Evidence map›Paper›PMID 33544155›Full record

ReviewCellular and molecular life sciences : CMLS2021

The dark-side of the outside: how extracellular heat shock proteins promote cancer.

Laura Seclì, Federica Fusella, Lidia Avalle, Mara Brancaccio

Open access · hybridAbstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed, 1 pooled it
4.2field-weighted citation impact, top 4% 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

43 citing papers in PubMed, 1 synthesis or guideline pooled it, 64 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Development of TheranosticACS applied bio materials · 2025
    Article
  11. Review
  12. Chaperone Proteins: The Rising Players in Muscle Atrophy.Journal of cachexia, sarcopenia and muscle · 2025
    Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. HSP90 multi-functionality in cancer.Frontiers in immunology · 2024
    Review
  19. Article
  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

4 authors at 1 institution in 1 country.

Laura Seclì *Department of Molecular Biotechnology and Health Sciences, University of Torino, Turin, Italy. laura.secli@unito.it.ORCID http://orcid.org/0000-0001-7129-3355
Federica Fusella *Department of Molecular Biotechnology and Health Sciences, University of Torino, Turin, Italy.ORCID https://orcid.org/0000-0002-7252-938X
Lidia AvalleDepartment of Molecular Biotechnology and Health Sciences, University of Torino, Turin, Italy.ORCID https://orcid.org/0000-0002-5060-633X
Mara BrancaccioDepartment of Molecular Biotechnology and Health Sciences, University of Torino, Turin, Italy. mara.brancaccio@unito.it.ORCID https://orcid.org/0000-0003-2327-6846
University of Turin · IT

Funding

AIRC 24216
6 · The paper itself

Abstract

In addition to exerting several essential house-keeping activities in the cell, heat shock proteins (HSPs) are crucial players in a well-structured molecular program activated in response to stressful challenges. Among the different activities carried out by HSPs during emergency, they reach the extracellular milieu, from where they scout the surroundings, regulate extracellular protein activity and send autocrine and paracrine signals. Cancer cells permanently experience stress conditions due to their altered equilibrium and behaviour, and constantly secrete heat shock proteins as a result. Other than supporting anti-tumour immunity, extracellular heat shock proteins (eHSPs), can also exacerbate cancer cell growth and malignancy by sustaining different cancer hallmarks. eHSPs are implicated in extracellular matrix remodelling, resistance to apoptosis, promotion of cell migration and invasion, induction of epithelial to mesenchymal transition, angiogenesis and activation of stromal cells, supporting ultimately, metastasis dissemination. A broader understanding of eHSP activity and contribution to tumour development and progression is leading to new opportunities in the diagnosis and treatment of cancer.

Indexed as

ATP-Binding Cassette TransportersCell MovementEpithelial-Mesenchymal TransitionExtracellular MatrixHeat-Shock ProteinsHumansLow Density Lipoprotein Receptor-Related Protein-1NeoplasmsToll-Like ReceptorsTumor MicroenvironmentATP-Binding Cassette TransportersHeat-Shock ProteinsLow Density Lipoprotein Receptor-Related Protein-1Toll-Like ReceptorsCancer hallmarksChaperonesExtracellularHeat shock proteinsTumour microenvironment

Identifiers

PMID33544155
PMCPMC8164615
OpenAlexW3128765060

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.