapy.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018
    Review
  16. Article
  17. Alarmins and immunity.Immunological reviews · 2017
    Review
  18. Review
  19. Article
  20. HSP70-based anti-cancer immunotherapy.Human vaccines & immunotherapeutics · 2016
    Article
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

8 authors at 2 institutions in 1 country.

Maxim A ShevtsovInstitute of Cytology of Russian Academy of Sciences, St. Petersburg, Russia.
Elena Y Komarova
Darya A Meshalkina
Natalia V Bychkova
Nikolai D Aksenov
Sergey V Abkin
Boris A Margulis
Irina V Guzhova
Institute of Cytology · RUMinistry of Emergency Situations · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Hsp70 chaperone is known to stimulate anti-tumour immunity in a variety of cancer models. Here we demonstrated that the addition of purified recombinant Hsp70 to the culture medium facilitated cancer cell cytolysis by lymphocytes. Importantly, exogenous Hsp70 triggered secretion of the intracellular Hsp70 to a cell surface and extracellular milieu, which played a role in cytolysis because down-regulation of the endogenous Hsp70 reduced both its presence at the cell surface and the lymphocyte-mediated cytolysis. Inhibitors that target both the ATPase and the peptide-binding domains of Hsp70 molecule potently decreased its anti-tumor effect. Using a variety of cell transport markers and inhibitors, we showed that the exchange of exogenous and intracellular Hsp70 is supported by classical and non-classical transport pathways, with a particular role of lipid rafts in the chaperone's intracellular transport. In conclusion, exogenous Hsp70 can eject endogenous Hsp70, thus exerting anticancer activity.

Indexed as

AnimalsBiological TransportCell Line, TumorCytotoxicity, ImmunologicFlow CytometryHSP70 Heat-Shock ProteinsHumansMembrane MicrodomainsMicroscopy, ConfocalNeoplasmsRatsHSP70 Heat-Shock Proteins

Identifiers

PMID24797019
PMCPMC4102795
OpenAlexW1543431526

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.