Evidence map›Paper›PMID 23986549›Full record

ArticleJournal of leukocyte biology2013

An essential role for Rab27a GTPase in eosinophil exocytosis.

John Dongil Kim, Lian Willetts, Sergei Ochkur, Nutan Srivastava, Rudolf Hamburg, Anooshirvan Shayeganpour, Miguel C Seabra, James J Lee, Redwan Moqbel, Paige Lacy

Open access · bronzeAbstract read
In one paragraph

Article in Journal of leukocyte biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

17 citing papers in PubMed, 32 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. The Enigma of Eosinophil Degranulation.International journal of molecular sciences · 2021
    Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. A common variant in RAB27A gene is associated with fractional exhaled nitric oxide levels in adults.Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology · 2015
    Article
  17. 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

10 authors at 4 institutions in 3 countries.

John Dongil Kim2.559 HMRC, Department of Medicine, University of Alberta, Edmonton, AB, T6G 2S2, Canada. paige.lacy@ualberta.ca.
Lian Willetts
Sergei Ochkur
Nutan Srivastava
Rudolf Hamburg
Anooshirvan Shayeganpour
Miguel C Seabra
James J Lee
Redwan Moqbel
Paige Lacy
University of Alberta · CAMayo Clinic in Arizona · USImperial College London · GBUniversity of Manitoba · CA

Funding

Canadian Institutes of Health Research
6 · The paper itself

Abstract

Eosinophil degranulation has been implicated in inflammatory processes associated with allergic asthma. Rab27a, a Rab-related GTPase, is a regulatory intracellular signaling molecule expressed in human eosinophils. We postulated that Rab27a regulates eosinophil degranulation. We investigated the role of Rab27a in eosinophil degranulation within the context of airway inflammation. Rab27a expression and localization in eosinophils were investigated by using subcellular fractionation combined with Western blot analysis, and the results were confirmed by immunofluorescence analysis of Rab27a and the granule membrane marker CD63. To determine the function of eosinophil Rab27a, we used Ashen mice, a strain of Rab27a-deficient animals. Ashen eosinophils were tested for degranulation in response to PAF and calcium ionophore by measuring released EPX activity. Airway EPX release was also determined by intratracheal injection of eosinophils into mice lacking EPX. Rab27a immunoreactivity colocalized with eosinophil crystalloid granules, as determined by subcellular fractionation and immunofluorescence analysis. PAF induced eosinophil degranulation in correlation with redistribution of Rab27a(+) structures, some of which colocalized with CD63(+) crystalloid granules at the cell membrane. Eosinophils from mice had significantly reduced EPX release compared with normal WT eosinophils, both in vitro and in vivo. In mouse models, Ashen mice demonstrated reduced EPX release in BAL fluid. These findings suggest that Rab27a has a key role in eosinophil degranulation. Furthermore, these findings have implications for Rab27a-dependent eosinophil degranulation in airway inflammation.

Indexed as

AnimalsAsthmaCell DegranulationDisease Models, AnimalEosinophilsFemaleGene Expression Regulation, EnzymologicHL-60 CellsHumansMaleMiceMice, Knockoutrab27 GTP-Binding Proteinsrab GTP-Binding ProteinsTetraspanin 30CD63 protein, humanCd63 protein, mouseRAB27A protein, humanRab27a protein, mouserab27 GTP-Binding Proteinsrab GTP-Binding ProteinsTetraspanin 30allergic asthmaAshen micedegranulationhE2 transgenic miceIL-5 transgenic micesubcellular fractionation

Identifiers

PMID23986549
PMCPMC3828600
OpenAlexW2166763897

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.