Evidence map›Paper›PMID 25071768›Full record

ArticleFrontiers in immunology2014

Heat shock protein 70 serum levels differ significantly in patients with chronic hepatitis, liver cirrhosis, and hepatocellular carcinoma.

Mathias Gehrmann, Melchiorre Cervello, Giuseppe Montalto, Francesco Cappello, Alessandro Gulino, Clemens Knape, Hanno M Specht, Gabriele Multhoff

Abstract read
In one paragraph

Article in Frontiers in immunology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
–field-weighted citation impact
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

34 citing papers in PubMed.

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  18. Article
  19. Membrane heat shock protein 70: a theranostic target for cancer therapy.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018
    Review
  20. Extracellular cell stress (heat shock) proteins-immune responses and disease: an overview.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018
    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

8 authors.

Mathias GehrmannDepartment of Radiation Oncology, Klinikum rechts der Isar, Technische Universität München , Munich , Germany.
Melchiorre CervelloInstitute of Biomedicine and Molecular Immunology "Alberto Monroy", National Research Council , Palermo , Italy.
Giuseppe MontaltoInstitute of Biomedicine and Molecular Immunology "Alberto Monroy", National Research Council , Palermo , Italy ; Biomedical Department of Internal Medicine and Specialties, University of Palermo , Palermo , Italy.
Francesco CappelloSection of Human Anatomy, Department of Experimental Biomedicine and Clinical Neurosciences, University of Palermo , Palermo , Italy ; Euro-Mediterranean Institute of Science and Technology , Palermo , Italy.
Alessandro GulinoTumor Immunology Unit, Department of Health Science, Human Pathology Section, School of Medicine, University of Palermo , Palermo , Italy.
Clemens KnapeDepartment of Radiation Oncology, Klinikum rechts der Isar, Technische Universität München , Munich , Germany.
Hanno M SpechtDepartment of Radiation Oncology, Klinikum rechts der Isar, Technische Universität München , Munich , Germany.
Gabriele MulthoffDepartment of Radiation Oncology, Klinikum rechts der Isar, Technische Universität München , Munich , Germany ; Clinical Cooperation Group (CCG) - Innate Immunity in Tumor Biology, Helmholtz Centre Munich, German Research Centre for Environmental Health , Munich , Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Members of the heat shock protein 70 (HSP70) family play an important role in assisting protein folding, preventing protein aggregation and transport of proteins across membranes under physiological conditions. Following environmental (i.e., irradiation, chemotherapy), physiological (i.e., cell growth, differentiation), and pathophysiological (i.e., inflammation, tumorigenesis) stress, the synthesis of heat shock proteins (HSPs) is highly up-regulated, whereas protein synthesis in general is reduced. In contrast to normal cells, many tumor entities including hepatocellular carcinoma (HCC) overexpress HSP70, the major-stress-inducible member of the HSP70 family, present it on their cell surface and secrete it into the extracellular milieu. Herein, the prognostic relevance of serum HSP70 levels in patients with chronic hepatitis (CH; n = 50), liver cirrhosis (LC; n = 46), and HCC (n = 47) was analyzed. Similar to other tumor entities, HSP70 is also present on the surface of primary HCC cells. The staining intensity of intracellular HSP70 in HCC tissue is stronger compared to control and cirrhotic liver sections. HSP70 serum levels in all HCC patients were significantly higher compared to a control group without liver disease (n = 40). No significant age- and gender-related differences in HSP70 serum levels were observed in male and female healthy human volunteers (n = 86). Patients with CH (n = 50) revealed significantly higher HSP70 serum levels compared to the control group, however, these values were significantly lower than those of HCC patients (n = 47). Furthermore, a subgroup of patients with LC who subsequently developed HCC (LC-HCC, n = 13) revealed higher HSP70 serum levels than patients with LC (n = 46, p = 0.05). These data indicate that serum HSP70 levels are consecutively increased in patients with CH, LC and liver carcinomas and thus might have a prognostic value.

Indexed as

chronic hepatitisHCCinflammationliver cirrhosisprognostic biomarkerserum HSP70

Identifiers

PMID25071768
PMCPMC4076752

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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.