Evidence map›Paper›PMID 15633295›Full record

ArticleCell stress & chaperones2004

Heat shock treatment protects osmotic stress-induced dysfunction of the blood-brain barrier through preservation of tight junction proteins.

Tzong-Shi Lu, Hsiang-Wen Chen, Maw-Hsiung Huang, Shu-Jung Wang, Rei-Cheng Yang

Open access · greenAbstract read
In one paragraph

Article in Cell stress & chaperones, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.7field-weighted citation impact, top 32% 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

14 citing papers in PubMed, 30 citations in OpenAlex.

  1. Review
  2. Article
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  5. Article
  6. Proteomic analysis of mouse choroid plexus cell line ECPC-4 treated with lipid A.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2016
    Article
  7. Intestinal epithelial barrier function and tight junction proteins with heat and exercise.Journal of applied physiology (Bethesda, Md. : 1985) · 2016
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. 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

5 authors at 1 institution in 1 country.

Tzong-Shi LuDepartment of Physiology, Graduate Institute of Medicine, Kaohsiung Medical University, Kaohsiung City 807, Taiwan, Republic of China.
Hsiang-Wen Chen
Maw-Hsiung Huang
Shu-Jung Wang
Rei-Cheng Yang
Kaohsiung Medical University · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The blood-brain barrier (BBB) is a specialized structure in the central nervous system (CNS), which participates in maintenance of a state of cerebrospinal fluid homeostasis. The endothelial cells of the cerebral capillaries and the tight junctions between them form the basis of the BBB. Research has shown that destruction of the BBB is associated with diseases of the CNS. However, there is little research on how the BBB might be protected. In this study, we used a high osmotic solution (1.6 M D-mannitol) to open the BBB of rats and Evans blue dye as a macromolecular marker. The effect of heat shock treatment was evaluated. The results show that increased synthesis of heat shock protein 72 (Hsp72) was induced in the heated group only. BBB permeability was significantly less in the heat shock-treated group after hyperosmotic shock. The major tight junction proteins, occludin and zonula occludens (ZO)-1, were significantly decreased after D-mannitol treatment in the nonheated group, whereas they were preserved in the heated group. The coimmunoprecipitation studies demonstrated that Hsp72 could be detected in the precipitates of brain extract interacting with anti-ZO-1 antibodies as well as those interacting with anti-occludin antibodies in the heated group. We conclude that the integrity of tight junctions could be maintained by previous heat shock treatment, which might be associated with the increased production of Hsp72.

Indexed as

AnimalsBlood-Brain BarrierDiuretics, OsmoticHeat-Shock ProteinsHot TemperatureHSP72 Heat-Shock ProteinsImmunohistochemistryMannitolMembrane ProteinsOsmotic PressureRatsRats, Sprague-DawleyTight JunctionsDiuretics, OsmoticHeat-Shock ProteinsHSP72 Heat-Shock ProteinsMannitolMembrane Proteins

Identifiers

PMID15633295
PMCPMC1065276
OpenAlexW2022777831

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.