Evidence map›Paper›PMID 24817194›Full record

ArticleCell stress & chaperones2014

The oxidation of HSP70 is associated with functional impairment and lack of stimulatory capacity.

Marcelo Sartori Grunwald, André Simões Pires, Alfeu Zanotto-Filho, Juciano Gasparotto, Daniel Pens Gelain, Diogo Ribeiro Demartini, Cinthia Maria Schöler, Paulo Ivo Homem de Bittencourt, José Cláudio Fonseca Moreira

Open access · bronzeAbstract 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 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
0.6field-weighted citation impact, top 34% 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

16 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
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  4. Cellular protection from HCell stress & chaperones · 2023
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  5. Heat Shock Protein 90's Mechanistic Role in Contact Hypersensitivity.Journal of immunology (Baltimore, Md. : 1950) · 2022
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  6. Review
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  8. The association of subchronic exposure to low concentration of PMEnvironmental science and pollution research international · 2020
    Article
  9. Review
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  13. Article
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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

9 authors at 1 institution in 1 country.

Marcelo Sartori GrunwaldDepartamento de Bioquímica, Instituto de Ciências Básicas da Saúde, Universidade Federal do Rio Grande do Sul, Rua Ramiro Barcelos, 2600, Porto Alegre, Rio Grande do Sul, CEP 90035-003, Brazil, marcelo.sartori@yahoo.com.br.
André Simões Pires
Alfeu Zanotto-Filho
Juciano Gasparotto
Daniel Pens Gelain
Diogo Ribeiro Demartini
Cinthia Maria Schöler
Paulo Ivo Homem de Bittencourt
José Cláudio Fonseca Moreira
Universidade Federal do Rio Grande do Sul · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Expression of intracellular HSP70 is associated with cytoprotective effects against a wide range of stressful stimuli, such as inflammation, oxidative stress, hypoxia, endotoxins, infections, and fever. This cytoprotective effect is mainly attributed to their ability to stabilize protein structures through chaperone-like reversible interactions. HSP70 was recently detected in the extracellular medium, and its presence in serum is commonly associated with pathological situations, where it exerts modulatory effects on cells of the immune system. Previously, we have described the relationship between serum HSP70 levels, oxidant status, and clinical outcome of septic patients; the group of patients with higher prooxidant status and higher serum HSP70 had also higher mortality. To investigate the possible association between oxidized HSP70 and cytoprotection or cell death, we incubated RAW 264.7 macrophages with oxidized HSP70 and evaluated nitrite production, cell proliferation, cell viability, TNF-α release, and phagocytic activity. We also evaluated structural modifications caused by oxidation in purified HSP70. Oxidation of HSP70 altered its protein structure; besides, the modulatory effect of oxidized HSP70 on RAW264.7 cells was different from that of native HSP70. Macrophages treated with oxidized HSP70 presented lower proliferation and viability, lower phagocytic activity, and lower TNF-α release. These results indicate that oxidation of extracellular HSP70 modified its signaling properties, causing alterations on its modulatory effects on macrophage function and viability.

Indexed as

Macrophage ActivationAnimalsCell LineCell ProliferationCell SurvivalHSP70 Heat-Shock ProteinsInflammation MediatorsMacrophagesMiceNitritesOxidation-ReductionPhagocytosisProtein ConformationSignal TransductionStructure-Activity RelationshipTumor Necrosis Factor-alphaHSP70 Heat-Shock ProteinsInflammation MediatorsNitritesTumor Necrosis Factor-alpha

Identifiers

PMID24817194
PMCPMC4389853
OpenAlexW2006299228

What OpenQuestion holds

Textmetadata
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.