Evidence map›Paper›PMID 26700624›Full record

ArticleOncotarget2016

The histone deacetylase inhibitor SAHA induces HSP60 nitration and its extracellular release by exosomal vesicles in human lung-derived carcinoma cells.

Claudia Campanella, Antonella D'Anneo, Antonella Marino Gammazza, Celeste Caruso Bavisotto, Rosario Barone, Sonia Emanuele, Filippa Lo Cascio, Emanuele Mocciaro, Stefano Fais, Everly Conway De Macario and 3 more

Open access · diamondAbstract read
In one paragraph

Article in Oncotarget, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

37 citing papers in PubMed, 73 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Molecular Chaperonin HSP60: Current Understanding and Future Prospects.International journal of molecular sciences · 2024
    Review
  6. Article
  7. Review
  8. Review
  9. Review
  10. Review
  11. Curcumin Affects HSP60 Folding Activity and Levels in Neuroblastoma Cells.International journal of molecular sciences · 2020
    Article
  12. Exosomes as Actively Targeted Nanocarriers for Cancer Therapy.International journal of nanomedicine · 2020
    Review
  13. Review
  14. Review
  15. Review
  16. Article
  17. Review
  18. Article
  19. Epigenetic Alterations of Heat Shock Proteins (HSPs) in Cancer.International journal of molecular sciences · 2019
    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

13 authors at 4 institutions in 2 countries.

Claudia CampanellaDepartment of Experimental Biomedicine and Clinical Neurosciences, Section of Human Anatomy "Emerico Luna", University of Palermo, Palermo, Italy.
Antonella D'AnneoDepartment of Biological, Chemical and Pharmaceutical Sciences and Technologies, Laboratory of Biochemistry, University of Palermo, Palermo, Italy.
Antonella Marino GammazzaDepartment of Experimental Biomedicine and Clinical Neurosciences, Section of Human Anatomy "Emerico Luna", University of Palermo, Palermo, Italy.
Celeste Caruso BavisottoDepartment of Experimental Biomedicine and Clinical Neurosciences, Section of Human Anatomy "Emerico Luna", University of Palermo, Palermo, Italy.
Rosario BaroneDepartment of Experimental Biomedicine and Clinical Neurosciences, Section of Human Anatomy "Emerico Luna", University of Palermo, Palermo, Italy.
Sonia EmanueleDepartment of Experimental Biomedicine and Clinical Neurosciences, Laboratory of Biochemistry, University of Palermo, Palermo, Italy.
Filippa Lo CascioDepartment of Experimental Biomedicine and Clinical Neurosciences, Section of Human Anatomy "Emerico Luna", University of Palermo, Palermo, Italy.
Emanuele MocciaroDepartment of Experimental Biomedicine and Clinical Neurosciences, Section of Human Anatomy "Emerico Luna", University of Palermo, Palermo, Italy.
Stefano FaisDepartment of Therapeutic Research and Medicine Evaluation, National Institute of Health (ISS), Rome, Italy.
Everly Conway De MacarioDepartment of Microbiology and Immunology, School of Medicine, University of Maryland at Baltimore and IMET, Columbus Center, Baltimore, USA.
Alberto J L MacarioEuro-Mediterranean Institute of Science and Technology, Palermo, Italy.
Francesco CappelloDepartment of Experimental Biomedicine and Clinical Neurosciences, Section of Human Anatomy "Emerico Luna", University of Palermo, Palermo, Italy.
Marianna LauricellaDepartment of Experimental Biomedicine and Clinical Neurosciences, Laboratory of Biochemistry, University of Palermo, Palermo, Italy.
Istituto Euro Mediterraneo di Scienza e Tecnologia · ITUniversity of Palermo · ITColumbus Center · USIstituto Superiore di Sanità · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

HSP60 undergoes changes in quantity and distribution in some types of tumors suggesting a participation of the chaperonin in the mechanism of transformation and cancer progression. Suberoylanilide hydroxamic acid (SAHA), a member of a family of histone deacetylase inhibitors (HDACi), has anti-cancer potential but its interaction, if any, with HSP60 has not been elucidated. We investigated the effects of SAHA in a human lung-derived carcinoma cell line (H292). We analysed cell viability and cycle; oxidative stress markers; mitochondrial integrity; HSP60 protein and mRNA levels; and HSP60 post-translational modifications, and its secretion. We found that SAHA is cytotoxic for H292 cells, interrupting the cycle at the G2/M phase, which is followed by death; cytotoxicity is associated with oxidative stress, mitochondrial damage, and diminution of intracellular levels of HSP60; HSP60 undergoes a post-translational modification and becomes nitrated; and nitrated HSP60 is exported via exosomes. We propose that SAHA causes ROS overproduction and mitochondrial dysfunction, which leads to HSP60 nitration and release into the intercellular space and circulation to interact with the immune system. These successive steps might constitute the mechanism of the anti-tumor action of SAHA and provide a basis to design supplementary therapeutic strategies targeting HSP60, which would be more efficacious than the compound alone.

Indexed as

Antineoplastic AgentsApoptosisCell Line, TumorCell ProliferationCell SurvivalChaperonin 60ExosomesHistone Deacetylase InhibitorsHumansHydroxamic AcidsLung NeoplasmsMitochondrial ProteinsNitrosationProtein Processing, Post-TranslationalVorinostatAntineoplastic AgentsChaperonin 60Histone Deacetylase InhibitorsHSPD1 protein, humanHydroxamic AcidsMitochondrial ProteinsVorinostatexosomeshistone deacetylase inhibitorHSP60oxidative stressSAHA

Identifiers

PMID26700624
PMCPMC5045361
OpenAlexW2222159314

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.