Evidence map›Paper›PMID 24057177›Full record

ArticleCell stress & chaperones2014

Elevated blood Hsp60, its structural similarities and cross-reactivity with thyroid molecules, and its presence on the plasma membrane of oncocytes point to the chaperonin as an immunopathogenic factor in Hashimoto's thyroiditis.

Antonella Marino Gammazza, Manfredi Rizzo, Roberto Citarrella, Francesca Rappa, Claudia Campanella, Fabio Bucchieri, Angelo Patti, Dragana Nikolic, Daniela Cabibi, Giandomenico Amico and 8 more

Open access · greenAbstract read
In one paragraph

Article in Cell stress & chaperones, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

31 citing papers in PubMed, 68 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Molecular Chaperonin HSP60: Current Understanding and Future Prospects.International journal of molecular sciences · 2024
    Review
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Observational
  11. Review
  12. Article
  13. Article
  14. Curcumin Affects HSP60 Folding Activity and Levels in Neuroblastoma Cells.International journal of molecular sciences · 2020
    Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Heat Shock Proteins as Immunomodulants.Molecules (Basel, Switzerland) · 2018
    Review
  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

18 authors at 6 institutions in 2 countries.

Antonella Marino GammazzaDepartment of Experimental Biomedicine and Clinical Neurosciences, University of Palermo, Palermo, Italy.
Manfredi Rizzo
Roberto Citarrella
Francesca Rappa
Claudia Campanella
Fabio Bucchieri
Angelo Patti
Dragana Nikolic
Daniela Cabibi
Giandomenico Amico
Pier Giulio Conaldi
Pier Luigi San Biagio
Giuseppe Montalto
Felicia Farina
Giovanni Zummo
Everly Conway de Macario
Alberto J L Macario
Francesco Cappello
University of Palermo · ITIstituto Euro Mediterraneo di Scienza e Tecnologia · ITIstituto Mediterraneo per i Trapianti e Terapie ad Alta Specializzazione · ITColumbus Center · USNational Research Council · ITUniversity of Maryland, Baltimore · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The role Hsp60 might play in various inflammatory and autoimmune diseases is under investigation, but little information exists pertaining to Hashimoto's thyroiditis (HT). With the aim to fill this gap, in the present work, we directed our attention to Hsp60 participation in HT pathogenesis. We found Hsp60 levels increased in the blood of HT patients compared to controls. The chaperonin was immunolocalized in thyroid tissue specimens from patients with HT, both in thyrocytes and oncocytes (Hurthle cells) with higher levels compared to controls (goiter). In oncocytes, we found Hsp60 not only in the cytoplasm but also on the plasma membrane, as shown by double immunofluorescence performed on fine needle aspiration cytology. By bioinformatics, we found regions in the Hsp60 molecule with remarkable structural similarity with the thyroglobulin (TG) and thyroid peroxidase (TPO) molecules, which supports the notion that autoantibodies against TG and TPO are likely to recognize Hsp60 on the plasma membrane of oncocytes. This was also supported by data obtained by ELISA, showing that anti-TG and anti-TPO antibodies cross-react with human recombinant Hsp60. Antibody-antigen (Hsp60) reaction on the cell surface could very well mediate thyroid cell damage and destruction, perpetuating inflammation. Experiments with recombinant Hsp60 did not show stimulation of cytokine production by peripheral blood mononuclear cells from HT patients. All together, these results led us to hypothesize that Hsp60 may be an active player in HT pathogenesis via an antibody-mediated immune mechanism.

Indexed as

AdultAmino Acid SequenceAutoantibodiesCell MembraneChaperonin 60Computational BiologyCross ReactionsEnzyme-Linked Immunosorbent AssayFemaleGoiterHashimoto DiseaseHumansImmunohistochemistryIntegrinsIodide PeroxidaseLeukocytes, Mononuclearanti-thyroglobulinAutoantibodiesChaperonin 60HSPD1 protein, humanIntegrinsIodide PeroxidaseMitochondrial ProteinsThyroglobulin

Identifiers

PMID24057177
PMCPMC3982029
OpenAlexW2019185580

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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.