Evidence map›Paper›PMID 27507972›Full record

ReviewFrontiers in immunology2016

Extracellular Release and Signaling by Heat Shock Protein 27: Role in Modifying Vascular Inflammation.

Zarah Batulan, Vivek Krishna Pulakazhi Venu, Yumei Li, Geremy Koumbadinga, Daiana Gisela Alvarez-Olmedo, Chunhua Shi, Edward R O'Brien

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in immunology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.

0numbers the graph read from it
0cells of the map it votes in
68citing papers in PubMed
8.0field-weighted citation impact, top 2% 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

68 citing papers in PubMed, 119 citations in OpenAlex.

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  14. Observational
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  17. Atheroprotective Aspects of Heat Shock Proteins.International journal of molecular sciences · 2023
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  19. Article
  20. Review

8 more citing papers are in PubMed but not listed here.

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

7 authors at 3 institutions in 2 countries.

Zarah BatulanVascular Biology Laboratory, Health Research Innovation Centre, Libin Cardiovascular Institute of Alberta, University of Calgary Cumming School of Medicine , Calgary, AB , Canada.
Vivek Krishna Pulakazhi VenuVascular Biology Laboratory, Health Research Innovation Centre, Libin Cardiovascular Institute of Alberta, University of Calgary Cumming School of Medicine , Calgary, AB , Canada.
Yumei LiVascular Biology Laboratory, Health Research Innovation Centre, Libin Cardiovascular Institute of Alberta, University of Calgary Cumming School of Medicine , Calgary, AB , Canada.
Geremy KoumbadingaVascular Biology Laboratory, Health Research Innovation Centre, Libin Cardiovascular Institute of Alberta, University of Calgary Cumming School of Medicine , Calgary, AB , Canada.
Daiana Gisela Alvarez-OlmedoOncology Laboratory, Institute for Experimental Medicine and Biology of Cuyo (IMBECU), CCT CONICET , Mendoza , Argentina.
Chunhua ShiVascular Biology Laboratory, Health Research Innovation Centre, Libin Cardiovascular Institute of Alberta, University of Calgary Cumming School of Medicine , Calgary, AB , Canada.
Edward R O'BrienVascular Biology Laboratory, Health Research Innovation Centre, Libin Cardiovascular Institute of Alberta, University of Calgary Cumming School of Medicine , Calgary, AB , Canada.
University of Calgary · CALibin Cardiovascular Institute of Alberta · CAInstituto de Medicina y Biología Experimental de Cuyo · AR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Heat shock protein 27 (HSP27) is traditionally viewed as an intracellular chaperone protein with anti-apoptotic properties. However, recent data indicate that a number of heat shock proteins, including HSP27, are also found in the extracellular space where they may signal via membrane receptors to alter gene transcription and cellular function. Therefore, there is increasing interest in better understanding how HSP27 is released from cells, its levels and composition in the extracellular space, and the cognate cell membrane receptors involved in effecting cell signaling. In this paper, the knowledge to date, as well as some emerging paradigms about the extracellular function of HSP27 is presented. Of particular interest is the role of HSP27 in attenuating atherogenesis by modifying lipid uptake and inflammation in the plaque. Moreover, the abundance of HSP27 in serum is an emerging new biomarker for ischemic events. Finally, HSP27 replacement therapy may represent a novel therapeutic opportunity for chronic inflammatory disorders, such as atherosclerosis.

Indexed as

atherosclerosiscoronary artery diseaseextracellular HSP27heat shock protein 27HSPB1inflammationnon-classical secretion

Identifiers

PMID27507972
PMCPMC4960997
OpenAlexW2482660348

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.