Evidence map›Paper›PMID 36959387›Full record

ArticleScientific reports2023

Heat shock protein A2 is a novel extracellular vesicle-associated protein.

Damian Robert Sojka, Agata Abramowicz, Małgorzata Adamiec-Organiściok, Elżbieta Karnas, Łukasz Mielańczyk, Daria Kania, Sławomir Blamek, Ewa Telka, Dorota Scieglinska

Open access · goldFull text read
In one paragraph

Article in Scientific reports, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

21 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
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  4. Recent insights into HSP70: proteostasis and beyond.Frontiers in molecular biosciences · 2026
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  19. Exosome Mediated Cell-Cell Crosstalk in Tissue Injury and Repair.Results and problems in cell differentiation · 2024
    Review
  20. 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

9 authors at 4 institutions in 2 countries.

Damian Robert Sojka *Maria Sklodowska-Curie National Research Institute of Oncology, Gliwice Branch, Wybrzeże Armii Krajowej 15, 44-102, Gliwice, Poland.
Agata Abramowicz *Maria Sklodowska-Curie National Research Institute of Oncology, Gliwice Branch, Wybrzeże Armii Krajowej 15, 44-102, Gliwice, Poland.
Małgorzata Adamiec-OrganiściokMaria Sklodowska-Curie National Research Institute of Oncology, Gliwice Branch, Wybrzeże Armii Krajowej 15, 44-102, Gliwice, Poland.
Elżbieta KarnasDepartment of Cell Biology, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Gronostajowa 7 St., 30-387, Kraków, Poland.
Łukasz MielańczykDepartment of Histology and Cell Pathology, Faculty of Medical Sciences in Zabrze, Medical University of Silesia, Katowice, Poland.
Daria KaniaMaria Sklodowska-Curie National Research Institute of Oncology, Gliwice Branch, Wybrzeże Armii Krajowej 15, 44-102, Gliwice, Poland.
Sławomir BlamekMaria Sklodowska-Curie National Research Institute of Oncology, Gliwice Branch, Wybrzeże Armii Krajowej 15, 44-102, Gliwice, Poland.
Ewa TelkaMaria Sklodowska-Curie National Research Institute of Oncology, Gliwice Branch, Wybrzeże Armii Krajowej 15, 44-102, Gliwice, Poland.
Dorota ScieglinskaMaria Sklodowska-Curie National Research Institute of Oncology, Gliwice Branch, Wybrzeże Armii Krajowej 15, 44-102, Gliwice, Poland. dorota.scieglinska@io.gliwice.pl.
The Maria Sklodowska-Curie National Research Institute of Oncology · PLJagiellonian University · PLMedical University of Silesia · PLNational Institute of Oncology · HU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

70-kDa Heat Shock Proteins (HSPA/HSP70) are chaperones playing a central role in the proteostasis control mechanisms. Their basal expression can be highly elevated as an adaptive response to environmental and pathophysiological stress conditions. HSPA2, one of poorly characterised chaperones of the HSPA/HSP70 family, has recently emerged as epithelial cells differentiation-related factor. It is also commonly expressed in cancer cells, where its functional significance remains unclear. Previously, we have found that proteotoxic stress provokes a decrease in HSPA2 levels in cancer cells. In the present study we found that proteasome inhibition-related loss of HSPA2 from cancer cells neither is related to a block in the gene transcription nor does it relate to increased autophagy-mediated disposals of the protein. Proteotoxic stress stimulated extracellular release of HSPA2 in extracellular vesicles (EVs). Interestingly, EVs containing HSPA2 are also released by non-stressed cancer and normal cells. In human urinary EVs levels of HSPA2 were correlated with the levels of TSG101, one of the main EVs markers. We conclude that HSPA2 may constitute basic components of EVs. Nevertheless, its specific role in EVs and cell-to-cell communication requires further investigation.

Indexed as

Extracellular VesiclesNeoplasmsHeat-Shock ProteinsHSP70 Heat-Shock ProteinsHumansMolecular ChaperonesHeat-Shock ProteinsHSP70 Heat-Shock ProteinsMolecular Chaperones

Identifiers

PMID36959387
PMCPMC10036471
OpenAlexW4360613824

What Socratic holds

Textfull text, public
LicenceCC BY
measurements read52
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 Socratic graph.