Evidence map›Paper›PMID 28630480›Full record

ArticleScientific reports2017

Pro-invasive stimuli and the interacting protein Hsp70 favour the route of alpha-enolase to the cell surface.

Giovanni Perconti, Cristina Maranto, Daniele P Romancino, Patrizia Rubino, Salvatore Feo, Antonella Bongiovanni, Agata Giallongo

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

18 citing papers in PubMed, 26 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Moonlight functions of glycolytic enzymes in cancer.Frontiers in molecular biosciences · 2023
    Review
  10. Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Review
  16. Why Do Intravascular Schistosomes Coat Themselves in Glycolytic Enzymes?BioEssays : news and reviews in molecular, cellular and developmental biology · 2019
    Article
  17. Review
  18. When Place Matters: Shuttling of Enolase-1 Across Cellular Compartments.Frontiers in cell and developmental biology · 2019
    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

7 authors at 3 institutions in 1 country.

Giovanni PercontiInstitute of Biomedicine and Molecular Immunology "A. Monroy" (IBIM), National Research Council (CNR), Palermo, Italy.
Cristina MarantoInstitute of Biomedicine and Molecular Immunology "A. Monroy" (IBIM), National Research Council (CNR), Palermo, Italy.
Daniele P RomancinoInstitute of Biomedicine and Molecular Immunology "A. Monroy" (IBIM), National Research Council (CNR), Palermo, Italy.
Patrizia RubinoInstitute of Biomedicine and Molecular Immunology "A. Monroy" (IBIM), National Research Council (CNR), Palermo, Italy.
Salvatore FeoInstitute of Biomedicine and Molecular Immunology "A. Monroy" (IBIM), National Research Council (CNR), Palermo, Italy.
Antonella BongiovanniInstitute of Biomedicine and Molecular Immunology "A. Monroy" (IBIM), National Research Council (CNR), Palermo, Italy.
Agata GiallongoInstitute of Biomedicine and Molecular Immunology "A. Monroy" (IBIM), National Research Council (CNR), Palermo, Italy. agata.giallongo@ibim.cnr.it.
Istituto di Biomedicina e di Immunologia Molecolare Alberto Monroy · ITNational Research Council · ITUniversity of Palermo · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cell surface expression of alpha-enolase, a glycolytic enzyme displaying moonlighting activities, has been shown to contribute to the motility and invasiveness of cancer cells through the protein non-enzymatic function of binding plasminogen and enhancing plasmin formation. Although a few recent records indicate the involvement of protein partners in the localization of alpha-enolase to the plasma membrane, the cellular mechanisms underlying surface exposure remain largely elusive. Searching for novel interactors and signalling pathways, we used low-metastatic breast cancer cells, a doxorubicin-resistant counterpart and a non-tumourigenic mammary epithelial cell line. Here, we demonstrate by a combination of experimental approaches that epidermal growth factor (EGF) exposure, like lipopolysaccharide (LPS) exposure, promotes the surface expression of alpha-enolase. We also establish Heat shock protein 70 (Hsp70), a multifunctional chaperone distributed in intracellular, plasma membrane and extracellular compartments, as a novel alpha-enolase interactor and demonstrate a functional involvement of Hsp70 in the surface localization of alpha-enolase. Our results contribute to shedding light on the control of surface expression of alpha-enolase in non-tumourigenic and cancer cells and suggest novel targets to counteract the metastatic potential of tumours.

Indexed as

Cell Line, TumorCell MembraneCell MovementGene Expression Regulation, NeoplasticHSP70 Heat-Shock ProteinsHumansLipopolysaccharidesPhosphopyruvate HydrataseProtein BindingHSP70 Heat-Shock ProteinsLipopolysaccharidesPhosphopyruvate Hydratase

Identifiers

PMID28630480
PMCPMC5476664
OpenAlexW2625401386

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.